Ferrous gluconate
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Identification
- Summary
Ferrous gluconate is a medication used to treat iron-deficiency anemia.
- Generic Name
- Ferrous gluconate
- DrugBank Accession Number
- DB14488
- Background
Not Available
- Type
- Small Molecule
- Groups
- Approved
- Structure
- Weight
- Average: 446.139
Monoisotopic: 446.035891 - Chemical Formula
- C12H22FeO14
- Synonyms
- D-gluconic acid, iron(2+) salt (2:1)
- Ferric Gluconate
- Ferrous gluconate anhydrous
- Iron(2+) gluconate (1:2)
- Iron(II) gluconate, anhydrous
Pharmacology
- Indication
Used in preventing and treating iron-deficiency anemia.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Used in combination to prevent Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• ••••••••••••• •••••••• •••••• •••••• Used in combination to treat Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• ••••••••••••• •••••••• •••••• •••••• Used in combination to treat Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• •••••••• ••••• •••••••• •••••• •••••• Used in combination to prevent Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• •••••••• ••••• •••••••• •••••• •••••• Used in combination to treat Iron deficiency Combination Product in combination with: Ascorbic acid (DB00126) •••••••••••• •••••• - 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
The major activity of supplemental iron is in the prevention and treatment of iron deficiency anemia. Iron has putative immune-enhancing, anticarcinogenic and cognition-enhancing activities.
- Mechanism of action
Iron is necessary for the production of hemoglobin. Iron-deficiency can lead to decreased production of hemoglobin and a microcytic, hypochromic anemia.
Target Actions Organism UTransferrin receptor protein 1 Not Available Humans UEgl nine homolog 1 Not Available Humans UHistone deacetylase 8 Not Available Humans UAlpha-hemoglobin-stabilizing protein Not Available Humans UHemoglobin subunit alpha Not Available Humans UFrataxin, mitochondrial Not Available Humans UFerritin heavy chain Not Available Humans UFlap endonuclease 1 Not Available Humans UEndonuclease 8-like 1 Not Available Humans UEndonuclease 8-like 2 Not Available Humans UDNA polymerase beta Not Available Humans UCeruloplasmin Not Available Humans USerotransferrin Not Available Humans - Absorption
The efficiency of absorption depends on the salt form, the amount administered, the dosing regimen and the size of iron stores. Subjects with normal iron stores absorb 10% to 35% of an iron dose. Those who are iron deficient may absorb up to 95% of an iron dose.
- 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
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Acute iron overdosage can be divided into four stages. In the first stage, which occurs up to six hours after ingestion, the principal symptoms are vomiting and diarrhea. Other symptoms include hypotension, tachycardia and CNS depression ranging from lethargy to coma. The second phase may occur at 6-24 hours after ingestion and is characterized by a temporary remission. In the third phase, gastrointestinal symptoms recur accompanied by shock, metabolic acidosis, coma, hepatic necrosis and jaundice, hypoglycemia, renal failure and pulmonary edema. The fourth phase may occur several weeks after ingestion and is characterized by gastrointestinal obstruction and liver damage. In a young child, 75 milligrams per kilogram is considered extremely dangerous. A dose of 30 milligrams per kilogram can lead to symptoms of toxicity. Estimates of a lethal dosage range from 180 milligrams per kilogram and upwards. A peak serum iron concentration of five micrograms or more per ml is associated with moderate to severe poisoning in many.
- Pathways
- Not Available
- 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.
Drug Interaction Integrate drug-drug
interactions in your softwareAlendronic acid Ferrous gluconate can cause a decrease in the absorption of Alendronic acid resulting in a reduced serum concentration and potentially a decrease in efficacy. Almasilate Almasilate can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Aluminium phosphate Aluminium phosphate can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Aluminum hydroxide Aluminum hydroxide can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Asenapine Asenapine can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. - Food Interactions
- Avoid milk and dairy products. Take ferrous gluconate at least 2 hours before or after milk.
- Limit caffeine intake. Food and beverages containing caffeine may reduce iron absorption.
- Take at least 2 hours before or after calcium supplements.
- Take separate from antacids. Take ferrous gluconate at least 2 hours before or after antacids.
- Take with food. This reduces gastric irritation.
- Take with foods containing vitamin C. Foods rich in vitamin C increase the absorption of iron.
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.
- Product Ingredients
Ingredient UNII CAS InChI Key Ferrous gluconate dihydrate U1B11I423Z 6047-12-7 OKGNXSFAYMSVNN-SYAJEJNSSA-L - Active Moieties
Name Kind UNII CAS InChI Key Iron unknown E1UOL152H7 7439-89-6 XEEYBQQBJWHFJM-UHFFFAOYSA-N Ferrous cation ionic GW89581OWR 15438-31-0 CWYNVVGOOAEACU-UHFFFAOYSA-N - Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Ferrous Gluconate Tablet 35 mg Oral Wn Pharmaceuticals Ltd. 2002-05-31 2007-08-07 Canada Ferrous Gluconate Tab 300mg Tablet 300 mg / tab Oral Pharmetics (2011) Inc. 1973-12-31 2000-08-21 Canada Ferrous Gluconate Tab 300mg Tablet 300 mg / tab Oral Shoppers Drug Mart Inc. 1977-12-31 1997-08-15 Canada Ferrous Gluconate Tab 300mg Tablet 300 mg Oral Vita Health Products Inc 1957-12-31 2005-07-20 Canada Ferrous Gluconate Tablet 300mg Tablet 300 mg Oral D.C. Labs Limited 1969-12-31 2005-07-19 Canada - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Alsimine W Vitamins A D Ferrous gluconate (16 mg / amp) + Calcium glycerophosphate (13 mg / amp) + Cyanocobalamin (10 mcg / amp) + Dexpanthenol (5 mg / amp) + Dexpanthenol (400 unit / amp) + Riboflavin-5'-phosphate sodium salt dihydrate (2 mg / amp) + Nicotinamide (40 mg / amp) + Pyridoxine hydrochloride (3 mg / amp) + Thiamine hydrochloride (4.5 mg / amp) + Vitamin A (10000 unit / amp) Capsule; Liquid Oral Alsi Cie Ltee 1978-12-31 2003-05-21 Canada ANFEZINC - G SURUP Ferrous gluconate (40 mg/5mL) + Zinc gluconate (15 mg/5mL) Syrup Oral BERAT BERAN İLAÇ SAN. VE TİC. LTD. ŞTİ. 2012-08-27 2024-01-23 Turkey Bev 29 Tab Ferrous gluconate (1 mg / tab) + Biotin (3 mcg / tab) + Choline (63 mg / tab) + Cyanocobalamin (50 mcg / tab) + Folic acid (.013 mg / tab) + Inositol (7 mg / tab) + Niacin (1 mg / tab) + Pantothenic acid (25 mg / tab) + Riboflavin (.025 mg / tab) + Thiamine (10 mg / tab) Tablet Oral Beverly International Nutrition 1987-12-31 1998-08-01 Canada Children's Chew Multi & Min Tab Ferrous gluconate (2.5 mg / tab) + Ascorbic acid (30 mg / tab) + Beta carotene (1250 unit / tab) + Biotin (75 mcg / tab) + Calcium carbonate (100 mg / tab) + Choline bitartrate (5 mg / tab) + Copper gluconate (1 mg / tab) + Cyanocobalamin (5 mcg / tab) + DL-alpha tocopheryl acetate (15 unit / tab) + Iodine (.075 mg / tab) + Magnesium oxide (25 mg / tab) + Manganese gluconate (.5 mg / tab) + Nicotinamide (10 mg / tab) + Calcium pantothenate (6.25 mg / tab) + Potassium chloride (.5 mg / tab) + Potassium chloride (5 mg / tab) + Pyridoxine hydrochloride (1.25 mg / tab) + Riboflavin (1.25 mg / tab) + Thiamine hydrochloride (1.25 mg / tab) + Vitamin A palmitate (1250 unit / tab) + Vitamin D (200 unit / tab) + Zinc gluconate (1.25 mg / tab) Tablet Oral Natrol, Inc. 1995-12-31 2001-07-30 Canada Dynam Ampoule Et Tablet Ferrous gluconate (16 mg / 10 mL) + Ascorbic acid (150 mg / 10 mL) + Cyanocobalamin (10 mcg / 10 mL) + Dexpanthenol (5 mg / 10 mL) + Riboflavin-5'-phosphate sodium salt dihydrate (2 mg / 10 mL) + Nicotinamide (40 mg / 10 mL) + Pyridoxine hydrochloride (3 mg / 10 mL) + Thiamine hydrochloride (4.5 mg / 10 mL) + Vitamin A (5000 unit / 10 mL) + Vitamin D (400 unit / 10 mL) Liquid; Tablet Oral Cardinaux Enrg Les Produits Naturels 1989-12-31 1996-09-09 Canada - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image BioFerr 90 Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Biocomp Pharma, Inc. 2014-07-01 Not applicable US CitraNatal 90 DHA Ferrous gluconate dihydrate (5 mg/1) + Ascorbic acid (120 mg/1) + Calcium citrate tetrahydrate (159 mg/1) + Cupric oxide (2 mg/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Iron (85 mg/1) + Nicotinamide (20 mg/1) + Potassium Iodide (150 ug/1) + Pyridoxine hydrochloride (20 mg/1) + Riboflavin (3.4 mg/1) + Thiamine chloride (3 mg/1) + Thiamine mononitrate (4.54 mg/1) + Vitamin D (400 [iU]/1) + Zinc oxide (25 mg/1) + alpha-Tocopherol acetate (30 [iU]/1) Tablet Oral Mission Pharmacal Company 2014-04-11 Not applicable US CitraNatal Bloom Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Mission Pharmacal Company 2017-08-01 2024-06-01 US CitraNatal Bloom Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Mission Pharmacal Company 2017-08-01 2017-07-20 US CitraNatal Bloom DHA Ferrous gluconate dihydrate (1.5 mg/1) + Ascorbic acid (120 mg/1) + Crypthecodinium cohnii DHA oil (300 mg/300mg) + Cyanocobalamin (12 ug/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Iron (88.5 mg/1) Kit Oral Mission Pharmacal Company 2018-01-18 Not applicable US
Categories
- ATC Codes
- B03AD05 — Ferrous gluconate and folic acid
- B03AD — Iron in combination with folic acid
- B03A — IRON PREPARATIONS
- B03 — ANTIANEMIC PREPARATIONS
- B — BLOOD AND BLOOD FORMING ORGANS
- Drug Categories
- Classification
- Not classified
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 781E2AXH0K
- CAS number
- 299-29-6
- InChI Key
- VRIVJOXICYMTAG-IYEMJOQQSA-L
- InChI
- InChI=1S/2C6H12O7.Fe/c2*7-1-2(8)3(9)4(10)5(11)6(12)13;/h2*2-5,7-11H,1H2,(H,12,13);/q;;+2/p-2/t2*2-,3-,4+,5-;/m11./s1
- IUPAC Name
- lambda2-iron(2+) bis((2R,3S,4R,5R)-2,3,4,5,6-pentahydroxyhexanoate)
- SMILES
- [Fe++].[H][C@@](O)(CO)[C@@]([H])(O)[C@]([H])(O)[C@@]([H])(O)C([O-])=O.[H][C@@](O)(CO)[C@@]([H])(O)[C@]([H])(O)[C@@]([H])(O)C([O-])=O
References
- General References
- TITCK Product Information: Ferrozinc-G (ferrous gluconate/zinc gluconate) oral syrup [Link]
- External Links
- PubChem Compound
- 9291
- ChemSpider
- 19953133
- Wikipedia
- Iron(II)_gluconate
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 dataNot Available Unknown Status Treatment Renal Failure Chronic Requiring Hemodialysis 1 somestatus stop reason just information to hide 4 Completed Basic Science Anemia 1 somestatus stop reason just information to hide 4 Completed Diagnostic Iron Absorption / Post-gastrointestinal bypass surgery / Roux-en-Y Gastric Bypass 1 somestatus stop reason just information to hide 4 Completed Treatment Anemia 1 somestatus stop reason just information to hide 4 Completed Treatment Endometrial Cancer / Perioperative Complications / Prehabilitation 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Capsule; liquid Oral Solution Oral 6.66 mg Suspension Oral 600 mg Tablet, film coated Oral Solution Oral 3.33 g Powder, for solution Oral 126 mg Powder, for solution Oral 126 MG/10ML Powder, for solution Oral 80 MG Tablet Oral 80 MG Tablet Oral 35 mg Tablet Oral 38 mg/1 Tablet Oral 300 mg / tab Tablet Oral 300 mg Syrup Oral 35 mg / 5 mL Tablet Oral Kit Oral Capsule, liquid filled Oral Powder, for solution Oral 300 mg Tablet, effervescent Oral 650 MG Tablet Oral 35 mg / tab Powder Oral Tablet, effervescent Oral 695.04 mg Tablet Oral 695 MG Tablet, effervescent Oral Syrup Oral Solution Oral Capsule, gelatin coated; kit; tablet Oral Solution, concentrate Intravenous Injection, solution, concentrate Intravenous Liquid; tablet Oral Solution Oral 650 mg Tablet, extended release Oral 35 mg / srt Tablet, extended release Oral 50 mg Liquid Oral Capsule Oral Tablet, effervescent Oral 695 mg Tablet, sugar coated Oral Capsule - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Not Available
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 36.6 mg/mL ALOGPS logP -2 ALOGPS logP -3.4 Chemaxon logS -1.1 ALOGPS pKa (Strongest Acidic) 3.39 Chemaxon pKa (Strongest Basic) -3 Chemaxon Physiological Charge -1 Chemaxon Hydrogen Acceptor Count 7 Chemaxon Hydrogen Donor Count 5 Chemaxon Polar Surface Area 141.28 Å2 Chemaxon Rotatable Bond Count 10 Chemaxon Refractivity 49.11 m3·mol-1 Chemaxon Polarizability 16.62 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
- Not Available
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Not Available
- Chromatographic Properties
Collision Cross Sections (CCS)
Not Available
Targets
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity)
- Specific Function
- double-stranded RNA binding
- Gene Name
- TFRC
- Uniprot ID
- P02786
- Uniprot Name
- Transferrin receptor protein 1
- Molecular Weight
- 84870.665 Da
References
- Hemadi M, Ha-Duong NT, El Hage Chahine JM: The mechanism of iron release from the transferrin-receptor 1 adduct. J Mol Biol. 2006 May 12;358(4):1125-36. Epub 2006 Mar 13. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif
- Specific Function
- 2-oxoglutarate-dependent dioxygenase activity
- Gene Name
- EGLN1
- Uniprot ID
- Q9GZT9
- Uniprot Name
- Egl nine homolog 1
- Molecular Weight
- 46020.585 Da
References
- Davidson TL, Chen H, Di Toro DM, D'Angelo G, Costa M: Soluble nickel inhibits HIF-prolyl-hydroxylases creating persistent hypoxic signaling in A549 cells. Mol Carcinog. 2006 Jul;45(7):479-89. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700). May play a role in smooth muscle cell contractility (PubMed:15772115). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810)
- Specific Function
- DNA-binding transcription factor binding
- Gene Name
- HDAC8
- Uniprot ID
- Q9BY41
- Uniprot Name
- Histone deacetylase 8
- Molecular Weight
- 41757.29 Da
References
- Gantt SL, Gattis SG, Fierke CA: Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry. 2006 May 16;45(19):6170-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia
- Specific Function
- hemoglobin binding
- Gene Name
- AHSP
- Uniprot ID
- Q9NZD4
- Uniprot Name
- Alpha-hemoglobin-stabilizing protein
- Molecular Weight
- 11840.325 Da
References
- Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in oxygen transport from the lung to the various peripheral tissues
- Specific Function
- heme binding
- Gene Name
- HBA1
- Uniprot ID
- P69905
- Uniprot Name
- Hemoglobin subunit alpha
- Molecular Weight
- 15257.405 Da
References
- Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly (PubMed:12785837, PubMed:24971490). Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release (PubMed:24971490). Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (PubMed:29576242). 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). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity (PubMed:15641778). May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (PubMed:11823441, PubMed:12755598). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation (PubMed:15247478). May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (PubMed:15123683, PubMed:16239244)
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- FXN
- Uniprot ID
- Q16595
- Uniprot Name
- Frataxin, mitochondrial
- Molecular Weight
- 23134.895 Da
References
- Bencze KZ, Kondapalli KC, Cook JD, McMahon S, Millan-Pacheco C, Pastor N, Stemmler TL: The structure and function of frataxin. Crit Rev Biochem Mol Biol. 2006 Sep-Oct;41(5):269-91. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity (PubMed:9003196). Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (PubMed:9003196). Also plays a role in delivery of iron to cells (By similarity). Mediates iron uptake in capsule cells of the developing kidney (By similarity). Delivery to lysosomes is mediated by the cargo receptor NCOA4 for autophagic degradation and release of iron (PubMed:24695223, PubMed:26436293)
- Specific Function
- ferric iron binding
- Gene Name
- FTH1
- Uniprot ID
- P02794
- Uniprot Name
- Ferritin heavy chain
- Molecular Weight
- 21225.47 Da
References
- Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP: High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA
- Specific Function
- 5'-3' exonuclease activity
- Gene Name
- FEN1
- Uniprot ID
- P39748
- Uniprot Name
- Flap endonuclease 1
- Molecular Weight
- 42592.635 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches. Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC
- Specific Function
- class I DNA-(apurinic or apyrimidinic site) endonuclease activity
- Gene Name
- NEIL1
- Uniprot ID
- Q96FI4
- Uniprot Name
- Endonuclease 8-like 1
- Molecular Weight
- 43683.625 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates
- Specific Function
- class I DNA-(apurinic or apyrimidinic site) endonuclease activity
- Gene Name
- NEIL2
- Uniprot ID
- Q969S2
- Uniprot Name
- Endonuclease 8-like 2
- Molecular Weight
- 36826.285 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142)
- Specific Function
- 5'-deoxyribose-5-phosphate lyase activity
- Gene Name
- POLB
- Uniprot ID
- P06746
- Uniprot Name
- DNA polymerase beta
- Molecular Weight
- 38177.34 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)
- Specific Function
- copper ion binding
- Gene Name
- CP
- Uniprot ID
- P00450
- Uniprot Name
- Ceruloplasmin
- Molecular Weight
- 122218.48 Da
References
- Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
- Specific Function
- enzyme binding
- Gene Name
- TF
- Uniprot ID
- P02787
- Uniprot Name
- Serotransferrin
- Molecular Weight
- 77049.175 Da
References
- Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]
Drug created at July 09, 2018 16:47 / Updated at October 29, 2024 14:47