Explore a selection of our essential drug information below, or:
Identification
- Summary
NADH is a nutrient used in some supplement products.
- Brand Names
- EnBrace HR, EnLyte
- Generic Name
- NADH
- DrugBank Accession Number
- DB00157
- Background
NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH, a coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). It forms NADP with the addition of a phosphate group to the 2' position of the adenosyl nucleotide through an ester linkage. (Dorland, 27th ed)
- Type
- Small Molecule
- Groups
- Approved, Nutraceutical
- Structure
Structure for NADH (DB00157)
- Weight
- Average: 665.441
Monoisotopic: 665.124771695 - Chemical Formula
- C21H29N7O14P2
- Synonyms
- 1,4-dihydronicotinamide adenine dinucleotide
- DPNH
- NAD reduced form
- Nicotinamide adenine dinucleotide (reduced)
- Nicotinamide-adenine dinucleotide, reduced
- Reduced nicotinamide adenine diphosphate
- Reduced nicotinamide-adenine dinucleotide
Pharmacology
- Indication
Some evidence suggests that NADH might be useful in treating Parkinson's disease, chronic fatigue syndrome, Alzheimer's disease and cardiovascular disease.
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Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Treatment of Macrocytic anemia •••••••••••• •••••••• ••••• Prevention of Vitamin b12 deficiency •••••••••••• •••••••• ••••• Prevention of Vitamin b12 deficiency •••••••••••• •••••••• ••••••• ••••••• ••••••• - Associated Therapies
- Contraindications & Blackbox Warnings
Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). The action of supplemental NADH is unclear. Oral NADH supplementation has been used to combat simple fatigue as well as such mysterious and energy-sapping disorders as chronic fatigue syndrome and fibromyalgia. Researchers are also studying the value of NADH supplements for improving mental function in people with Alzheimer's disease, and minimizing physical disability and relieving depression in people with Parkinson's disease. Some healthy individuals also take NADH supplements orally to improve concentration and memory capacity, as well as to increase athletic endurance. However, to date there have been no published studies to indicate that using NADH is in any way effective or safe for these purposes.
- Mechanism of action
NADH is synthesized by the body and thus is not an essential nutrient. It does require the essential nutrient nicotinamide for its synthesis, and its role in energy production is certainly an essential one. In addition to its role in the mitochondrial electron transport chain, NADH is produced in the cytosol. The mitochondrial membrane is impermeable to NADH, and this permeability barrier effectively separates the cytoplasmic from the mitochondrial NADH pools. However, cytoplasmic NADH can be used for biologic energy production. This occurs when the malate-aspartate shuttle introduces reducing equivalents from NADH in the cytosol to the electron transport chain of the mitochondria. This shuttle mainly occurs in the liver and heart.
- Absorption
Unclear how much of an administered dose is absorbed.
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
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No reports of overdose, however, high doses of NADH (10 mg a day or more) may cause jitteriness, anxiety, and insomnia.
- Pathways
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image HEPASELAMİN AMİNOASİT IV İNFÜZYON ÇÖZELTİSİ 500 ML SETLİ ŞİŞE NADH (0.45 %) + Ademetionine (0.24 %) + Adenine (0.8 %) + Ascorbic acid (0.6 %) + Aspartame (0.9 %) + Biotin (0.1 %) + Calcifediol (0.9 %) + Cysteine (0.066 %) + Lysine (0.61 %) + Methionine (0.5 %) + Phosphoric acid (0.115 %) + Thiamine (0.02 %) + Tryptophan (1.1 %) + Tyrosine (0.1 %) + Valine (0.77 %) + Vitamin A (0.84 %) Solution Intravenous OSEL İLAÇ SAN. VE TİC. A.Ş. 2003-12-31 Not applicable Turkey 
HEPASELAMİN AMİNOASİT IV İNFÜZYON ÇÖZELTİSİ 500 ML SETSİZ ŞİŞE NADH (0.45 %) + Ademetionine (0.24 %) + Adenine (0.8 %) + Ascorbic acid (0.6 %) + Aspartame (0.9 %) + Biotin (0.1 %) + Calcifediol (0.9 %) + Cysteine (0.066 %) + Lysine (0.61 %) + Methionine (0.5 %) + Phosphoric acid (0.115 %) + Thiamine (0.02 %) + Tryptophan (1.1 %) + Tyrosine (0.1 %) + Valine (0.77 %) + Vitamin A (0.84 %) Solution Intravenous OSEL İLAÇ SAN. VE TİC. A.Ş. 2003-12-31 Not applicable Turkey HEPATAMINE %8 500 ML(SETLI) NADH (0.45 %) + Ademetionine (0.24 %) + Adenine (0.8 %) + Ascorbic acid (0.6 %) + Aspartame (0.9 %) + Biotin (0.1 %) + Calcifediol (0.9 %) + Cysteine (0.066 %) + Lysine (0.61 %) + Methionine (0.5 %) + Phosphoric acid (0.115 %) + Sodium bisulfite (0.01 %) + Thiamine (0.02 %) + Tryptophan (1.1 %) + Tyrosine (0.1 %) + Valine (0.77 %) + Vitamin A (0.84 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 1990-01-16 2024-01-23 Turkey HEPATAMINE %8 500 ML(SETSIZ) NADH (0.45 %) + Ademetionine (0.24 %) + Adenine (0.8 %) + Ascorbic acid (0.6 %) + Aspartame (0.9 %) + Biotin (0.1 %) + Calcifediol (0.9 %) + Cysteine (0.066 %) + Lysine (0.61 %) + Methionine (0.5 %) + Phosphoric acid (0.115 %) + Sodium bisulfite (0.01 %) + Thiamine (0.02 %) + Tryptophan (1.1 %) + Tyrosine (0.1 %) + Valine (0.77 %) + Vitamin A (0.84 %) Solution Intravenous ECZACIBAŞI-BAXTER HASTANE ÜRÜNLERİ SAN.VE TİC. A.Ş. 1990-01-16 2024-01-23 Turkey PramLyte NADH (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Escitalopram oxalate (10 mg/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic acid (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + Magnesium ascorbate (24 mg/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Sodium citrate (3.67 mg/1) + Zinc ascorbate (1 mg/1) Kit Oral Allegis Pharmaceuticals, LLC 2015-09-11 2016-01-04 US 
- Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image BumP DHA NADH (25 ug/1) + Cobamamide (500 mg/1) + Flavin adenine dinucleotide (1 mg/1) + Flavin mononucleotide (2 mg/1) + Iron (15 mg/1) + Leucovorin (1 mg/1) + Levomefolate magnesium (1 mg/1) + Magnesium oxide (125 mg/1) + Omega-3 fatty acids (300 mg/1) + Potassium Iodide (250 ug/1) + Pyridoxal phosphate (5 mg/1) + Pyridoxine hydrochloride (20 mg/1) + Zinc glycinate (15 1/1) Capsule Oral Centurion Labs 2017-03-24 2017-04-17 US EnBrace HR NADH (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic acid (1 mg/1) + Magnesium L-threonate (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (5.23 mg/1) + Magnesium ascorbate (24 mg/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Zinc ascorbate (1 mg/1) Capsule, delayed release pellets Oral Jaymac Pharmaceuticals Llc 2011-08-12 Not applicable US Lexazin NADH (5 mg/1) + Ascorbic acid (125 mg/1) + Cholecalciferol (500 [iU]/1) + Folic acid (1 mg/1) + Mecobalamin (5 mg/1) + Pyridoxal phosphate (12.5 mg/1) + Thiamine hydrochloride (25 mg/1) + Coenzyme q10, (2z)- (50 mg/1) Capsule Oral Sterling-Knight Pharmaceuticals, LLC 2018-01-02 2018-10-01 US PaxLyte NADH (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 mg/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (025 ug/1) + Folic acid (1 mg/1) + Magnesium L-threonate (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + Magnesium ascorbate (24 mg/1) + Phosphatidyl serine (12 mg/1) + Pyridoxal phosphate (25 ug/1) + Sodium citrate (1.83 mg/1) + Zinc ascorbate (1 mg/1) Capsule Oral Jaymac Pharmaceuticals Llc 2024-08-01 Not applicable US
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as (5'->5')-dinucleotides. These are dinucleotides where the two bases are connected via a (5'->5')-phosphodiester linkage.
- Kingdom
- Organic compounds
- Super Class
- Nucleosides, nucleotides, and analogues
- Class
- (5'->5')-dinucleotides
- Sub Class
- Not Available
- Direct Parent
- (5'->5')-dinucleotides
- Alternative Parents
- Purine nucleotide sugars / Purine ribonucleoside diphosphates / Purine ribonucleoside monophosphates / Nicotinamide nucleotides / Pentose phosphates / Glycosylamines / 6-aminopurines / Monosaccharide phosphates / N-substituted nicotinamides / Organic pyrophosphates show 19 more
- Substituents
- (5'->5')-dinucleotide / 6-aminopurine / Alcohol / Alkyl phosphate / Amine / Amino acid or derivatives / Aminopyrimidine / Aromatic heteropolycyclic compound / Azacycle / Azole show 42 more
- Molecular Framework
- Aromatic heteropolycyclic compounds
- External Descriptors
- NAD, NAD(P)H (CHEBI:16908)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- 4J24DQ0916
- CAS number
- 58-68-4
- InChI Key
- BOPGDPNILDQYTO-NNYOXOHSSA-N
- InChI
- InChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
- IUPAC Name
- [({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4R,5R)-5-(3-carbamoyl-1,4-dihydropyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid
- SMILES
- NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C(N)N=CN=C23)[C@@H](O)[C@H]1O
References
- Synthesis Reference
Youichi Niimura, Michio Kozaki, Hisashi Yamagata, Miki Ikuta, Yasurou Kurusu, Hideaki Yukawa, Makiko Kukushima, Masato Terasausa, "Process for producing NADH oxidase." U.S. Patent US5416012, issued February, 1984.
US5416012- General References
- Belenky P, Bogan KL, Brenner C: NAD+ metabolism in health and disease. Trends Biochem Sci. 2007 Jan;32(1):12-9. Epub 2006 Dec 11. [Article]
- Pollak N, Dolle C, Ziegler M: The power to reduce: pyridine nucleotides--small molecules with a multitude of functions. Biochem J. 2007 Mar 1;402(2):205-18. [Article]
- Khan JA, Forouhar F, Tao X, Tong L: Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin Ther Targets. 2007 May;11(5):695-705. [Article]
- Lin SJ, Guarente L: Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol. 2003 Apr;15(2):241-6. [Article]
- Biellmann JF, Lapinte C, Haid E, Weimann G: Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry. 1979 Apr 3;18(7):1212-7. [Article]
- External Links
- Human Metabolome Database
- HMDB0001487
- KEGG Compound
- C00004
- PubChem Compound
- 439153
- PubChem Substance
- 46504879
- ChemSpider
- 388299
- 7222
- ChEBI
- 16908
- ChEMBL
- CHEMBL1234616
- ZINC
- ZINC000008215403
- Therapeutic Targets Database
- DAP001291
- PharmGKB
- PA164755085
- PDBe Ligand
- NAI
- PDRhealth
- PDRhealth Drug Page
- Wikipedia
- Nicotinamide_adenine_dinucleotide
- PDB Entries
- 1ahi / 1arz / 1c1d / 1dlj / 1e3e / 1e3i / 1ek6 / 1f17 / 1fmc / 1giq … show 412 more
- MSDS
- Download (136 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample data4 Withdrawn Treatment Menstrual Related Mood Disorder / Premenstrual Dysphoric Disorder (PMDD) / Premenstrual Syndrome (PMS) / Premenstrual tension with edema 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Spectrum Pharmaceuticals
- Dosage Forms
Form Route Strength Capsule Oral Capsule, liquid filled Oral Capsule, delayed release pellets Oral Solution Intravenous Kit Oral Tablet Oral - Prices
Unit description Cost Unit Nicotinamide adenine powder 154.53USD g DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 140.0-142.0 °C Not Available logP -5.1 Not Available - Predicted Properties
Property Value Source Water Solubility 2.95 mg/mL ALOGPS logP -1.4 ALOGPS logP -6 Chemaxon logS -2.4 ALOGPS pKa (Strongest Acidic) -7.5 Chemaxon pKa (Strongest Basic) 4.93 Chemaxon Physiological Charge -2 Chemaxon Hydrogen Acceptor Count 16 Chemaxon Hydrogen Donor Count 8 Chemaxon Polar Surface Area 317.62 Å2 Chemaxon Rotatable Bond Count 11 Chemaxon Refractivity 143 m3·mol-1 Chemaxon Polarizability 59.53 Å3 Chemaxon Number of Rings 5 Chemaxon Bioavailability 0 Chemaxon Rule of Five No Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule Yes Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption - 0.6017 Blood Brain Barrier + 0.5641 Caco-2 permeable - 0.7045 P-glycoprotein substrate Substrate 0.601 P-glycoprotein inhibitor I Non-inhibitor 0.7066 P-glycoprotein inhibitor II Non-inhibitor 0.912 Renal organic cation transporter Non-inhibitor 0.9361 CYP450 2C9 substrate Non-substrate 0.8412 CYP450 2D6 substrate Non-substrate 0.8303 CYP450 3A4 substrate Substrate 0.5242 CYP450 1A2 substrate Non-inhibitor 0.7565 CYP450 2C9 inhibitor Non-inhibitor 0.849 CYP450 2D6 inhibitor Non-inhibitor 0.8849 CYP450 2C19 inhibitor Non-inhibitor 0.8294 CYP450 3A4 inhibitor Non-inhibitor 0.8753 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.8373 Ames test Non AMES toxic 0.8146 Carcinogenicity Non-carcinogens 0.9227 Biodegradation Not ready biodegradable 0.9883 Rat acute toxicity 2.8642 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9379 hERG inhibition (predictor II) Non-inhibitor 0.5992
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 273.2848527 predictedDarkChem Lite v0.1.0 [M-H]- 271.9955527 predictedDarkChem Lite v0.1.0 [M-H]- 274.6383527 predictedDarkChem Lite v0.1.0 [M-H]- 209.5491 predictedDeepCCS 1.0 (2019) [M+H]+ 274.6828527 predictedDarkChem Lite v0.1.0 [M+H]+ 273.8931527 predictedDarkChem Lite v0.1.0 [M+H]+ 275.9093527 predictedDarkChem Lite v0.1.0 [M+H]+ 211.374 predictedDeepCCS 1.0 (2019) [M+Na]+ 274.0187527 predictedDarkChem Lite v0.1.0 [M+Na]+ 274.0605527 predictedDarkChem Lite v0.1.0 [M+Na]+ 274.8503527 predictedDarkChem Lite v0.1.0 [M+Na]+ 217.1927 predictedDeepCCS 1.0 (2019)
Targets
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Use our structured and evidence-based datasets to unlock newinsights and accelerate drug research.
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Binder
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:25118196). Essential for the catalytic activity of complex I (PubMed:25118196)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND3
- Uniprot ID
- P03897
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 3
- Molecular Weight
- 13185.87 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716)
- Specific Function
- identical protein binding
- Gene Name
- UGDH
- Uniprot ID
- O60701
- Uniprot Name
- UDP-glucose 6-dehydrogenase
- Molecular Weight
- 55023.545 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Castellani AA, De Luca G, Rindi S, Salvini R, Tira ME: Regulatory mechanisms of UDP-glucuronic acid biosynthesis in cultured human skin fibroblasts. Ital J Biochem. 1986 Sep-Oct;35(5):296-303. [Article]
- Alary J, Cravedi JP, Baradat M, Carrera G: Mechanism of cadmium-decreased glucuronidation in the rat. Biochem Pharmacol. 1992 Dec 1;44(11):2139-47. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH1A
- Uniprot ID
- P07327
- Uniprot Name
- Alcohol dehydrogenase 1A
- Molecular Weight
- 39858.37 Da
References
- Bieganowski P, Seidle HF, Wojcik M, Brenner C: Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions. J Biol Chem. 2006 Aug 11;281(32):22439-45. Epub 2006 Jun 7. [Article]
- Manriquez D, El-Sharkawy I, Flores FB, El-Yahyaoui F, Regad F, Bouzayen M, Latche A, Pech JC: Two highly divergent alcohol dehydrogenases of melon exhibit fruit ripening-specific expression and distinct biochemical characteristics. Plant Mol Biol. 2006 Jul;61(4-5):675-85. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively (PubMed:3365415). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. The polyol pathway is believed to be involved in the etiology of diabetic complications, such as diabetic neuropathy and retinopathy, induced by hyperglycemia (PubMed:12962626, PubMed:25105142, PubMed:29966615). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (PubMed:16278369). May have a more general function in the metabolism of secondary alcohols since it also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP(+) as the electron acceptor (PubMed:3365415)
- Specific Function
- (R,R)-butanediol dehydrogenase activity
- Gene Name
- SORD
- Uniprot ID
- Q00796
- Uniprot Name
- Sorbitol dehydrogenase
- Molecular Weight
- 38324.25 Da
References
- Ido Y: Pyridine nucleotide redox abnormalities in diabetes. Antioxid Redox Signal. 2007 Jul;9(7):931-42. [Article]
- Klimacek M, Hellmer H, Nidetzky B: Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-->Cys forms of yeast xylitol dehydrogenase. Biochem J. 2007 Jun 15;404(3):421-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Also catalyzes the reduction of benzoquinones (PubMed:10514444)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH4
- Uniprot ID
- P08319
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH4
- Molecular Weight
- 40221.335 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Thielen J, Ciriacy M: Biochemical basis of mitochondrial acetaldehyde dismutation in Saccharomyces cerevisiae. J Bacteriol. 1991 Nov;173(21):7012-7. [Article]
- Plapp BV, Mitchell JL, Berst KB: Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism. Chem Biol Interact. 2001 Jan 30;130-132(1-3):445-56. [Article]
- Widenius TV: Ethanol-induced inhibition of testosterone biosynthesis in vitro: lack of acetaldehyde effect. Alcohol Alcohol. 1987;22(1):17-22. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Alcohol dehydrogenase. Exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH1C
- Uniprot ID
- P00326
- Uniprot Name
- Alcohol dehydrogenase 1C
- Molecular Weight
- 39867.27 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Plapp BV, Berst KB: Specificity of human alcohol dehydrogenase 1C*2 (gamma2gamma2) for steroids and simulation of the uncompetitive inhibition of ethanol metabolism. Chem Biol Interact. 2003 Feb 1;143-144:183-93. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed:15369820, PubMed:16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed:15369820)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH1B
- Uniprot ID
- P00325
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH1B
- Molecular Weight
- 39835.17 Da
References
- Manriquez D, El-Sharkawy I, Flores FB, El-Yahyaoui F, Regad F, Bouzayen M, Latche A, Pech JC: Two highly divergent alcohol dehydrogenases of melon exhibit fruit ripening-specific expression and distinct biochemical characteristics. Plant Mol Biol. 2006 Jul;61(4-5):675-85. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid (PubMed:15369820, PubMed:16787387, PubMed:9600267). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and aldehydes and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and hexanal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:15369820, PubMed:16787387). Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation (PubMed:15369820, PubMed:16787387, PubMed:9600267)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH7
- Uniprot ID
- P40394
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH7
- Molecular Weight
- 41480.985 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Dalfo D, Marques N, Albalat R: Analysis of the NADH-dependent retinaldehyde reductase activity of amphioxus retinol dehydrogenase enzymes enhances our understanding of the evolution of the retinol dehydrogenase family. FEBS J. 2007 Jul;274(14):3739-52. Epub 2007 Jul 2. [Article]
- Suzuki Y, Ishiguro S, Tamai M: Identification and immunohistochemistry of retinol dehydrogenase from bovine retinal pigment epithelium. Biochim Biophys Acta. 1993 May 13;1163(2):201-8. [Article]
- Kim DS, Lee CB, Park YS, Ahn YH, Kim TW, Kee CS, Kang JS, Om AS: Effect of thyroid hormone on the alcohol dehydrogenase activities in rat tissues. J Korean Med Sci. 2001 Jun;16(3):313-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Has glycerol-3-phosphate dehydrogenase activity
- Specific Function
- glycerol-3-phosphate dehydrogenase (NAD+) activity
- Gene Name
- GPD1
- Uniprot ID
- P21695
- Uniprot Name
- Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic
- Molecular Weight
- 37567.4 Da
References
- Fonvielle M, Therisod H, Hemery M, Therisod M: New competitive inhibitors of cytosolic (NADH-dependent) rabbit muscle glycerophosphate dehydrogenase. Bioorg Med Chem Lett. 2007 Jan 15;17(2):410-3. Epub 2006 Oct 17. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the interconversion of L-lactate and pyruvate with nicotinamide adenine dinucleotide NAD(+) as a coenzyme (PubMed:18351441). Significantly increases the transcriptional activity of JUN, when overexpressed
- Specific Function
- L-lactate dehydrogenase activity
- Gene Name
- LDHAL6A
- Uniprot ID
- Q6ZMR3
- Uniprot Name
- L-lactate dehydrogenase A-like 6A
- Molecular Weight
- 36507.015 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed:33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity)
- Specific Function
- alcohol dehydrogenase (NAD+) activity, zinc-dependent
- Gene Name
- ADH5
- Uniprot ID
- P11766
- Uniprot Name
- Alcohol dehydrogenase class-3
- Molecular Weight
- 39723.945 Da
References
- Schirwitz K, Schmidt A, Lamzin VS: High-resolution structures of formate dehydrogenase from Candida boidinii. Protein Sci. 2007 Jun;16(6):1146-56. [Article]
- Baumchen C, Roth AH, Biedendieck R, Malten M, Follmann M, Sahm H, Bringer-Meyer S, Jahn D: D-mannitol production by resting state whole cell biotrans-formation of D-fructose by heterologous mannitol and formate dehydrogenase gene expression in Bacillus megaterium. Biotechnol J. 2007 Nov;2(11):1408-16. [Article]
- Okochi M, Nakagawa I, Kobayashi T, Hayashi S, Furusaki S, Honda H: Enhanced activity of 3alpha-hydroxysteroid dehydrogenase by addition of the co-solvent 1-butyl-3-methylimidazolium (L)-lactate in aqueous phase of biphasic systems for reductive production of steroids. J Biotechnol. 2007 Feb 1;128(2):376-82. Epub 2006 Oct 12. [Article]
- Baron R, Lioubashevski O, Katz E, Niazov T, Willner I: Logic gates and elementary computing by enzymes. J Phys Chem A. 2006 Jul 13;110(27):8548-53. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia (PubMed:1936586). Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426). Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:21329684)
- Specific Function
- aldose reductase (NADPH) activity
- Gene Name
- AKR1B1
- Uniprot ID
- P15121
- Uniprot Name
- Aldo-keto reductase family 1 member B1
- Molecular Weight
- 35853.125 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (PubMed:10600649, PubMed:12917011, PubMed:18996107, PubMed:19706438, PubMed:20077426, PubMed:25925575, PubMed:26950678, PubMed:28888424, PubMed:9553139). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (PubMed:10600649, PubMed:12917011, PubMed:25925575, PubMed:26950678, PubMed:9553139). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (PubMed:18996107, PubMed:19706438, PubMed:20077426). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids (PubMed:10600649, PubMed:12917011). Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel (PubMed:19706438, PubMed:28888424). Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (PubMed:26338420). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (PubMed:9338779). Essential for structural and functional integrity of mitochondria (PubMed:20077426)
- Specific Function
- 17-beta-hydroxysteroid dehydrogenase (NAD+) activity
- Gene Name
- HSD17B10
- Uniprot ID
- Q99714
- Uniprot Name
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Molecular Weight
- 26922.87 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- L-malate dehydrogenase activity
- Gene Name
- MDH2
- Uniprot ID
- P40926
- Uniprot Name
- Malate dehydrogenase, mitochondrial
- Molecular Weight
- 35502.935 Da
References
- Baumchen C, Roth AH, Biedendieck R, Malten M, Follmann M, Sahm H, Bringer-Meyer S, Jahn D: D-mannitol production by resting state whole cell biotrans-formation of D-fructose by heterologous mannitol and formate dehydrogenase gene expression in Bacillus megaterium. Biotechnol J. 2007 Nov;2(11):1408-16. [Article]
- Gallarta F, Sainz FJ, Saenz C: Fluorescent sensing layer for the determination of L-malic acid in wine. Anal Bioanal Chem. 2007 Mar;387(6):2297-305. Epub 2007 Jan 4. [Article]
- Markova EV, Zotova NV, Savchenko AA, Titova NM, Slepov EV, Cherdantsev DV, Konovalenko AN: [Lymphocyte metabolism in patients with acute pancreatitis with different genotypes of GSTM1 and GSTT1 genes]. Biomed Khim. 2006 May-Jun;52(3):317-26. [Article]
- Yennaco LJ, Hu Y, Holden JF: Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum. Extremophiles. 2007 Sep;11(5):741-6. Epub 2007 May 9. [Article]
- Rzem R, Vincent MF, Van Schaftingen E, Veiga-da-Cunha M: L-2-hydroxyglutaric aciduria, a defect of metabolite repair. J Inherit Metab Dis. 2007 Oct;30(5):681-9. Epub 2007 Jun 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+)
- Specific Function
- cadherin binding
- Gene Name
- LDHA
- Uniprot ID
- P00338
- Uniprot Name
- L-lactate dehydrogenase A chain
- Molecular Weight
- 36688.465 Da
References
- Semenza GL: Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1. Biochem J. 2007 Jul 1;405(1):1-9. [Article]
- Draghia AC: Histochemical and histopathological study of the gastric mucosa in the portal hypertensive gastropathy. Rom J Morphol Embryol. 2006;47(3):259-62. [Article]
- O'Brien J, Kla KM, Hopkins IB, Malecki EA, McKenna MC: Kinetic parameters and lactate dehydrogenase isozyme activities support possible lactate utilization by neurons. Neurochem Res. 2007 Apr-May;32(4-5):597-607. Epub 2006 Sep 28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate
- Specific Function
- electron transfer activity
- Gene Name
- ME2
- Uniprot ID
- P23368
- Uniprot Name
- NAD-dependent malic enzyme, mitochondrial
- Molecular Weight
- 65442.945 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Bifunctional enzyme acting on the peroxisomal fatty acid beta-oxidation pathway. Catalyzes two of the four reactions in fatty acid degradation: hydration of 2-enoyl-CoA (trans-2-enoyl-CoA) to produce (3R)-3-hydroxyacyl-CoA, and dehydrogenation of (3R)-3-hydroxyacyl-CoA to produce 3-ketoacyl-CoA (3-oxoacyl-CoA), which is further metabolized by SCPx. Can use straight-chain and branched-chain fatty acids, as well as bile acid intermediates as substrates
- Specific Function
- (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity
- Gene Name
- HSD17B4
- Uniprot ID
- P51659
- Uniprot Name
- Peroxisomal multifunctional enzyme type 2
- Molecular Weight
- 79685.715 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Haapalainen AM, Koski MK, Qin YM, Hiltunen JK, Glumoff T: Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution. Structure. 2003 Jan;11(1):87-97. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- L-lactate dehydrogenase activity
- Gene Name
- LDHAL6B
- Uniprot ID
- Q9BYZ2
- Uniprot Name
- L-lactate dehydrogenase A-like 6B
- Molecular Weight
- 41942.53 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Possible role in sperm motility
- Specific Function
- L-lactate dehydrogenase activity
- Gene Name
- LDHC
- Uniprot ID
- P07864
- Uniprot Name
- L-lactate dehydrogenase C chain
- Molecular Weight
- 36310.965 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Spielmann H, Eibs HG, Mentzel C: Rapid purification of lactate dehydrogenase X from mouse testes by two steps of affinity chromatography on oxamate-sepharose. Experientia. 1976 Aug 15;32(8):1085-6. [Article]
- Morris ID, Higgins C, Matlin SA: Inhibition of testicular LDH-X from laboratory animals and man by gossypol and its isomers. J Reprod Fertil. 1986 Jul;77(2):607-12. [Article]
- Gu Y, Davis DR, Lin YC: Developmental changes in lactate dehydrogenase-X activity in young jaundiced male rats. Arch Androl. 1989;22(2):131-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+)
- Specific Function
- identical protein binding
- Gene Name
- LDHB
- Uniprot ID
- P07195
- Uniprot Name
- L-lactate dehydrogenase B chain
- Molecular Weight
- 36638.225 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Razeto A, Kochhar S, Hottinger H, Dauter M, Wilson KS, Lamzin VS: Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus. J Mol Biol. 2002 Apr 19;318(1):109-19. [Article]
- Mdluli K, Booth MP, Brady RL, Rumsby G: A preliminary account of the properties of recombinant human Glyoxylate reductase (GRHPR), LDHA and LDHB with glyoxylate, and their potential roles in its metabolism. Biochim Biophys Acta. 2005 Dec 1;1753(2):209-16. Epub 2005 Aug 22. [Article]
- Clausen J: Lactate dehydrogenase isoenzymes of sperm cells and tests. Biochem J. 1969 Jan;111(2):207-18. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (PubMed:15060085)
- Specific Function
- 3-hydroxyacyl-CoA dehydratase activity
- Gene Name
- EHHADH
- Uniprot ID
- Q08426
- Uniprot Name
- Peroxisomal bifunctional enzyme
- Molecular Weight
- 79494.18 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial fatty acid beta-oxidation enzyme that catalyzes the third step of the beta-oxidation cycle for medium and short-chain 3-hydroxy fatty acyl-CoAs (C4 to C10) (PubMed:10231530, PubMed:11489939, PubMed:16725361). Plays a role in the control of insulin secretion by inhibiting the activation of glutamate dehydrogenase 1 (GLUD1), an enzyme that has an important role in regulating amino acid-induced insulin secretion (By similarity). Plays a role in the maintenance of normal spermatogenesis through the reduction of fatty acid accumulation in the testes (By similarity)
- Specific Function
- 3-hydroxyacyl-CoA dehydrogenase activity
- Gene Name
- HADH
- Uniprot ID
- Q16836
- Uniprot Name
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Molecular Weight
- 34293.275 Da
References
- Norman JP, Perry SW, Kasischke KA, Volsky DJ, Gelbard HA: HIV-1 trans activator of transcription protein elicits mitochondrial hyperpolarization and respiratory deficit, with dysregulation of complex IV and nicotinamide adenine dinucleotide homeostasis in cortical neurons. J Immunol. 2007 Jan 15;178(2):869-76. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidative decarboxylation of (S)-malate to pyruvate using NADP(+) as a cofactor (PubMed:7818469). Can also reverse the decarboxylation reaction, but only with significantly lower efficiency (PubMed:7818469)
- Specific Function
- malate dehydrogenase (decarboxylating) (NADP+) activity
- Gene Name
- ME3
- Uniprot ID
- Q16798
- Uniprot Name
- NADP-dependent malic enzyme, mitochondrial
- Molecular Weight
- 67067.875 Da
References
- Luo C, Wang X, Long J, Liu J: An NADH-tetrazolium-coupled sensitive assay for malate dehydrogenase in mitochondria and crude tissue homogenates. J Biochem Biophys Methods. 2006 Aug 31;68(2):101-11. Epub 2006 Apr 26. [Article]
- Wei H, Dhanaraj AL, Arora R, Rowland LJ, Fu Y, Sun L: Identification of cold acclimation-responsive Rhododendron genes for lipid metabolism, membrane transport and lignin biosynthesis: importance of moderately abundant ESTs in genomic studies. Plant Cell Environ. 2006 Apr;29(4):558-70. [Article]
- Rzem R, Vincent MF, Van Schaftingen E, Veiga-da-Cunha M: L-2-hydroxyglutaric aciduria, a defect of metabolite repair. J Inherit Metab Dis. 2007 Oct;30(5):681-9. Epub 2007 Jun 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- 3-hydroxybutyrate dehydrogenase activity
- Gene Name
- BDH1
- Uniprot ID
- Q02338
- Uniprot Name
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Molecular Weight
- 38156.77 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Tabata M, Totani M: A chemiluminescence-flow injection analysis of serum 3-hydroxybutyrate using a bioreactor consisting of 3-hydroxybutyrate dehydrogenase and NADH oxidase. Anal Biochem. 1995 Jul 20;229(1):133-8. [Article]
- Rudy B, Dubois H, Mink R, Trommer WE, McIntyre JO, Fleischer S: Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme: lecithin acts as an allosteric modulator to enhance the affinity for coenzyme. Biochemistry. 1989 Jun 27;28(13):5354-66. [Article]
- Smith CM, Plaut GW: Activities of NAD-specific and NADP-specific isocitrate dehydrogenases in rat-liver mitochondria. Studies with D-threo-alpha-methylisocitrate. Eur J Biochem. 1979 Jun;97(1):283-95. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH (PubMed:2449162, PubMed:3052244). Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation (PubMed:31538237). Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen species (ROS) (PubMed:34012073)
- Specific Function
- diiodophenylpyruvate reductase activity
- Gene Name
- MDH1
- Uniprot ID
- P40925
- Uniprot Name
- Malate dehydrogenase, cytoplasmic
- Molecular Weight
- 36425.795 Da
References
- Drew DP, Lunde C, Lahnstein J, Fincher GB: Heterologous expression of cDNAs encoding monodehydroascorbate reductases from the moss, Physcomitrella patens and characterization of the expressed enzymes. Planta. 2007 Mar;225(4):945-54. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- 3-hydroxyisobutyrate dehydrogenase activity
- Gene Name
- HIBADH
- Uniprot ID
- P31937
- Uniprot Name
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Molecular Weight
- 35328.515 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids (PubMed:16216911, PubMed:26545797, PubMed:27927697, PubMed:8075637). Favors the reduction of androstenedione to testosterone (PubMed:16216911, PubMed:26545797, PubMed:27927697). Testosterone is the key androgen driving male development and function (PubMed:8075637). Uses NADPH while the two other EDH17B enzymes use NADH (PubMed:16216911, PubMed:26545797, PubMed:8075637). Androgens such as epiandrosterone, dehydroepiandrosterone, androsterone and androstanedione are accepted as substrates and reduced at C-17 (PubMed:16216911). Can reduce 11-ketoandrostenedione as well as 11beta-hydroxyandrostenedione at C-17 to the respective testosterone forms (PubMed:16216911, PubMed:27927697)
- Specific Function
- 17-beta-hydroxysteroid dehydrogenase (NADP+) activity
- Gene Name
- HSD17B3
- Uniprot ID
- P37058
- Uniprot Name
- 17-beta-hydroxysteroid dehydrogenase type 3
- Molecular Weight
- 34515.345 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Inano H, Tamaoki B: Relationship between steroids and pyridine nucleotides in the oxido-reduction catalyzed by the 17 beta-hydroxysteroid dehydrogenase purified from the porcine testicular microsomal fraction. Eur J Biochem. 1975 May 6;53(2):319-26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is the main target of statins, a class of cholesterol-lowering drugs (PubMed:11349148, PubMed:18540668, PubMed:36745799)
- Specific Function
- coenzyme A binding
- Gene Name
- HMGCR
- Uniprot ID
- P04035
- Uniprot Name
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Molecular Weight
- 97475.155 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Huber R, Riepe MW: Improved posthypoxic recovery in vitro on treatment with drugs used for secondary stroke prevention. Neuropharmacology. 2005 Mar;48(4):558-65. [Article]
- Hedl M, Rodwell VW: Inhibition of the class II HMG-CoA reductase of Pseudomonas mevalonii. Protein Sci. 2004 Jun;13(6):1693-7. [Article]
- Li S, Wagner CA, Friesen JA, Borst DW: 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the lobster mandibular organ: regulation by the eyestalk. Gen Comp Endocrinol. 2003 Nov;134(2):147-55. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate
- Specific Function
- ADP binding
- Gene Name
- ME1
- Uniprot ID
- P48163
- Uniprot Name
- NADP-dependent malic enzyme
- Molecular Weight
- 64149.075 Da
References
- McKinlay JB, Shachar-Hill Y, Zeikus JG, Vieille C: Determining Actinobacillus succinogenes metabolic pathways and fluxes by NMR and GC-MS analyses of 13C-labeled metabolic product isotopomers. Metab Eng. 2007 Mar;9(2):177-92. Epub 2006 Nov 17. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate
- Specific Function
- electron transfer activity
- Gene Name
- PHGDH
- Uniprot ID
- O43175
- Uniprot Name
- D-3-phosphoglycerate dehydrogenase
- Molecular Weight
- 56650.03 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Grant GA: A new family of 2-hydroxyacid dehydrogenases. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1371-4. [Article]
- Goldsmith LA, O'Barr T: Serine biosynthesis in human hair follicles by the phosphorylated pathway: follicular 3-phosphoglycerate dehydrogenase. J Invest Dermatol. 1976 Jun;66(6):360-6. [Article]
- Grant GA, Hu Z, Xu XL: Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding. J Biol Chem. 2002 Oct 18;277(42):39548-53. Epub 2002 Aug 14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis (PubMed:11165030, PubMed:12574203, PubMed:12732193, PubMed:12829805, PubMed:19772289, PubMed:20659585). Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids. Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2) (PubMed:12574203, PubMed:12732193, PubMed:19772289). Converts dihydrotestosterone (DHT) to its inactive form 5a-androstane-3b,17b-diol (PubMed:12574203, PubMed:12732193, PubMed:19772289). Converts moderately progesterone to 3beta-hydroxypregn-4-ene-20-one, leading to its inactivation (PubMed:12574203, PubMed:12732193). Additionally, participates in the post-squalene cholesterol biosynthesis, as a 3-ketosteroid reductase (PubMed:11165030, PubMed:12829805, PubMed:20659585)
- Specific Function
- 3-keto sterol reductase activity
- Gene Name
- HSD17B7
- Uniprot ID
- P56937
- Uniprot Name
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Molecular Weight
- 38205.77 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers
- Specific Function
- ATP binding
- Gene Name
- IDH3G
- Uniprot ID
- P51553
- Uniprot Name
- Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
- Molecular Weight
- 42793.97 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Stein AM, Stein JH, Kirkman SK: Diphosphopyridine nucleotide specific isocitric dehydrogenase of mammalian mitochondria. I. On the roles of pyridine nucleotide transhydrogenase and the isocitric dehydrogenases in the respiration of mitochondria of normal and neoplastic tissues. Biochemistry. 1967 May;6(5):1370-9. [Article]
- SANWAL BD, ZINK MW, STACHOW CS: NICOTINAMIDE ADENINE DINUCLEOTIDE-SPECIFIC ISOCITRIC DEHYDROGENASE. A POSSIBLE REGULATORY PROTEIN. J Biol Chem. 1964 May;239:1597-603. [Article]
- Rose ZB: The stereochemistry of the nicotinamide adenine dinucleotide-specific isocitric dehydrogenase reaction. J Biol Chem. 1966 May 25;241(10):2311-3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers
- Specific Function
- electron transfer activity
- Gene Name
- IDH3B
- Uniprot ID
- O43837
- Uniprot Name
- Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
- Molecular Weight
- 42183.39 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Stein AM, Stein JH, Kirkman SK: Diphosphopyridine nucleotide specific isocitric dehydrogenase of mammalian mitochondria. I. On the roles of pyridine nucleotide transhydrogenase and the isocitric dehydrogenases in the respiration of mitochondria of normal and neoplastic tissues. Biochemistry. 1967 May;6(5):1370-9. [Article]
- SANWAL BD, ZINK MW, STACHOW CS: NICOTINAMIDE ADENINE DINUCLEOTIDE-SPECIFIC ISOCITRIC DEHYDROGENASE. A POSSIBLE REGULATORY PROTEIN. J Biol Chem. 1964 May;239:1597-603. [Article]
- Rose ZB: The stereochemistry of the nicotinamide adenine dinucleotide-specific isocitric dehydrogenase reaction. J Biol Chem. 1966 May 25;241(10):2311-3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers
- Specific Function
- isocitrate dehydrogenase (NAD+) activity
- Gene Name
- IDH3A
- Uniprot ID
- P50213
- Uniprot Name
- Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
- Molecular Weight
- 39591.365 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- PLAUT GW, SUNG SC: Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues. J Biol Chem. 1954 Mar;207(1):305-14. [Article]
- Stein AM, Stein JH, Kirkman SK: Diphosphopyridine nucleotide specific isocitric dehydrogenase of mammalian mitochondria. I. On the roles of pyridine nucleotide transhydrogenase and the isocitric dehydrogenases in the respiration of mitochondria of normal and neoplastic tissues. Biochemistry. 1967 May;6(5):1370-9. [Article]
- Rose ZB: The stereochemistry of the nicotinamide adenine dinucleotide-specific isocitric dehydrogenase reaction. J Biol Chem. 1966 May 25;241(10):2311-3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Favors the reduction of estrogens and androgens. Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2) (PubMed:8994190). Also has 20-alpha-HSD activity. Uses preferentially NADH
- Specific Function
- 17-beta-hydroxysteroid dehydrogenase (NADP+) activity
- Gene Name
- HSD17B1
- Uniprot ID
- P14061
- Uniprot Name
- 17-beta-hydroxysteroid dehydrogenase type 1
- Molecular Weight
- 34949.715 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Pineda JA, Murdock GL, Watson RJ, Warren JC: Stereospecificity of hydrogen transfer by bovine testicular 20 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem. 1989 Dec;33(6):1223-8. [Article]
- Fukuda T, Hirato K, Yanaihara T, Nakayama T: Microsomal 20 alpha-hydroxysteroid dehydrogenase activity for progesterone in human placenta. Endocrinol Jpn. 1986 Jun;33(3):361-8. [Article]
- Rimsay RL, Murphy GW, Martin CJ, Orr JC: The 20 alpha-hydroxysteroid dehydrogenase of Streptomyces hydrogenans. Eur J Biochem. 1988 Jun 1;174(2):437-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of the highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity
- Specific Function
- 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity
- Gene Name
- HSD17B2
- Uniprot ID
- P37059
- Uniprot Name
- 17-beta-hydroxysteroid dehydrogenase type 2
- Molecular Weight
- 42784.75 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Fukuda T, Hirato K, Yanaihara T, Nakayama T: Microsomal 20 alpha-hydroxysteroid dehydrogenase activity for progesterone in human placenta. Endocrinol Jpn. 1986 Jun;33(3):361-8. [Article]
- Pineda JA, Murdock GL, Watson RJ, Warren JC: Stereospecificity of hydrogen transfer by bovine testicular 20 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem. 1989 Dec;33(6):1223-8. [Article]
- Wintergalen N, Thole HH, Galla HJ, Schlegel W: Prostaglandin-E2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20 alpha-hydroxysteroid dehydrogenase activity. Eur J Biochem. 1995 Nov 15;234(1):264-70. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner (PubMed:10588954, PubMed:11675386, PubMed:9115228, PubMed:9931293). Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (PubMed:29541409, PubMed:9931293)
- Specific Function
- 11-cis-retinol dehydrogenase
- Gene Name
- RDH5
- Uniprot ID
- Q92781
- Uniprot Name
- Retinol dehydrogenase 5
- Molecular Weight
- 34978.425 Da
References
- Dalfo D, Marques N, Albalat R: Analysis of the NADH-dependent retinaldehyde reductase activity of amphioxus retinol dehydrogenase enzymes enhances our understanding of the evolution of the retinol dehydrogenase family. FEBS J. 2007 Jul;274(14):3739-52. Epub 2007 Jul 2. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes (By similarity). Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway (PubMed:12858176, PubMed:18628520, PubMed:23132696). In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway (By similarity). May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate (By similarity). The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum (PubMed:12858176, PubMed:18628520, PubMed:23132696). By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity (PubMed:18628520)
- Specific Function
- 6-phosphogluconolactonase activity
- Gene Name
- H6PD
- Uniprot ID
- O95479
- Uniprot Name
- GDH/6PGL endoplasmic bifunctional protein
- Molecular Weight
- 88891.99 Da
References
- Siu E, Won K, Park CB: Electrochemical regeneration of NADH using conductive vanadia-silica xerogels. Biotechnol Prog. 2007 Jan-Feb;23(1):293-6. [Article]
- Lu Y, Mei L: Co-expression of P450 BM3 and glucose dehydrogenase by recombinant Escherichia coli and its application in an NADPH-dependent indigo production system. J Ind Microbiol Biotechnol. 2007 Mar;34(3):247-53. Epub 2006 Dec 14. [Article]
- Takenaka M, Verbitskiy D, van der Merwe JA, Zehrmann A, Plessmann U, Urlaub H, Brennicke A: In vitro RNA editing in plant mitochondria does not require added energy. FEBS Lett. 2007 Jun 12;581(14):2743-7. Epub 2007 May 21. [Article]
- Markova EV, Zotova NV, Savchenko AA, Titova NM, Slepov EV, Cherdantsev DV, Konovalenko AN: [Lymphocyte metabolism in patients with acute pancreatitis with different genotypes of GSTM1 and GSTT1 genes]. Biomed Khim. 2006 May-Jun;52(3):317-26. [Article]
- Zhang M, Mullens C, Gorski W: Coimmobilization of dehydrogenases and their cofactors in electrochemical biosensors. Anal Chem. 2007 Mar 15;79(6):2446-50. Epub 2007 Feb 14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex that acts as a scaffold protein required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference; this enzymatic activity is not needed for the KAR function (PubMed:19571038, PubMed:25203508, PubMed:30508570). Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+) (PubMed:19571038). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (Probable) (PubMed:30508570). NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol (17beta-estradiol or E2). Has very low activity towards testosterone and dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one). Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active 17beta-estradiol (PubMed:17978863)
- Specific Function
- (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity
- Gene Name
- HSD17B8
- Uniprot ID
- Q92506
- Uniprot Name
- (3R)-3-hydroxyacyl-CoA dehydrogenase
- Molecular Weight
- 26973.56 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Liver specific enzyme that acts as an NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain (PubMed:10634139, PubMed:10998348, PubMed:11158055, PubMed:14672942, PubMed:1530633, PubMed:19218247, PubMed:7650035). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:14672942). Acts preferentially as a 3-alpha-hydroxysteroid dehydrogenase (HSD) with a subsidiary 3-beta-HSD activity (PubMed:14672942). Catalyzes efficiently the transformation of the potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT or 17beta-hydroxy-5alpha-androstan-3-one) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10998348, PubMed:11158055, PubMed:14672942). Catalyzes the reduction of estrone into 17beta-estradiol but with low efficiency (PubMed:14672942). Metabolizes a broad spectrum of natural and synthetic therapeutic steroid and plays an important role in metabolism of androgens, estrogens, progestereone and conjugated steroids (PubMed:10998348, PubMed:14672942, PubMed:19218247). Catalyzes the biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leading to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route (PubMed:2427522)
- Specific Function
- 5alpha-androstane-3beta,17beta-diol dehydrogenase activity
- Gene Name
- AKR1C4
- Uniprot ID
- P17516
- Uniprot Name
- Aldo-keto reductase family 1 member C4
- Molecular Weight
- 37066.52 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Atalla A, Breyer-Pfaff U, Maser E: Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol. Xenobiotica. 2000 Aug;30(8):755-69. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (PubMed:7763314, PubMed:7903306). Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism (PubMed:14766016). It may also have a role in the development of malignancy and the growth progression of some tumors
- Specific Function
- DNA binding
- Gene Name
- IMPDH2
- Uniprot ID
- P12268
- Uniprot Name
- Inosine-5'-monophosphate dehydrogenase 2
- Molecular Weight
- 55804.495 Da
References
- Wang J, Zeevi A, Webber S, Girnita DM, Addonizio L, Selby R, Hutchinson IV, Burckart GJ: A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity. Pharmacogenet Genomics. 2007 Apr;17(4):283-90. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Acts as a NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain and regulates the metabolism of androgens, estrogens and progesterone (PubMed:10622721, PubMed:11165022, PubMed:7650035, PubMed:9415401, PubMed:9927279). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:11165022, PubMed:14672942). Acts preferentially as a 17-ketosteroid reductase and has the highest catalytic efficiency of the AKR1C enzyme for the reduction of delta4-androstenedione to form testosterone (PubMed:20036328). Reduces prostaglandin (PG) D2 to 11beta-prostaglandin F2, progesterone to 20alpha-hydroxyprogesterone and estrone to 17beta-estradiol (PubMed:10622721, PubMed:10998348, PubMed:11165022, PubMed:15047184, PubMed:19010934, PubMed:20036328). Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10557352, PubMed:10998348, PubMed:11165022, PubMed:14672942, PubMed:7650035, PubMed:9415401). Also displays retinaldehyde reductase activity toward 9-cis-retinal (PubMed:21851338)
- Specific Function
- 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
- Gene Name
- AKR1C3
- Uniprot ID
- P42330
- Uniprot Name
- Aldo-keto reductase family 1 member C3
- Molecular Weight
- 36852.89 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Pineda JA, Murdock GL, Watson RJ, Warren JC: Stereospecificity of hydrogen transfer by bovine testicular 20 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem. 1989 Dec;33(6):1223-8. [Article]
- Pineda JA, Murdock GL, Watson RJ, Warren JC: Stereospecificity of hydrogen transfer between progesterone and cofactor by human placental estradiol-17 beta dehydrogenase. J Steroid Biochem Mol Biol. 1990 Sep;37(1):65-70. [Article]
- Nicolas JC, Boussioux AM, Boularan AM, Descomps B, Crastes de Paulet A: Bioluminescent assay of femtomole levels of estrone and estradiol. Anal Biochem. 1983 Nov;135(1):141-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites (PubMed:10837478, PubMed:16757471, PubMed:16828555, PubMed:21916491, PubMed:25586183, PubMed:8086429). Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression (PubMed:15574495, PubMed:25586183). Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation (PubMed:16757471, PubMed:22844113)
- Specific Function
- 15-hydroxyprostaglandin dehydrogenase (NAD+) activity
- Gene Name
- HPGD
- Uniprot ID
- P15428
- Uniprot Name
- 15-hydroxyprostaglandin dehydrogenase [NAD(+)]
- Molecular Weight
- 28977.105 Da
References
- Gao L, He P, Sha J, Liu C, Dai L, Hui N, Ni X: Corticotropin-releasing hormone receptor type 1 and type 2 mediate differential effects on 15-hydroxy prostaglandin dehydrogenase expression in cultured human chorion trophoblasts. Endocrinology. 2007 Aug;148(8):3645-54. Epub 2007 Apr 26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction
- Specific Function
- electron transfer activity
- Gene Name
- GFUS
- Uniprot ID
- Q13630
- Uniprot Name
- GDP-L-fucose synthase
- Molecular Weight
- 35892.46 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699)
- Specific Function
- 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity
- Gene Name
- AKR1C1
- Uniprot ID
- Q04828
- Uniprot Name
- Aldo-keto reductase family 1 member C1
- Molecular Weight
- 36788.02 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Pineda JA, Murdock GL, Watson RJ, Warren JC: Stereospecificity of hydrogen transfer by bovine testicular 20 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem. 1989 Dec;33(6):1223-8. [Article]
- Fukuda T, Hirato K, Yanaihara T, Nakayama T: Microsomal 20 alpha-hydroxysteroid dehydrogenase activity for progesterone in human placenta. Endocrinol Jpn. 1986 Jun;33(3):361-8. [Article]
- Burczynski ME, Sridhar GR, Palackal NT, Penning TM: The reactive oxygen species--and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene. J Biol Chem. 2001 Jan 26;276(4):2890-7. Epub 2000 Nov 1. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:10497248, PubMed:12460758, PubMed:14973125, PubMed:15152005, PubMed:15280030, PubMed:17593962, PubMed:21453287, PubMed:27927697, PubMed:30902677). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (PubMed:10497248, PubMed:12414862, PubMed:15152005, PubMed:21453287). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (PubMed:11481269). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (PubMed:10497248, PubMed:11481269, PubMed:12414862, PubMed:12460758). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates (PubMed:15095019, PubMed:15152005, PubMed:17593962, PubMed:21453287). Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (PubMed:17593962). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (PubMed:15095019, PubMed:15152005). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (PubMed:15095019). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (PubMed:21453287). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as a ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (PubMed:30902677)
- Specific Function
- 11-beta-hydroxysteroid dehydrogenase (NADP+) activity
- Gene Name
- HSD11B1
- Uniprot ID
- P28845
- Uniprot Name
- 11-beta-hydroxysteroid dehydrogenase 1
- Molecular Weight
- 32400.665 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Diederich S, Hanke B, Oelkers W, Bahr V: Metabolism of dexamethasone in the human kidney: nicotinamide adenine dinucleotide-dependent 11beta-reduction. J Clin Endocrinol Metab. 1997 May;82(5):1598-602. [Article]
- Hermans JJ, Steckel B, Thijssen HH, Janssen BJ, Netter KJ, Maser E: Comparison of 11 beta-hydroxysteroid dehydrogenase in spontaneously hypertensive and Wistar-Kyoto rats. Steroids. 1995 Nov;60(11):773-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids
- Specific Function
- 3-beta-hydroxy-delta5-steroid dehydrogenase (NAD+) activity
- Gene Name
- HSD3B2
- Uniprot ID
- P26439
- Uniprot Name
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Molecular Weight
- 42051.845 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Widenius TV, Orava MM, Vihko RK, Ylikahri RH, Eriksson CJ: Inhibition of testosterone biosynthesis by ethanol: multiple sites and mechanisms in dispersed Leydig cells. J Steroid Biochem. 1987 Aug;28(2):185-8. [Article]
- Fan DF, Troen P: Studies of the human testis. VII. Conversion of pregnenolone to progesterone. J Clin Endocrinol Metab. 1975 Sep;41(3):563-74. [Article]
- Thomas JL, Myers RP, Strickler RC: Analysis of coenzyme binding by human placental 3 beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5----4-ene-isomerase using 5'-[p-(fluorosulfonyl)benzoyl]adenosine, an affinity labeling cofactor analog. J Steroid Biochem Mol Biol. 1991 Oct;39(4A):471-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo-Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. Specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Also converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone (PubMed:1401999, PubMed:2139411). Expected to use NAD(+) as preferred electron donor for the 3beta-hydroxy-steroid dehydrogenase activity and NADPH for the 3-ketosteroid reductase activity (Probable)
- Specific Function
- 3-beta-hydroxy-delta5-steroid dehydrogenase (NAD+) activity
- Gene Name
- HSD3B1
- Uniprot ID
- P14060
- Uniprot Name
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Molecular Weight
- 42251.25 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Widenius TV, Orava MM, Vihko RK, Ylikahri RH, Eriksson CJ: Inhibition of testosterone biosynthesis by ethanol: multiple sites and mechanisms in dispersed Leydig cells. J Steroid Biochem. 1987 Aug;28(2):185-8. [Article]
- Thomas JL, Myers RP, Rosik LO, Strickler RC: Affinity alkylation of human placental 3 beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5----4-ene-isomerase by 2 alpha-bromoacetoxyprogesterone: evidence for separate dehydrogenase and isomerase sites on one protein. J Steroid Biochem. 1990 Jun;36(1-2):117-23. [Article]
- Ishii-Ohba H, Inano H, Tamaoki B: Testicular and adrenal 3 beta-hydroxy-5-ene-steroid dehydrogenase and 5-ene-4-ene isomerase. J Steroid Biochem. 1987;27(4-6):775-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors
- Specific Function
- DNA binding
- Gene Name
- IMPDH1
- Uniprot ID
- P20839
- Uniprot Name
- Inosine-5'-monophosphate dehydrogenase 1
- Molecular Weight
- 55405.365 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Bowne SJ, Sullivan LS, Mortimer SE, Hedstrom L, Zhu J, Spellicy CJ, Gire AI, Hughbanks-Wheaton D, Birch DG, Lewis RA, Heckenlively JR, Daiger SP: Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and leber congenital amaurosis. Invest Ophthalmol Vis Sci. 2006 Jan;47(1):34-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway (PubMed:1550553, PubMed:29915090, PubMed:30850536, PubMed:8135828). The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA (PubMed:29915090). Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids (PubMed:30850536). Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity (PubMed:29915090, PubMed:30850536, PubMed:8135828). Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity (PubMed:23152787). It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP (PubMed:23152787). Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity (PubMed:23152787)
- Specific Function
- 3-hydroxyacyl-CoA dehydratase activity
- Gene Name
- HADHA
- Uniprot ID
- P40939
- Uniprot Name
- Trifunctional enzyme subunit alpha, mitochondrial
- Molecular Weight
- 82998.97 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage
- Specific Function
- aldehyde dehydrogenase (NAD+) activity
- Gene Name
- ALDH2
- Uniprot ID
- P05091
- Uniprot Name
- Aldehyde dehydrogenase, mitochondrial
- Molecular Weight
- 56380.93 Da
References
- Quintanilla ME, Tampier L, Sapag A, Gerdtzen Z, Israel Y: Sex differences, alcohol dehydrogenase, acetaldehyde burst, and aversion to ethanol in the rat: a systems perspective. Am J Physiol Endocrinol Metab. 2007 Aug;293(2):E531-7. Epub 2007 May 8. [Article]
- Quintanilla ME, Israel Y, Sapag A, Tampier L: The UChA and UChB rat lines: metabolic and genetic differences influencing ethanol intake. Addict Biol. 2006 Sep;11(3-4):310-23. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) (PubMed:10497248, PubMed:12788846, PubMed:17314322, PubMed:22796344, PubMed:27927697, PubMed:30902677, PubMed:33387577, PubMed:7859916, PubMed:8538347). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (PubMed:10497248, PubMed:12788846, PubMed:17314322, PubMed:33387577, PubMed:7859916). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen (PubMed:22796344, PubMed:27927697). Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone (PubMed:27927697). Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro (PubMed:30902677). 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as a ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (PubMed:30902677). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (By similarity)
- Specific Function
- 11-beta-hydroxysteroid dehydrogenase (NAD+) activity
- Gene Name
- HSD11B2
- Uniprot ID
- P80365
- Uniprot Name
- 11-beta-hydroxysteroid dehydrogenase type 2
- Molecular Weight
- 44126.06 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Mercer WR, Krozowski ZS: Localization of an 11 beta hydroxysteroid dehydrogenase activity to the distal nephron. Evidence for the existence of two species of dehydrogenase in the rat kidney. Endocrinology. 1992 Jan;130(1):540-3. [Article]
- Hermans JJ, Steckel B, Thijssen HH, Janssen BJ, Netter KJ, Maser E: Comparison of 11 beta-hydroxysteroid dehydrogenase in spontaneously hypertensive and Wistar-Kyoto rats. Steroids. 1995 Nov;60(11):773-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:15929998, PubMed:17034817, PubMed:17442338, PubMed:8573067). Also specifically able to produce 17beta-hydroxy-5alpha-androstan-3-one/5alphaDHT (PubMed:10998348). May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699)
- Specific Function
- aldose reductase (NADPH) activity
- Gene Name
- AKR1C2
- Uniprot ID
- P52895
- Uniprot Name
- Aldo-keto reductase family 1 member C2
- Molecular Weight
- 36734.97 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Rizner TL, Lin HK, Peehl DM, Steckelbroeck S, Bauman DR, Penning TM: Human type 3 3alpha-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells. Endocrinology. 2003 Jul;144(7):2922-32. [Article]
- Trauger JW, Jiang A, Stearns BA, LoGrasso PV: Kinetics of allopregnanolone formation catalyzed by human 3 alpha-hydroxysteroid dehydrogenase type III (AKR1C2). Biochemistry. 2002 Nov 12;41(45):13451-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD(P)(+)-dependent oxidative decarboxylation of the C4 methyl groups of 4-alpha-carboxysterols in post-squalene cholesterol biosynthesis (By similarity). Also plays a role in the regulation of the endocytic trafficking of EGFR (By similarity)
- Specific Function
- 3-beta-hydroxy-delta5-steroid dehydrogenase (NAD+) activity
- Gene Name
- NSDHL
- Uniprot ID
- Q15738
- Uniprot Name
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Molecular Weight
- 41899.99 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Cunningham D, Swartzlander D, Liyanarachchi S, Davuluri RV, Herman GE: Changes in gene expression associated with loss of function of the NSDHL sterol dehydrogenase in mouse embryonic fibroblasts. J Lipid Res. 2005 Jun;46(6):1150-62. Epub 2005 Apr 1. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Oxidizes medium and long chain aldehydes into non-toxic fatty acids
- Specific Function
- 3-chloroallyl aldehyde dehydrogenase activity
- Gene Name
- ALDH3B2
- Uniprot ID
- P48448
- Uniprot Name
- Aldehyde dehydrogenase family 3 member B2
- Molecular Weight
- 42634.6 Da
References
Details56. Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Malonate and methylmalonate semialdehyde dehydrogenase involved in the catabolism of valine, thymine, and compounds catabolized by way of beta-alanine, including uracil and cytidine
- Specific Function
- malonate-semialdehyde dehydrogenase (acetylating) activity
- Gene Name
- ALDH6A1
- Uniprot ID
- Q02252
- Uniprot Name
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Molecular Weight
- 57839.31 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Kedishvili NY, Popov KM, Harris RA: The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase. Arch Biochem Biophys. 1991 Oct;290(1):21-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids (PubMed:1737758). Preferentially oxidizes aromatic aldehyde substrates (PubMed:1737758). Comprises about 50 percent of corneal epithelial soluble proteins (By similarity). May play a role in preventing corneal damage caused by ultraviolet light (By similarity)
- Specific Function
- 3-chloroallyl aldehyde dehydrogenase activity
- Gene Name
- ALDH3A1
- Uniprot ID
- P30838
- Uniprot Name
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Molecular Weight
- 50394.57 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Wroczynski P, Nowak M, Wierzchowski J, Szubert A, Polanski J: Activities of cytosolic aldehyde dehydrogenase isozymes in colon cancer: determination using selective, fluorimetric assays. Acta Pol Pharm. 2005 Nov-Dec;62(6):427-33. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12941160, PubMed:15623782, PubMed:17175089, PubMed:19296407, PubMed:25450233, PubMed:26373694). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (By similarity). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:12941160, PubMed:15623782, PubMed:19296407). Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (PubMed:17175089). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity)
- Specific Function
- 3-deoxyglucosone dehydrogenase activity
- Gene Name
- ALDH1A1
- Uniprot ID
- P00352
- Uniprot Name
- Aldehyde dehydrogenase 1A1
- Molecular Weight
- 54861.44 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Wroczynski P, Nowak M, Wierzchowski J, Szubert A, Polanski J: Activities of cytosolic aldehyde dehydrogenase isozymes in colon cancer: determination using selective, fluorimetric assays. Acta Pol Pharm. 2005 Nov-Dec;62(6):427-33. [Article]
- Russo J, Barnes A, Berger K, Desgrosellier J, Henderson J, Kanters A, Merkov L: 4-(N,N-dipropylamino)benzaldehyde inhibits the oxidation of all-trans retinal to all-trans retinoic acid by ALDH1A1, but not the differentiation of HL-60 promyelocytic leukemia cells exposed to all-trans retinal. BMC Pharmacol. 2002;2:4. Epub 2002 Feb 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity)
- Specific Function
- glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
- Gene Name
- GAPDHS
- Uniprot ID
- O14556
- Uniprot Name
- Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
- Molecular Weight
- 44500.835 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Maeda K, Nagata H, Nonaka A, Kataoka K, Tanaka M, Shizukuishi S: Oral streptococcal glyceraldehyde-3-phosphate dehydrogenase mediates interaction with Porphyromonas gingivalis fimbriae. Microbes Infect. 2004 Nov;6(13):1163-70. [Article]
- Graciet E, Lebreton S, Camadro JM, Gontero B: Characterization of native and recombinant A4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for confromation changes upon association with the small protein CP12. Eur J Biochem. 2003 Jan;270(1):129-36. [Article]
- Ismail SA, Park HW: Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1508-13. Epub 2005 Oct 19. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency. Catalyzes the oxidation of aldehydes arising from biogenic amines and polyamines
- Specific Function
- 4-trimethylammoniobutyraldehyde dehydrogenase activity
- Gene Name
- ALDH9A1
- Uniprot ID
- P49189
- Uniprot Name
- 4-trimethylaminobutyraldehyde dehydrogenase
- Molecular Weight
- 53801.495 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Prieto MI, Martin J, Balana-Fouce R, Garrido-Pertierra A: Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie. 1987 Nov-Dec;69(11-12):1161-8. [Article]
- Testore G, Colombatto S, Silvagno F, Bedino S: Purification and kinetic characterization of gamma-aminobutyraldehyde dehydrogenase from rat liver. Int J Biochem Cell Biol. 1995 Nov;27(11):1201-10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (By similarity) (PubMed:27759097). High specificity for all-trans-retinal as substrate, can also accept acetaldehyde as substrate in vitro but with lower affinity (PubMed:27759097). Required for the biosynthesis of normal levels of retinoate in the embryonic ocular and nasal regions; a critical lipid in the embryonic development of the eye and the nasal region (By similarity)
- Specific Function
- aldehyde dehydrogenase (NAD+) activity
- Gene Name
- ALDH1A3
- Uniprot ID
- P47895
- Uniprot Name
- Retinaldehyde dehydrogenase 3
- Molecular Weight
- 56107.995 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Graham CE, Brocklehurst K, Pickersgill RW, Warren MJ: Characterization of retinaldehyde dehydrogenase 3. Biochem J. 2006 Feb 15;394(Pt 1):67-75. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation
- Specific Function
- aldehyde dehydrogenase (NAD+) activity
- Gene Name
- ALDH1B1
- Uniprot ID
- P30837
- Uniprot Name
- Aldehyde dehydrogenase X, mitochondrial
- Molecular Weight
- 57248.96 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Oxidizes medium and long chain saturated and unsaturated aldehydes (PubMed:17382292, PubMed:23721920). Metabolizes also benzaldehyde (PubMed:17382292). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (PubMed:17382292). May have a protective role against the cytotoxicity induced by lipid peroxidation (PubMed:17382292)
- Specific Function
- 3-chloroallyl aldehyde dehydrogenase activity
- Gene Name
- ALDH3B1
- Uniprot ID
- P43353
- Uniprot Name
- Aldehyde dehydrogenase family 3 member B1
- Molecular Weight
- 51839.245 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity)
- Specific Function
- aspartic-type endopeptidase inhibitor activity
- Gene Name
- GAPDH
- Uniprot ID
- P04406
- Uniprot Name
- Glyceraldehyde-3-phosphate dehydrogenase
- Molecular Weight
- 36053.0 Da
References
- Markova EV, Zotova NV, Savchenko AA, Titova NM, Slepov EV, Cherdantsev DV, Konovalenko AN: [Lymphocyte metabolism in patients with acute pancreatitis with different genotypes of GSTM1 and GSTT1 genes]. Biomed Khim. 2006 May-Jun;52(3):317-26. [Article]
- Ido Y: Pyridine nucleotide redox abnormalities in diabetes. Antioxid Redox Signal. 2007 Jul;9(7):931-42. [Article]
- Trost P, Fermani S, Marri L, Zaffagnini M, Falini G, Scagliarini S, Pupillo P, Sparla F: Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms. Photosynth Res. 2006 Sep;89(2-3):263-75. Epub 2006 Sep 22. [Article]
- Swearengin TA, Fibuch EE, Seidler NW: Sevoflurane modulates the activity of glyceraldehyde 3-phosphate dehydrogenase. J Enzyme Inhib Med Chem. 2006 Oct;21(5):575-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (PubMed:29240402, PubMed:33565183). Retinoate signaling is critical for the transcriptional control of many genes, for instance it is crucial for initiation of meiosis in both male and female (Probable) (PubMed:33565183). Recognizes retinal as substrate, both in its free form and when bound to cellular retinol-binding protein (By similarity). Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal (By similarity). Displays complete lack of activity with citral (By similarity)
- Specific Function
- 3-chloroallyl aldehyde dehydrogenase activity
- Gene Name
- ALDH1A2
- Uniprot ID
- O94788
- Uniprot Name
- Retinal dehydrogenase 2
- Molecular Weight
- 56723.495 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Lamb AL, Newcomer ME: The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity. Biochemistry. 1999 May 11;38(19):6003-11. [Article]
- Russo J, Barnes A, Berger K, Desgrosellier J, Henderson J, Kanters A, Merkov L: 4-(N,N-dipropylamino)benzaldehyde inhibits the oxidation of all-trans retinal to all-trans retinoic acid by ALDH1A1, but not the differentiation of HL-60 promyelocytic leukemia cells exposed to all-trans retinal. BMC Pharmacol. 2002;2:4. Epub 2002 Feb 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation of medium and long chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length (PubMed:18035827, PubMed:18182499, PubMed:22633490, PubMed:25047030, PubMed:9133646, PubMed:9662422). Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (PubMed:22633490)
- Specific Function
- 3-chloroallyl aldehyde dehydrogenase activity
- Gene Name
- ALDH3A2
- Uniprot ID
- P51648
- Uniprot Name
- Aldehyde dehydrogenase family 3 member A2
- Molecular Weight
- 54847.36 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Bognar A, Meighen E: Mechanism of a long-chain fatty aldehyde dehydrogenase induced during the development of bioluminescence in Beneckea harveyi. Can J Biochem Cell Biol. 1983 May;61(5):301-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)
- Specific Function
- identical protein binding
- Gene Name
- ALDH5A1
- Uniprot ID
- P51649
- Uniprot Name
- Succinate-semialdehyde dehydrogenase, mitochondrial
- Molecular Weight
- 57214.23 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism
- Specific Function
- aldehyde dehydrogenase (NAD+) activity
- Gene Name
- ALDH7A1
- Uniprot ID
- P49419
- Uniprot Name
- Alpha-aminoadipic semialdehyde dehydrogenase
- Molecular Weight
- 58486.74 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- de La Fuente JL, Rumbero A, Martin JF, Liras P: Delta-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms alpha-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem J. 1997 Oct 1;327 ( Pt 1):59-64. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Enzyme that can both act as a NAD(P)H-dependent reductase and a S-nitroso-CoA-dependent nitrosyltransferase (PubMed:10620517, PubMed:18241201, PubMed:27207795, PubMed:38056462, PubMed:7929092). Promotes fetal heme degradation during development (PubMed:10858451, PubMed:18241201, PubMed:7929092). Also expressed in adult tissues, where it acts as a regulator of hematopoiesis, intermediary metabolism (glutaminolysis, glycolysis, TCA cycle and pentose phosphate pathway) and insulin signaling (PubMed:27207795, PubMed:29500232, PubMed:38056462). Has a broad specificity oxidoreductase activity by catalyzing the NAD(P)H-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone) (PubMed:10620517, PubMed:18241201, PubMed:7929092). Contributes to fetal heme catabolism by catalyzing reduction of biliverdin IXbeta into bilirubin IXbeta in the liver (PubMed:10858451, PubMed:18241201, PubMed:7929092). Biliverdin IXbeta, which constitutes the major heme catabolite in the fetus is not present in adult (PubMed:10858451, PubMed:18241201, PubMed:7929092). Does not reduce bilirubin IXalpha (PubMed:10858451, PubMed:18241201, PubMed:7929092). Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH (PubMed:10620517). Acts as a protein nitrosyltransferase by catalyzing nitrosylation of cysteine residues of target proteins, such as HMOX2, INSR and IRS1 (PubMed:38056462). S-nitroso-CoA-dependent nitrosyltransferase activity is mediated via 'ping-pong' mechanism: BLVRB first associates with both S-nitroso-CoA and protein substrate, nitric oxide group is then transferred from S-nitroso-CoA to Cys-109 and Cys-188 residues of BLVRB and from S-nitroso-BLVRB to the protein substrate (PubMed:38056462). Inhibits insulin signaling by mediating nitrosylation of INSR and IRS1, leading to their inhibition (PubMed:38056462)
- Specific Function
- biliberdin reductase NAD+ activity
- Gene Name
- BLVRB
- Uniprot ID
- P30043
- Uniprot Name
- Flavin reductase (NADPH)
- Molecular Weight
- 22119.215 Da
References
- Deng D, Li X, Fang X, Sun G: Characterization of two components of the 2-naphthoate monooxygenase system from Burkholderia sp. strain JT1500. FEMS Microbiol Lett. 2007 Aug;273(1):22-7. Epub 2007 Jun 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (PubMed:2722838, PubMed:6894153). Involved in cellular response to oxidative stress (PubMed:25865492)
- Specific Function
- pyrroline-5-carboxylate reductase activity
- Gene Name
- PYCR2
- Uniprot ID
- Q96C36
- Uniprot Name
- Pyrroline-5-carboxylate reductase 2
- Molecular Weight
- 33636.815 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Murahama M, Yoshida T, Hayashi F, Ichino T, Sanada Y, Wada K: Purification and characterization of Delta(1)-pyrroline-5-carboxylate reductase isoenzymes, indicating differential distribution in spinach (Spinacia oleracea L.) leaves. Plant Cell Physiol. 2001 Jul;42(7):742-50. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress
- Specific Function
- identical protein binding
- Gene Name
- PYCR1
- Uniprot ID
- P32322
- Uniprot Name
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Molecular Weight
- 33360.27 Da
References
- Wang ZQ, Yuan YZ, Ou JQ, Lin QH, Zhang CF: Glutamine synthetase and glutamate dehydrogenase contribute differentially to proline accumulation in leaves of wheat (Triticum aestivum) seedlings exposed to different salinity. J Plant Physiol. 2007 Jun;164(6):695-701. Epub 2006 Jun 14. [Article]
- Forlani G, Giberti S, Berlicki L, Petrollino D, Kafarski P: Plant P5C reductase as a new target for aminomethylenebisphosphonates. J Agric Food Chem. 2007 May 30;55(11):4340-7. Epub 2007 May 3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:11032875, PubMed:11254391, PubMed:16023112, PubMed:16959573). Plays a role in insulin homeostasis (PubMed:11297618, PubMed:9571255). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity)
- Specific Function
- ADP binding
- Gene Name
- GLUD1
- Uniprot ID
- P00367
- Uniprot Name
- Glutamate dehydrogenase 1, mitochondrial
- Molecular Weight
- 61397.315 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle
- Specific Function
- pyruvate dehydrogenase (acetyl-transferring) activity
- Gene Name
- PDHB
- Uniprot ID
- P11177
- Uniprot Name
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Molecular Weight
- 39233.1 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Taylor SI, Mukherjee C, Jungas RL: Regulation of pyruvate dehydrogenase in isolated rat liver mitochondria. Effects of octanoate, oxidation-reduction state, and adenosine triphosphate to adenosine diphosphate ratio. J Biol Chem. 1975 Mar 25;250(6):2028-35. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle
- Specific Function
- pyruvate dehydrogenase (acetyl-transferring) activity
- Gene Name
- PDHA2
- Uniprot ID
- P29803
- Uniprot Name
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Molecular Weight
- 42932.855 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle
- Specific Function
- pyruvate dehydrogenase (acetyl-transferring) activity
- Gene Name
- PDHA1
- Uniprot ID
- P08559
- Uniprot Name
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Molecular Weight
- 43295.255 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IXalpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor (PubMed:10858451, PubMed:7929092, PubMed:8424666, PubMed:8631357). Does not reduce bilirubin IXbeta (PubMed:10858451). Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7) (PubMed:7929092, PubMed:8424666, PubMed:8631357). NADPH, however, is the probable reactant in biological systems (PubMed:7929092)
- Specific Function
- biliberdin reductase NAD+ activity
- Gene Name
- BLVRA
- Uniprot ID
- P53004
- Uniprot Name
- Biliverdin reductase A
- Molecular Weight
- 33428.225 Da
References
- Franklin E, Browne S, Hayes J, Boland C, Dunne A, Elliot G, Mantle TJ: Activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions. Biochem J. 2007 Jul 1;405(1):61-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:11134486, PubMed:21237683)
- Specific Function
- acyl-CoA dehydrogenase activity
- Gene Name
- ACADS
- Uniprot ID
- P16219
- Uniprot Name
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Molecular Weight
- 44296.705 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2
- Specific Function
- dihydrofolate reductase activity
- Gene Name
- DHFR
- Uniprot ID
- P00374
- Uniprot Name
- Dihydrofolate reductase
- Molecular Weight
- 21452.61 Da
References
- Argyrou A, Jin L, Siconilfi-Baez L, Angeletti RH, Blanchard JS: Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis. Biochemistry. 2006 Nov 28;45(47):13947-53. [Article]
- Vickers TJ, Orsomando G, de la Garza RD, Scott DA, Kang SO, Hanson AD, Beverley SM: Biochemical and genetic analysis of methylenetetrahydrofolate reductase in Leishmania metabolism and virulence. J Biol Chem. 2006 Dec 15;281(50):38150-8. Epub 2006 Oct 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- 2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC (PubMed:24495017, PubMed:25210035, PubMed:28435050). Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (PubMed:24495017, PubMed:25210035, PubMed:28435050, PubMed:35272141). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids (PubMed:25210035). Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate (PubMed:28435050). Mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711)
- Specific Function
- metal ion binding
- Gene Name
- OGDH
- Uniprot ID
- Q02218
- Uniprot Name
- 2-oxoglutarate dehydrogenase complex component E1
- Molecular Weight
- 115934.37 Da
References
- Mailloux RJ, Beriault R, Lemire J, Singh R, Chenier DR, Hamel RD, Appanna VD: The tricarboxylic acid cycle, an ancient metabolic network with a novel twist. PLoS One. 2007 Aug 1;2(8):e690. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission
- Specific Function
- ADP binding
- Gene Name
- GLUD2
- Uniprot ID
- P49448
- Uniprot Name
- Glutamate dehydrogenase 2, mitochondrial
- Molecular Weight
- 61433.465 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core (PubMed:25637936, PubMed:38297129, PubMed:38297130, PubMed:9465114, PubMed:9634533). Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta(24)-sterol reductase (DHCR24) to cholesterol (By similarity). Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation (PubMed:38297129, PubMed:38297130)
- Specific Function
- 7-dehydrocholesterol reductase activity
- Gene Name
- DHCR7
- Uniprot ID
- Q9UBM7
- Uniprot Name
- 7-dehydrocholesterol reductase
- Molecular Weight
- 54488.98 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis
- Specific Function
- chloride ion binding
- Gene Name
- NQO2
- Uniprot ID
- P16083
- Uniprot Name
- Ribosyldihydronicotinamide dehydrogenase [quinone]
- Molecular Weight
- 25918.4 Da
References
- Jamieson D, Tung AT, Knox RJ, Boddy AV: Reduction of mitomycin C is catalysed by human recombinant NRH:quinone oxidoreductase 2 using reduced nicotinamide adenine dinucleotide as an electron donating co-factor. Br J Cancer. 2006 Nov 6;95(9):1229-33. Epub 2006 Oct 10. [Article]
- Iskander K, Li J, Han S, Zheng B, Jaiswal AK: NQO1 and NQO2 regulation of humoral immunity and autoimmunity. J Biol Chem. 2006 Oct 13;281(41):30917-24. Epub 2006 Aug 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Binder
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:16996290). Essential for the catalytic activity and assembly of complex I (PubMed:16996290)
- Specific Function
- ionotropic glutamate receptor binding
- Gene Name
- MT-ND2
- Uniprot ID
- P03891
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 2
- Molecular Weight
- 38960.47 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Nikonova EV, Vijayasarathy C, Zhang L, Cater JR, Galante RJ, Ward SE, Avadhani NG, Pack AI: Differences in activity of cytochrome C oxidase in brain between sleep and wakefulness. Sleep. 2005 Jan;28(1):21-7. [Article]
- Zhang HB, Chen SL, Liu JZ, Xiao B, Chen ZB, Wang HJ: [The changes of gene expression in multiple myeloma treated with thalidomide]. Zhonghua Nei Ke Za Zhi. 2003 May;42(5):300-2. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Bifunctional enzyme that catalyzes the first two steps in lysine degradation
- Specific Function
- histone binding
- Gene Name
- AASS
- Uniprot ID
- Q9UDR5
- Uniprot Name
- Alpha-aminoadipic semialdehyde synthase, mitochondrial
- Molecular Weight
- 102130.895 Da
References
- Xu H, West AH, Cook PF: Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jun 26;46(25):7625-36. Epub 2007 Jun 2. [Article]
- Xu H, West AH, Cook PF: Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2006 Oct 3;45(39):12156-66. [Article]
- Xu H, Alguindigue SS, West AH, Cook PF: A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jan 23;46(3):871-82. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:17275378). Essential for the catalytic activity of complex I (PubMed:17275378)
- Specific Function
- 4 iron, 4 sulfur cluster binding
- Gene Name
- NDUFS7
- Uniprot ID
- O75251
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
- Molecular Weight
- 23563.3 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Schuler F, Yano T, Di Bernardo S, Yagi T, Yankovskaya V, Singer TP, Casida JE: NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron-sulfur cluster N2 to quinone. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):4149-53. [Article]
- Hyslop SJ, Duncan AM, Pitkanen S, Robinson BH: Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13. Genomics. 1996 Nov 1;37(3):375-80. [Article]
- Albracht SP: Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: ubiquinone oxidoreductase. Biochim Biophys Acta. 1993 Sep 13;1144(2):221-4. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Trifunctional enzyme that catalyzes the interconversion of three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and (6S)-10-formyltetrahydrofolate (PubMed:10828945, PubMed:18767138, PubMed:1881876). These derivatives of tetrahydrofolate are differentially required in nucleotide and amino acid biosynthesis, (6S)-10-formyltetrahydrofolate being required for purine biosynthesis while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine and methionine biosynthesis for instance (PubMed:18767138, PubMed:25633902)
- Specific Function
- ATP binding
- Gene Name
- MTHFD1
- Uniprot ID
- P11586
- Uniprot Name
- C-1-tetrahydrofolate synthase, cytoplasmic
- Molecular Weight
- 101530.36 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency
- Specific Function
- magnesium ion binding
- Gene Name
- MTHFD2
- Uniprot ID
- P13995
- Uniprot Name
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
- Molecular Weight
- 37894.775 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
- Specific Function
- 1-pyrroline-5-carboxylate dehydrogenase activity
- Gene Name
- ALDH4A1
- Uniprot ID
- P30038
- Uniprot Name
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Molecular Weight
- 61718.93 Da
References
- Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH: Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase. J Mol Biol. 2006 Sep 22;362(3):490-501. Epub 2006 Jul 29. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor
- Specific Function
- ADP binding
- Gene Name
- CYB5R3
- Uniprot ID
- P00387
- Uniprot Name
- NADH-cytochrome b5 reductase 3
- Molecular Weight
- 34234.55 Da
References
- Roma GW, Crowley LJ, Barber MJ: Expression and characterization of a functional canine variant of cytochrome b5 reductase. Arch Biochem Biophys. 2006 Aug 1;452(1):69-82. Epub 2006 May 24. [Article]
- Nussenzveig RH, Lingam HB, Gaikwad A, Zhu Q, Jing N, Prchal JT: A novel mutation of the cytochrome-b5 reductase gene in an Indian patient: the molecular basis of type I methemoglobinemia. Haematologica. 2006 Nov;91(11):1542-5. [Article]
- Kim S, Suga M, Ogasahara K, Ikegami T, Minami Y, Yubisui T, Tsukihara T: Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt 4):274-9. Epub 2007 Mar 23. [Article]
- Kurian JR, Chin NA, Longlais BJ, Hayes KL, Trepanier LA: Reductive detoxification of arylhydroxylamine carcinogens by human NADH cytochrome b5 reductase and cytochrome b5. Chem Res Toxicol. 2006 Oct;19(10):1366-73. [Article]
- Ikegami T, Kameyama E, Yamamoto SY, Minami Y, Yubisui T: Structure and properties of the recombinant NADH-cytochrome b5 reductase of Physarum polycephalum. Biosci Biotechnol Biochem. 2007 Mar;71(3):783-90. Epub 2007 Mar 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- Not Available
- Gene Name
- NDUFA11
- Uniprot ID
- Q86Y39
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
- Molecular Weight
- 14851.96 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827, PubMed:8344246, PubMed:8644732). Essential for the catalytic activity and assembly of complex I (PubMed:15250827, PubMed:8344246, PubMed:8644732)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND4
- Uniprot ID
- P03905
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 4
- Molecular Weight
- 51580.26 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Shen XY, Zacal N, Singh G, Rainbow AJ: Alterations in mitochondrial and apoptosis-regulating gene expression in photodynamic therapy-resistant variants of HT29 colon carcinoma cells. Photochem Photobiol. 2005 Mar-Apr;81(2):306-13. [Article]
- Carper DA, Sun JK, Iwata T, Zigler JS Jr, Ibaraki N, Lin LR, Reddy V: Oxidative stress induces differential gene expression in a human lens epithelial cell line. Invest Ophthalmol Vis Sci. 1999 Feb;40(2):400-6. [Article]
- Dzelzkalns VA, Obinger C, Regelsberger G, Niederhauser H, Kamensek M, Peschek GA, Bogorad L: Deletion of the structural gene for the NADH-dehydrogenase subunit 4 of Synechocystis 6803 alters respiratory properties. Plant Physiol. 1994 Dec;106(4):1435-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the conversion of quinonoid dihydrobiopterin into tetrahydrobiopterin
- Specific Function
- 6,7-dihydropteridine reductase activity
- Gene Name
- QDPR
- Uniprot ID
- P09417
- Uniprot Name
- Dihydropteridine reductase
- Molecular Weight
- 25789.295 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Nakanishi N, Ozawa K, Yamada S: Determination of NADPH-specific dihydropteridine reductase in extract from human, monkey, and bovine livers by single radial immunodiffusion: selective assay differentiating NADPH- and NADH-specific enzymes. J Biochem. 1986 May;99(5):1311-5. [Article]
- van der Heiden C, Brink W: Spectral studies of the interaction of the substrate 'quinonoid' 6-methyl dihydropterine and the coenzyme NADH used as marker in the dihydropteridine reductase assay. J Inherit Metab Dis. 1982;5(3):132-6. [Article]
- Lee PL, Halloran C, Cross AR, Beutler E: NADH-ferric reductase activity associated with dihydropteridine reductase. Biochem Biophys Res Commun. 2000 May 19;271(3):788-95. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Binder
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:1959619). Essential for the catalytic activity and assembly of complex I (PubMed:1959619, PubMed:26929434)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND1
- Uniprot ID
- P03886
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 1
- Molecular Weight
- 35660.055 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity). May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (PubMed:22634753)
- Specific Function
- NAD binding
- Gene Name
- NNT
- Uniprot ID
- Q13423
- Uniprot Name
- NAD(P) transhydrogenase, mitochondrial
- Molecular Weight
- 113894.595 Da
References
- Kabus A, Georgi T, Wendisch VF, Bott M: Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Appl Microbiol Biotechnol. 2007 May;75(1):47-53. Epub 2007 Jan 11. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA5
- Uniprot ID
- Q16718
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
- Molecular Weight
- 13458.605 Da
References
- Chen CL, Zhang L, Yeh A, Chen CA, Green-Church KB, Zweier JL, Chen YR: Site-specific S-glutathiolation of mitochondrial NADH ubiquinone reductase. Biochemistry. 2007 May 15;46(19):5754-65. Epub 2007 Apr 20. [Article]
- Belevich G, Euro L, Wikstrom M, Verkhovskaya M: Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli. Biochemistry. 2007 Jan 16;46(2):526-33. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Required for proper complex I assembly (PubMed:28671271). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA9
- Uniprot ID
- Q16795
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
- Molecular Weight
- 42509.18 Da
References
- Barker CD, Reda T, Hirst J: The flavoprotein subcomplex of complex I (NADH:ubiquinone oxidoreductase) from bovine heart mitochondria: insights into the mechanisms of NADH oxidation and NAD+ reduction from protein film voltammetry. Biochemistry. 2007 Mar 20;46(11):3454-64. Epub 2007 Feb 27. [Article]
- Balaban RS: Maintenance of the metabolic homeostasis of the heart: developing a systems analysis approach. Ann N Y Acad Sci. 2006 Oct;1080:140-53. [Article]
- Matsuzaki S, Szweda LI: Inhibition of complex I by Ca2+ reduces electron transport activity and the rate of superoxide anion production in cardiac submitochondrial particles. Biochemistry. 2007 Feb 6;46(5):1350-7. [Article]
- Fisher N, Bray PG, Ward SA, Biagini GA: The malaria parasite type II NADH:quinone oxidoreductase: an alternative enzyme for an alternative lifestyle. Trends Parasitol. 2007 Jul;23(7):305-10. Epub 2007 May 10. [Article]
- Liu Y, Qiao DR, Zheng HB, Dai XL, Bai LH, Zeng J, Cao Y: Cloning and sequence analysis of the gene encoding 19-kD subunit of Complex I from Dunaliella salina. Mol Biol Rep. 2008 Sep;35(3):397-403. Epub 2007 May 26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:28844695). Part of the enzyme membrane arm which is embedded in the lipid bilayer and involved in proton translocation (PubMed:28844695)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND4L
- Uniprot ID
- P03901
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 4L
- Molecular Weight
- 10741.005 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA10
- Uniprot ID
- O95299
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
- Molecular Weight
- 40750.28 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA7
- Uniprot ID
- O95182
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
- Molecular Weight
- 12551.27 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA1
- Uniprot ID
- O15239
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
- Molecular Weight
- 8072.325 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Au HC, Seo BB, Matsuno-Yagi A, Yagi T, Scheffler IE: The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria. Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4354-9. [Article]
- Raha S, Myint AT, Johnstone L, Robinson BH: Control of oxygen free radical formation from mitochondrial complex I: roles for protein kinase A and pyruvate dehydrogenase kinase. Free Radic Biol Med. 2002 Mar 1;32(5):421-30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14595656, PubMed:8644732). Essential for the catalytic activity and assembly of complex I (PubMed:14595656, PubMed:8644732)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND6
- Uniprot ID
- P03923
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 6
- Molecular Weight
- 18622.045 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827). Essential for the catalytic activity and assembly of complex I (PubMed:15250827)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- MT-ND5
- Uniprot ID
- P03915
- Uniprot Name
- NADH-ubiquinone oxidoreductase chain 5
- Molecular Weight
- 67025.67 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Johnson WE, O'Brien SJ: Phylogenetic reconstruction of the Felidae using 16S rRNA and NADH-5 mitochondrial genes. J Mol Evol. 1997;44 Suppl 1:S98-116. [Article]
- Bao HG, Zhao CJ, Li JY, Wu Ch: Association of MT-ND5 gene variation with mitochondrial respiratory control ratio and NADH dehydrogenase activity in Tibet chicken embryos. Anim Genet. 2007 Oct;38(5):514-6. Epub 2007 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (PubMed:22902835). NDUFA4 is required for complex IV maintenance (PubMed:22902835)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA4
- Uniprot ID
- O00483
- Uniprot Name
- Cytochrome c oxidase subunit NDUFA4
- Molecular Weight
- 9369.78 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly (PubMed:30245030). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA6
- Uniprot ID
- P56556
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
- Molecular Weight
- 15136.485 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity) (PubMed:27626371). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (PubMed:27626371). Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:31664822). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity)
- Specific Function
- acyl binding
- Gene Name
- NDUFAB1
- Uniprot ID
- O14561
- Uniprot Name
- Acyl carrier protein, mitochondrial
- Molecular Weight
- 17417.095 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA2
- Uniprot ID
- O43678
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
- Molecular Weight
- 10921.45 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371, PubMed:32385911, PubMed:33153867). Complex I functions in the transfer of electrons from NADH to the respiratory chain (PubMed:27626371). The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371)
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA8
- Uniprot ID
- P51970
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
- Molecular Weight
- 20104.875 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Triepels R, van den Heuvel L, Loeffen J, Smeets R, Trijbels F, Smeitink J: The nuclear-encoded human NADH:ubiquinone oxidoreductase NDUFA8 subunit: cDNA cloning, chromosomal localization, tissue distribution, and mutation detection in complex-I-deficient patients. Hum Genet. 1998 Nov;103(5):557-63. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA3
- Uniprot ID
- O95167
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
- Molecular Weight
- 9278.785 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB8
- Uniprot ID
- O95169
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial
- Molecular Weight
- 21765.665 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFC2
- Uniprot ID
- O95298
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 subunit C2
- Molecular Weight
- 14187.33 Da
References
- Gyan S, Shiohira Y, Sato I, Takeuchi M, Sato T: Regulatory loop between redox sensing of the NADH/NAD(+) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis. J Bacteriol. 2006 Oct;188(20):7062-71. [Article]
- Quiles MJ: Stimulation of chlororespiration by heat and high light intensity in oat plants. Plant Cell Environ. 2006 Aug;29(8):1463-70. [Article]
- Brooijmans RJ, Poolman B, Schuurman-Wolters GK, de Vos WM, Hugenholtz J: Generation of a membrane potential by Lactococcus lactis through aerobic electron transport. J Bacteriol. 2007 Jul;189(14):5203-9. Epub 2007 May 11. [Article]
- Bao HG, Zhao CJ, Li JY, Wu Ch: Association of MT-ND5 gene variation with mitochondrial respiratory control ratio and NADH dehydrogenase activity in Tibet chicken embryos. Anim Genet. 2007 Oct;38(5):514-6. Epub 2007 Jul 5. [Article]
- Zhu X, Liu B, Zhou S, Chen YR, Deng Y, Zweier JL, He G: Ischemic preconditioning prevents in vivo hyperoxygenation in postischemic myocardium with preservation of mitochondrial oxygen consumption. Am J Physiol Heart Circ Physiol. 2007 Sep;293(3):H1442-50. Epub 2007 May 18. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB1
- Uniprot ID
- O75438
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1
- Molecular Weight
- 6961.165 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:30879903, PubMed:31557978). Essential for catalysing the entry and efficient transfer of electrons within complex I (PubMed:31557978). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:30879903, PubMed:31557978)
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- NDUFS1
- Uniprot ID
- P28331
- Uniprot Name
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Molecular Weight
- 79466.77 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB10
- Uniprot ID
- O96000
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
- Molecular Weight
- 20776.545 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB4
- Uniprot ID
- O95168
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
- Molecular Weight
- 15208.4 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB3
- Uniprot ID
- O43676
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
- Molecular Weight
- 11401.945 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB2
- Uniprot ID
- O95178
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial
- Molecular Weight
- 12058.36 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB7
- Uniprot ID
- P17568
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
- Molecular Weight
- 16401.82 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Raha S, Myint AT, Johnstone L, Robinson BH: Control of oxygen free radical formation from mitochondrial complex I: roles for protein kinase A and pyruvate dehydrogenase kinase. Free Radic Biol Med. 2002 Mar 1;32(5):421-30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB9
- Uniprot ID
- Q9Y6M9
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
- Molecular Weight
- 21830.75 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:22036843, PubMed:30922174, PubMed:28031252). Essential for the catalytic activity of complex I (PubMed:22036843, PubMed:30922174). Essential for the assembly of complex I (By similarity). Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174). Plays an important role in carotid body sensing of hypoxia (By similarity). Essential for glia-like neural stem and progenitor cell proliferation, differentiation and subsequent oligodendrocyte or neuronal maturation (By similarity)
- Specific Function
- 4 iron, 4 sulfur cluster binding
- Gene Name
- NDUFS2
- Uniprot ID
- O75306
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
- Molecular Weight
- 52545.26 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB5
- Uniprot ID
- O43674
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial
- Molecular Weight
- 21750.05 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFC1
- Uniprot ID
- O43677
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
- Molecular Weight
- 8734.155 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFB6
- Uniprot ID
- O95139
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6
- Molecular Weight
- 15489.145 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFV3
- Uniprot ID
- P56181
- Uniprot Name
- NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial
- Molecular Weight
- 11940.435 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity)
- Specific Function
- dihydrolipoyl dehydrogenase activity
- Gene Name
- DLD
- Uniprot ID
- P09622
- Uniprot Name
- Dihydrolipoyl dehydrogenase, mitochondrial
- Molecular Weight
- 54176.91 Da
References
- Yan LJ, Yang SH, Shu H, Prokai L, Forster MJ: Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE. Electrophoresis. 2007 Apr;28(7):1036-45. [Article]
- Gutierrez-Correa J: Trypanosoma cruzi dihydrolipoamide dehydrogenase as target for phenothiazine cationic radicals. Effect of antioxidants. Curr Drug Targets. 2006 Sep;7(9):1155-79. [Article]
- Islam MM, Wallin R, Wynn RM, Conway M, Fujii H, Mobley JA, Chuang DT, Hutson SM: A novel branched-chain amino acid metabolon. Protein-protein interactions in a supramolecular complex. J Biol Chem. 2007 Apr 20;282(16):11893-903. Epub 2007 Feb 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14729820, PubMed:30140060). Essential for the catalytic activity and assembly of complex I (PubMed:14729820, PubMed:24028823, PubMed:30140060)
- Specific Function
- electron transfer activity
- Gene Name
- NDUFS3
- Uniprot ID
- O75489
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial
- Molecular Weight
- 30241.245 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Maintains high levels of reduced glutathione in the cytosol
- Specific Function
- electron transfer activity
- Gene Name
- GSR
- Uniprot ID
- P00390
- Uniprot Name
- Glutathione reductase, mitochondrial
- Molecular Weight
- 56256.565 Da
References
- Knapp KG, Swartz JR: Evidence for an additional disulfide reduction pathway in Escherichia coli. J Biosci Bioeng. 2007 Apr;103(4):373-6. [Article]
- Aon MA, Cortassa S, Maack C, O'Rourke B: Sequential opening of mitochondrial ion channels as a function of glutathione redox thiol status. J Biol Chem. 2007 Jul 27;282(30):21889-900. Epub 2007 May 31. [Article]
- Wan C, Li S, Wen L, Kong J, Wang K, Zhu Y: Damage of oxidative stress on mitochondria during microspores development in Honglian CMS line of rice. Plant Cell Rep. 2007 Mar;26(3):373-82. Epub 2006 Oct 12. [Article]
- Cheng Z, Arscott LD, Ballou DP, Williams CH Jr: The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila. Biochemistry. 2007 Jul 3;46(26):7875-85. Epub 2007 Jun 6. [Article]
- Gazaryan IG, Krasinskaya IP, Kristal BS, Brown AM: Zinc irreversibly damages major enzymes of energy production and antioxidant defense prior to mitochondrial permeability transition. J Biol Chem. 2007 Aug 17;282(33):24373-80. Epub 2007 Jun 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFA12
- Uniprot ID
- Q9UI09
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
- Molecular Weight
- 17114.43 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFS5
- Uniprot ID
- O43920
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
- Molecular Weight
- 12517.415 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Loeffen J, Smeets R, Smeitink J, Triepels R, Sengers R, Trijbels F, van den Heuvel L: The human NADH: ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA cloning, chromosomal localization, tissue distribution and the absence of mutations in isolated complex I-deficient patients. J Inherit Metab Dis. 1999 Feb;22(1):19-28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- NADH dehydrogenase (ubiquinone) activity
- Gene Name
- NDUFS4
- Uniprot ID
- O43181
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
- Molecular Weight
- 20107.84 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Papa S, Sardanelli AM, Scacco S, Petruzzella V, Technikova-Dobrova Z, Vergari R, Signorile A: The NADH: ubiquinone oxidoreductase (complex I) of the mammalian respiratory chain and the cAMP cascade. J Bioenerg Biomembr. 2002 Feb;34(1):1-10. [Article]
- Petruzzella V, Vergari R, Puzziferri I, Boffoli D, Lamantea E, Zeviani M, Papa S: A nonsense mutation in the NDUFS4 gene encoding the 18 kDa (AQDQ) subunit of complex I abolishes assembly and activity of the complex in a patient with Leigh-like syndrome. Hum Mol Genet. 2001 Mar 1;10(5):529-35. [Article]
- Raha S, Myint AT, Johnstone L, Robinson BH: Control of oxygen free radical formation from mitochondrial complex I: roles for protein kinase A and pyruvate dehydrogenase kinase. Free Radic Biol Med. 2002 Mar 1;32(5):421-30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:28844695). Part of the peripheral arm of the enzyme, where the electrons from NADH are accepted by flavin mononucleotide (FMN) and then passed along a chain of iron-sulfur clusters by electron tunnelling to the final acceptor ubiquinone (PubMed:28844695). Contains FMN, which is the initial electron acceptor as well as one iron-sulfur cluster (PubMed:28844695)
- Specific Function
- 4 iron, 4 sulfur cluster binding
- Gene Name
- NDUFV1
- Uniprot ID
- P49821
- Uniprot Name
- NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
- Molecular Weight
- 50816.685 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Schuelke M, Loeffen J, Mariman E, Smeitink J, van den Heuvel L: Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon inducible protein (IP-30) precursor: is this a link between mitochondrial myopathy and inflammation? Biochem Biophys Res Commun. 1998 Apr 17;245(2):599-606. [Article]
- Ali ST, Duncan AM, Schappert K, Heng HH, Tsui LC, Chow W, Robinson BH: Chromosomal localization of the human gene encoding the 51-kDa subunit of mitochondrial complex I (NDUFV1) to 11q13. Genomics. 1993 Nov;18(2):435-9. [Article]
- Grad LI, Lemire BD: Mitochondrial complex I mutations in Caenorhabditis elegans produce cytochrome c oxidase deficiency, oxidative stress and vitamin-responsive lactic acidosis. Hum Mol Genet. 2004 Feb 1;13(3):303-14. Epub 2003 Dec 8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (Probable). Parts of the peripheral arm of the enzyme, where the electrons from NADH are accepted by flavin mononucleotide (FMN) and then passed along a chain of iron-sulfur clusters by electron tunnelling to the final acceptor ubiquinone (Probable). Contains one iron-sulfur cluster (Probable)
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- NDUFV2
- Uniprot ID
- P19404
- Uniprot Name
- NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
- Molecular Weight
- 27391.36 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Paunesku T, Chang-Liu CM, Shearin-Jones P, Watson C, Milton J, Oryhon J, Salbego D, Milosavljevic A, Woloschak GE: Identification of genes regulated by UV/salicylic acid. Int J Radiat Biol. 2000 Feb;76(2):189-98. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis (PubMed:27626371). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:27626371). Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes (PubMed:15753091)
- Specific Function
- ATP binding
- Gene Name
- NDUFA13
- Uniprot ID
- Q9P0J0
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
- Molecular Weight
- 16698.175 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen
- Specific Function
- cysteine dioxygenase activity
- Gene Name
- CDO1
- Uniprot ID
- Q16878
- Uniprot Name
- Cysteine dioxygenase type 1
- Molecular Weight
- 22971.745 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
- Specific Function
- electron transfer activity
- Gene Name
- NDUFS6
- Uniprot ID
- O75380
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
- Molecular Weight
- 13711.535 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Not Available
- Gene Name
- NDUFA4L2
- Uniprot ID
- Q9NRX3
- Uniprot Name
- NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2
- Molecular Weight
- 9965.58 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:22499348). Essential for the catalytic activity and assembly of complex I (PubMed:22499348)
- Specific Function
- 4 iron, 4 sulfur cluster binding
- Gene Name
- NDUFS8
- Uniprot ID
- O00217
- Uniprot Name
- NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
- Molecular Weight
- 23704.795 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Albracht SP, Hedderich R: Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH--ubiquinone oxidoreductase (Complex I). FEBS Lett. 2000 Nov 17;485(1):1-6. [Article]
- Loeffen J, Smeitink J, Triepels R, Smeets R, Schuelke M, Sengers R, Trijbels F, Hamel B, Mullaart R, van den Heuvel L: The first nuclear-encoded complex I mutation in a patient with Leigh syndrome. Am J Hum Genet. 1998 Dec;63(6):1598-608. [Article]
- Jose Quiles M, Cuello J: Association of ferredoxin-NADP oxidoreductase with the chloroplastic pyridine nucleotide dehydrogenase complex in barley leaves Plant Physiol. 1998 May;117(1):235-44. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid (PubMed:10553002, PubMed:10660572). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10620324, PubMed:10660572, PubMed:15611369). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:7679927). May contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening (PubMed:18182499). Omega-hydroxylates (9R,10S)-epoxy-octadecanoate stereoisomer (PubMed:15145985). Plays a minor role in omega-oxidation of long-chain 3-hydroxy fatty acids (PubMed:18065749). Has little activity toward prostaglandins A1 and E1 (PubMed:7679927)
- Specific Function
- alkane 1-monooxygenase activity
- Gene Name
- CYP4A11
- Uniprot ID
- Q02928
- Uniprot Name
- Cytochrome P450 4A11
- Molecular Weight
- 59347.31 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Ngo S, Kong S, Kirlich A, McKinnon RA, Stupans I: Cytochrome P450 4A, peroxisomal enzymes and nicotinamide cofactors in koala liver. Comp Biochem Physiol C Toxicol Pharmacol. 2000 Dec;127(3):327-34. [Article]
Details138. Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (Probable). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable)
- Specific Function
- dihydrolipoyllysine-residue acetyltransferase activity
- Gene Name
- DLAT
- Uniprot ID
- P10515
- Uniprot Name
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Molecular Weight
- 68996.03 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Shi S, Ehrt S: Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis. Infect Immun. 2006 Jan;74(1):56-63. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- The glycine cleavage system catalyzes the degradation of glycine
- Specific Function
- aminomethyltransferase activity
- Gene Name
- AMT
- Uniprot ID
- P48728
- Uniprot Name
- Aminomethyltransferase, mitochondrial
- Molecular Weight
- 43945.65 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be subsequently metabolized to cholesterol (PubMed:21285510, PubMed:23583456, PubMed:26114596, PubMed:28673550). Also involved in drug metabolism, as it can metabolize eldecalcitol (ED-71 or 1alpha,25-dihydroxy-2beta-(3-hydroxypropoxy)-cholecalciferol), a second-generation vitamin D analog, into 1alpha,2beta,25-trihydroxy vitamin D3; this reaction occurs via enzymatic hydroxylation and spontaneous O-dehydroxypropylation (PubMed:26038696)
- Specific Function
- C-4 methylsterol oxidase activity
- Gene Name
- MSMO1
- Uniprot ID
- Q15800
- Uniprot Name
- Methylsterol monooxygenase 1
- Molecular Weight
- 35215.42 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707)
- Specific Function
- enzyme binding
- Gene Name
- HMOX1
- Uniprot ID
- P09601
- Uniprot Name
- Heme oxygenase 1
- Molecular Weight
- 32818.345 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Calo LA, Pagnin E, Davis PA, Sartori M, Semplicini A: Oxidative stress-related factors in Bartter's and Gitelman's syndromes: relevance for angiotensin II signalling. Nephrol Dial Transplant. 2003 Aug;18(8):1518-25. [Article]
- Auclair K, Huang HW, Moenne-Loccoz P, Ortiz de Montellano PR: Cloning and expression of a heme binding protein from the genome of Saccharomyces cerevisiae. Protein Expr Purif. 2003 Apr;28(2):340-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron
- Specific Function
- heme binding
- Gene Name
- HMOX2
- Uniprot ID
- P30519
- Uniprot Name
- Heme oxygenase 2
- Molecular Weight
- 36032.615 Da
References
- Tanaka M, Ohkubo K, Fukuzumi S: DNA cleavage by UVA irradiation of NADH with dioxygen via radical chain processes. J Phys Chem A. 2006 Sep 28;110(38):11214-8. [Article]
- Goldstone AB, Liochev SI, Fridovich I: Inactivation of copper, zinc superoxide dismutase by H2O2 : mechanism of protection. Free Radic Biol Med. 2006 Dec 15;41(12):1860-3. Epub 2006 Sep 19. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426). Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol (Probable) (PubMed:25301938, PubMed:9452426). Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:36640554, PubMed:9452426). Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA (PubMed:36640554). Also 16-alpha hydroxylates androgens, relevant for estriol synthesis (PubMed:25301938, PubMed:27339894). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426)
- Specific Function
- heme binding
- Gene Name
- CYP17A1
- Uniprot ID
- P05093
- Uniprot Name
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Molecular Weight
- 57369.995 Da
References
- Pandey AV, Kempna P, Hofer G, Mullis PE, Fluck CE: Modulation of human CYP19A1 activity by mutant NADPH P450 oxidoreductase. Mol Endocrinol. 2007 Oct;21(10):2579-95. Epub 2007 Jun 26. [Article]
Details144. Tyrosinase
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (PubMed:28661582)
- Specific Function
- copper ion binding
- Gene Name
- TYR
- Uniprot ID
- P14679
- Uniprot Name
- Tyrosinase
- Molecular Weight
- 60392.69 Da
References
- Jadhav JP, Parshetti GK, Kalme SD, Govindwar SP: Decolourization of azo dye methyl red by Saccharomyces cerevisiae MTCC 463. Chemosphere. 2007 Jun;68(2):394-400. Epub 2007 Feb 9. [Article]
- Zafar KS, Siegel D, Ross D: A potential role for cyclized quinones derived from dopamine, DOPA, and 3,4-dihydroxyphenylacetic acid in proteasomal inhibition. Mol Pharmacol. 2006 Sep;70(3):1079-86. Epub 2006 Jun 21. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (PubMed:10510318, PubMed:30538128). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes (By similarity). Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN) (PubMed:11306097, PubMed:18276838). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (PubMed:30538128). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (PubMed:31649033). Displays no reductase activity towards retinoids (By similarity)
- Specific Function
- aldo-keto reductase (NADPH) activity
- Gene Name
- AKR1A1
- Uniprot ID
- P14550
- Uniprot Name
- Aldo-keto reductase family 1 member A1
- Molecular Weight
- 36572.71 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH1A
- Uniprot ID
- P07327
- Uniprot Name
- Alcohol dehydrogenase 1A
- Molecular Weight
- 39858.37 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed:15369820, PubMed:16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed:15369820)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH1B
- Uniprot ID
- P00325
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH1B
- Molecular Weight
- 39835.17 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (PubMed:17279314). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Also catalyzes the reduction of benzoquinones (PubMed:10514444)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH4
- Uniprot ID
- P08319
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH4
- Molecular Weight
- 40221.335 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed:8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed:16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed:8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed:33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity)
- Specific Function
- alcohol dehydrogenase (NAD+) activity, zinc-dependent
- Gene Name
- ADH5
- Uniprot ID
- P11766
- Uniprot Name
- Alcohol dehydrogenase class-3
- Molecular Weight
- 39723.945 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid (PubMed:15369820, PubMed:16787387, PubMed:9600267). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and aldehydes and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and hexanal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:15369820, PubMed:16787387). Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation (PubMed:15369820, PubMed:16787387, PubMed:9600267)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH7
- Uniprot ID
- P40394
- Uniprot Name
- All-trans-retinol dehydrogenase [NAD(+)] ADH7
- Molecular Weight
- 41480.985 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- XDH
- Uniprot ID
- P47989
- Uniprot Name
- Xanthine dehydrogenase/oxidase
- Molecular Weight
- 146422.99 Da
References
- Kalimuthu P, Leimkuhler S, Bernhardt PV: Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity. J Phys Chem B. 2011 Mar 24;115(11):2655-62. doi: 10.1021/jp111809f. Epub 2011 Mar 1. [Article]
- Al-Gonaiah M, Smith RA, Stone TW: Xanthine oxidase-induced neuronal death via the oxidation of NADH: prevention by micromolar EDTA. Brain Res. 2009 Jul 14;1280:33-42. doi: 10.1016/j.brainres.2009.05.024. Epub 2009 May 18. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- AOX1
- Uniprot ID
- Q06278
- Uniprot Name
- Aldehyde oxidase
- Molecular Weight
- 147916.735 Da
References
- Mantle D, Preedy VR: Free radicals as mediators of alcohol toxicity. Adverse Drug React Toxicol Rev. 1999 Nov;18(4):235-52. [Article]
- Li H, Kundu TK, Zweier JL: Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite. J Biol Chem. 2009 Dec 4;284(49):33850-8. doi: 10.1074/jbc.M109.019125. Epub 2009 Sep 28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- SubstrateActivator
- General Function
- Alcohol dehydrogenase (PubMed:1755855). Catalyzes the NAD-dependent oxidation of primary alcohols to the corresponding aldehydes (PubMed:1755855). Oxidizes secondary alcohols to the corresponding ketones (By similarity)
- Specific Function
- alcohol dehydrogenase (NAD+) activity
- Gene Name
- ADH6
- Uniprot ID
- P28332
- Uniprot Name
- Alcohol dehydrogenase 6
- Molecular Weight
- 39072.275 Da
References
- Plapp BV: Conformational changes and catalysis by alcohol dehydrogenase. Arch Biochem Biophys. 2010 Jan 1;493(1):3-12. doi: 10.1016/j.abb.2009.07.001. Epub 2009 Jul 5. [Article]
Drug created at June 13, 2005 13:24 / Updated at August 26, 2024 19:23