Coenzyme A
Identification
- Generic Name
- Coenzyme A
- DrugBank Accession Number
- DB01992
- Background
Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, well known for it's role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it, or a thioester form of it, as a substrate. It is used as a supplement for the hypothetical treatment of acne.
- Type
- Small Molecule
- Groups
- Investigational, Nutraceutical
- Structure
- Weight
- Average: 767.534
Monoisotopic: 767.115208365 - Chemical Formula
- C21H36N7O16P3S
- Synonyms
- 3'-phosphoadenosine-(5')diphospho(4')pantatheine
- CoA
- CoA-SH
- CoASH
- HSCoA
Pharmacology
- Indication
Not Available
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- Pharmacodynamics
Not Available
- Mechanism of action
Target Actions Organism UGalactoside O-acetyltransferase Not Available Escherichia coli (strain K12) U3-hydroxy-3-methylglutaryl-coenzyme A reductase Not Available Humans UFatty acid metabolism regulator protein Not Available Shigella flexneri UHistone acetyltransferase KAT5 Not Available Humans U2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase Not Available Unknown prokaryotic organism UAcetyl-CoA acetyltransferase, cytosolic Not Available Humans UAcetyl-CoA acetyltransferase Not Available Zoogloea ramigera UStreptogramin A acetyltransferase Not Available Enterococcus faecium UCitrate synthase, mitochondrial Not Available Humans U3-oxoacyl-[acyl-carrier-protein] synthase 3 Not Available Escherichia coli (strain K12) UFormyl-coenzyme A transferase Not Available Oxalobacter formigenes UDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex Not Available Azotobacter vinelandii UPantothenate kinase Not Available Escherichia coli (strain K12) UAcetyl-coenzyme A synthetase Not Available Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) UAcyl-CoA-binding protein Not Available Humans UFormyl-coenzyme A transferase Not Available Shigella flexneri UCarnitine O-acetyltransferase Not Available Humans UCrotonobetainyl-CoA:carnitine CoA-transferase Not Available Escherichia coli (strain K12) UFormate acetyltransferase 1 Not Available Escherichia coli (strain K12) UMalate synthase G Not Available Mycobacterium tuberculosis U3-hydroxy-3-methylglutaryl-coenzyme A reductase Not Available Pseudomonas mevalonii UPhosphopantetheine adenylyltransferase Not Available Shigella flexneri UHolo-[acyl-carrier-protein] synthase Not Available Bacillus subtilis (strain 168) UProtease synthase and sporulation negative regulatory protein PAI 1 Not Available Bacillus subtilis (strain 168) UGentamicin 3'-acetyltransferase Not Available Pseudomonas aeruginosa UBifunctional protein GlmU Not Available Escherichia coli (strain K12) UAcetyl transferase Not Available Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) UUncharacterized N-acetyltransferase YvbK Not Available Bacillus subtilis (strain 168) UAminoglycoside N(6')-acetyltransferase type 1 Not Available Salmonella enteritidis UAcyl-CoA hydrolase Not Available Bacillus cereus (strain ATCC 14579 / DSM 31) UUncharacterized acyl-CoA thioester hydrolase HI_0827 Not Available Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) U3-oxoacyl-[acyl-carrier-protein] synthase 3 Not Available Streptomyces lividans UMycothiol acetyltransferase Not Available Mycobacterium tuberculosis UHistone acetyltransferase KAT2A Not Available Humans UAcyl-CoA hydrolase Not Available Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) UHistone acetyltransferase KAT2B Not Available Humans U1,4-Dihydroxy-2-naphthoyl-CoA synthase Not Available Mycobacterium tuberculosis UCitrate synthase Not Available Thermus thermophilus UAminoglycoside 2'-N-acetyltransferase Not Available Mycobacterium tuberculosis UAac(6')-Ii protein Not Available Enterococcus faecium U4'-phosphopantetheinyl transferase sfp Not Available Bacillus subtilis (strain 168) UUncharacterized protein Not Available Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) USerine acetyltransferase Not Available Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) UCitrate synthase Not Available Antarctic bacterium DS2-3R U4-hydroxybenzoyl-CoA thioesterase Not Available Arthrobacter sp. - Absorption
Not Available
- 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
Not Available
- 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.Not Available
- Food Interactions
- Not Available
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as coenzyme a and derivatives. These are derivative of vitamin B5 containing a 4'-phosphopantetheine moiety attached to a diphospho-adenosine.
- Kingdom
- Organic compounds
- Super Class
- Nucleosides, nucleotides, and analogues
- Class
- Purine nucleotides
- Sub Class
- Purine ribonucleotides
- Direct Parent
- Coenzyme A and derivatives
- Alternative Parents
- Purine ribonucleoside diphosphates / Pentose phosphates / Ribonucleoside 3'-phosphates / Glycosylamines / 6-aminopurines / Monosaccharide phosphates / Organic pyrophosphates / Aminopyrimidines and derivatives / Monoalkyl phosphates / N-substituted imidazoles show 13 more
- Substituents
- 6-aminopurine / Alcohol / Alkyl phosphate / Alkylthiol / Amine / Aminopyrimidine / Aromatic heteropolycyclic compound / Azacycle / Azole / Carboximidic acid show 37 more
- Molecular Framework
- Aromatic heteropolycyclic compounds
- External Descriptors
- adenosine 3',5'-bisphosphate (CHEBI:15346)
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- SAA04E81UX
- CAS number
- 85-61-0
- InChI Key
- RGJOEKWQDUBAIZ-IBOSZNHHSA-N
- InChI
- InChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
- IUPAC Name
- {[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid
- SMILES
- CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)[C@@H](O)C(=O)NCCC(=O)NCCS
References
- Synthesis Reference
Shigeru Ikuta, Shigeyuki Imamura, Hidehiko Ishikawa, Kazuo Matsuura, Masaki Takada, Hideo Misaki, "Process for the production of acyl-Coenzyme A oxidase." U.S. Patent US4346173, issued September, 1980.
US4346173- General References
- Not Available
- External Links
- Human Metabolome Database
- HMDB0001423
- KEGG Compound
- C00010
- PubChem Compound
- 87642
- PubChem Substance
- 46507023
- ChemSpider
- 79067
- BindingDB
- 50367033
- 1314344
- ChEBI
- 15346
- ChEMBL
- CHEMBL1213327
- ZINC
- ZINC000008551087
- PDBe Ligand
- COA
- Wikipedia
- Coenzyme_A
- PDB Entries
- 1a59 / 1aca / 1aj8 / 1bo4 / 1bq6 / 1cm0 / 1cqi / 1cqj / 1d6h / 1dlv … show 703 more
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Recruiting Treatment Instent Restenosis / Major Adverse Cardiovascular Events 1 3 Completed Treatment Hyperlipoproteinemias 2 3 Recruiting Treatment Aortic Stenosis 1 2 Completed Treatment Hyperlipoproteinemias 1 2, 3 Unknown Status Treatment Hyperlipoproteinemias 1 1, 2 Recruiting Treatment Castration Resistant Prostate Cancer 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 4.64 mg/mL ALOGPS logP -0.61 ALOGPS logP -5.9 Chemaxon logS -2.2 ALOGPS pKa (Strongest Acidic) 0.83 Chemaxon pKa (Strongest Basic) 4.89 Chemaxon Physiological Charge -4 Chemaxon Hydrogen Acceptor Count 16 Chemaxon Hydrogen Donor Count 10 Chemaxon Polar Surface Area 346.56 Å2 Chemaxon Rotatable Bond Count 18 Chemaxon Refractivity 162.74 m3·mol-1 Chemaxon Polarizability 66.08 Å3 Chemaxon Number of Rings 3 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 + 0.7401 Blood Brain Barrier - 0.7907 Caco-2 permeable - 0.7208 P-glycoprotein substrate Substrate 0.76 P-glycoprotein inhibitor I Non-inhibitor 0.6842 P-glycoprotein inhibitor II Non-inhibitor 0.9863 Renal organic cation transporter Non-inhibitor 0.9581 CYP450 2C9 substrate Non-substrate 0.8266 CYP450 2D6 substrate Non-substrate 0.7883 CYP450 3A4 substrate Substrate 0.5836 CYP450 1A2 substrate Non-inhibitor 0.8318 CYP450 2C9 inhibitor Non-inhibitor 0.8355 CYP450 2D6 inhibitor Non-inhibitor 0.842 CYP450 2C19 inhibitor Non-inhibitor 0.8115 CYP450 3A4 inhibitor Non-inhibitor 0.8203 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9333 Ames test Non AMES toxic 0.667 Carcinogenicity Non-carcinogens 0.8271 Biodegradation Not ready biodegradable 1.0 Rat acute toxicity 2.6158 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.944 hERG inhibition (predictor II) Non-inhibitor 0.6083
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
Spectrum Spectrum Type Splash Key Predicted GC-MS Spectrum - GC-MS Predicted GC-MS Not Available Predicted MS/MS Spectrum - 10V, Positive (Annotated) Predicted LC-MS/MS Not Available Predicted MS/MS Spectrum - 20V, Positive (Annotated) Predicted LC-MS/MS Not Available Predicted MS/MS Spectrum - 40V, Positive (Annotated) Predicted LC-MS/MS Not Available Predicted MS/MS Spectrum - 10V, Negative (Annotated) Predicted LC-MS/MS Not Available Predicted MS/MS Spectrum - 20V, Negative (Annotated) Predicted LC-MS/MS Not Available Predicted MS/MS Spectrum - 40V, Negative (Annotated) Predicted LC-MS/MS Not Available
Targets

- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Galactoside o-acetyltransferase activity
- Specific Function
- May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into the cell.
- Gene Name
- lacA
- Uniprot ID
- P07464
- Uniprot Name
- Galactoside O-acetyltransferase
- Molecular Weight
- 22798.89 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Nadph binding
- Specific Function
- Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including...
- Gene Name
- HMGCR
- Uniprot ID
- P04035
- Uniprot Name
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Molecular Weight
- 97475.155 Da
References
- Kind
- Protein
- Organism
- Shigella flexneri
- Pharmacological action
- Unknown
- General Function
- Transcription factor activity, sequence-specific dna binding
- Specific Function
- Multifunctional regulator of fatty acid metabolism.
- Gene Name
- fadR
- Uniprot ID
- P0A8V9
- Uniprot Name
- Fatty acid metabolism regulator protein
- Molecular Weight
- 26968.35 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transcription coactivator activity
- Specific Function
- Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This m...
- Gene Name
- KAT5
- Uniprot ID
- Q92993
- Uniprot Name
- Histone acetyltransferase KAT5
- Molecular Weight
- 58581.45 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]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Unknown prokaryotic organism
- Pharmacological action
- Unknown
- General Function
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate n-succinyltransferase activity
- Specific Function
- Not Available
- Gene Name
- dapD
- Uniprot ID
- P56220
- Uniprot Name
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Molecular Weight
- 29886.885 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Acetyl-coa c-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- ACAT2
- Uniprot ID
- Q9BWD1
- Uniprot Name
- Acetyl-CoA acetyltransferase, cytosolic
- Molecular Weight
- 41350.5 Da
References
- Kind
- Protein
- Organism
- Zoogloea ramigera
- Pharmacological action
- Unknown
- General Function
- Acetyl-coa c-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- phbA
- Uniprot ID
- P07097
- Uniprot Name
- Acetyl-CoA acetyltransferase
- Molecular Weight
- 40472.955 Da
References
- Kind
- Protein
- Organism
- Enterococcus faecium
- Pharmacological action
- Unknown
- General Function
- Transferase activity, transferring acyl groups
- Specific Function
- Inactivates the A compounds of streptogramin antibiotics by acetylation, thus providing resistance to these antibiotics.
- Gene Name
- vatD
- Uniprot ID
- P50870
- Uniprot Name
- Streptogramin A acetyltransferase
- Molecular Weight
- 23649.22 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Poly(a) rna binding
- Specific Function
- Not Available
- Gene Name
- CS
- Uniprot ID
- O75390
- Uniprot Name
- Citrate synthase, mitochondrial
- Molecular Weight
- 51712.025 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]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Beta-ketoacyl-acyl-carrier-protein synthase iii activity
- Specific Function
- Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid...
- Gene Name
- fabH
- Uniprot ID
- P0A6R0
- Uniprot Name
- 3-oxoacyl-[acyl-carrier-protein] synthase 3
- Molecular Weight
- 33514.78 Da
References
- Kind
- Protein
- Organism
- Oxalobacter formigenes
- Pharmacological action
- Unknown
- General Function
- Formyl-coa transferase activity
- Specific Function
- Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it r...
- Gene Name
- frc
- Uniprot ID
- O06644
- Uniprot Name
- Formyl-CoA:oxalate CoA-transferase
- Molecular Weight
- 47326.775 Da
References
- Kind
- Protein
- Organism
- Azotobacter vinelandii
- Pharmacological action
- Unknown
- General Function
- Dihydrolipoyllysine-residue acetyltransferase activity
- Specific Function
- The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihy...
- Gene Name
- Not Available
- Uniprot ID
- P10802
- Uniprot Name
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Molecular Weight
- 65044.135 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Pantothenate kinase activity
- Specific Function
- Not Available
- Gene Name
- coaA
- Uniprot ID
- P0A6I3
- Uniprot Name
- Pantothenate kinase
- Molecular Weight
- 36359.435 Da
References
- Kind
- Protein
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Pharmacological action
- Unknown
- General Function
- Metal ion binding
- Specific Function
- Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half react...
- Gene Name
- acs
- Uniprot ID
- Q8ZKF6
- Uniprot Name
- Acetyl-coenzyme A synthetase
- Molecular Weight
- 72152.085 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein dimerization activity
- Specific Function
- Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (B...
- Gene Name
- DBI
- Uniprot ID
- P07108
- Uniprot Name
- Acyl-CoA-binding protein
- Molecular Weight
- 10044.37 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]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Shigella flexneri
- Pharmacological action
- Unknown
- General Function
- Formyl-coa transferase activity
- Specific Function
- Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl...
- Gene Name
- frc
- Uniprot ID
- P69903
- Uniprot Name
- Formyl-CoA:oxalate CoA-transferase
- Molecular Weight
- 45827.825 Da
References
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Receptor binding
- Specific Function
- Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of ...
- Gene Name
- CRAT
- Uniprot ID
- P43155
- Uniprot Name
- Carnitine O-acetyltransferase
- Molecular Weight
- 70857.055 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]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Coa-transferase activity
- Specific Function
- Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transf...
- Gene Name
- caiB
- Uniprot ID
- P31572
- Uniprot Name
- L-carnitine CoA-transferase
- Molecular Weight
- 45126.41 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Formate c-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- pflB
- Uniprot ID
- P09373
- Uniprot Name
- Formate acetyltransferase 1
- Molecular Weight
- 85356.555 Da
References
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- General Function
- Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
- Specific Function
- Coenzyme binding
- Gene Name
- glcB
- Uniprot ID
- P9WK17
- Uniprot Name
- Malate synthase G
- Molecular Weight
- 80402.24 Da
References
- Kind
- Protein
- Organism
- Pseudomonas mevalonii
- Pharmacological action
- Unknown
- General Function
- Hydroxymethylglutaryl-coa reductase activity
- Specific Function
- P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.
- Gene Name
- mvaA
- Uniprot ID
- P13702
- Uniprot Name
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Molecular Weight
- 45589.915 Da
References
- Kind
- Protein
- Organism
- Shigella flexneri
- Pharmacological action
- Unknown
- General Function
- Pantetheine-phosphate adenylyltransferase activity
- Specific Function
- Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
- Gene Name
- coaD
- Uniprot ID
- P0A6I8
- Uniprot Name
- Phosphopantetheine adenylyltransferase
- Molecular Weight
- 17836.51 Da
References
- Kind
- Protein
- Organism
- Bacillus subtilis (strain 168)
- Pharmacological action
- Unknown
- General Function
- Magnesium ion binding
- Specific Function
- Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl c...
- Gene Name
- acpS
- Uniprot ID
- P96618
- Uniprot Name
- Holo-[acyl-carrier-protein] synthase
- Molecular Weight
- 13717.63 Da
References
- Kind
- Protein
- Organism
- Bacillus subtilis (strain 168)
- Pharmacological action
- Unknown
- General Function
- Diamine n-acetyltransferase activity
- Specific Function
- Involved in the protection against polyamine toxicity by regulating their concentration. Also could be involved in the negative control of sporulation as well as production of degradative enzymes s...
- Gene Name
- paiA
- Uniprot ID
- P21340
- Uniprot Name
- Spermidine/spermine N(1)-acetyltransferase
- Molecular Weight
- 20014.605 Da
References
- Kind
- Protein
- Organism
- Pseudomonas aeruginosa
- Pharmacological action
- Unknown
- General Function
- Aminoglycoside 3-n-acetyltransferase activity
- Specific Function
- Responsible for gentamicin resistance and has a limited substrate range.
- Gene Name
- aacC1
- Uniprot ID
- P23181
- Uniprot Name
- Gentamicin 3-N-acetyltransferase
- Molecular Weight
- 19441.81 Da
References
- Kind
- Protein
- Organism
- Escherichia coli (strain K12)
- Pharmacological action
- Unknown
- General Function
- Udp-n-acetylglucosamine diphosphorylase activity
- Specific Function
- Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl co...
- Gene Name
- glmU
- Uniprot ID
- P0ACC7
- Uniprot Name
- Bifunctional protein GlmU
- Molecular Weight
- 49189.765 Da
References
- Kind
- Protein
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Pharmacological action
- Unknown
- General Function
- N-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- rimL
- Uniprot ID
- Q8ZPC0
- Uniprot Name
- Acetyl transferase
- Molecular Weight
- 20605.37 Da
- Kind
- Protein
- Organism
- Bacillus subtilis (strain 168)
- Pharmacological action
- Unknown
- General Function
- N-acetyltransferase activity
- Specific Function
- Probable N-acetyltransferase.
- Gene Name
- yvbK
- Uniprot ID
- O32248
- Uniprot Name
- Uncharacterized N-acetyltransferase YvbK
- Molecular Weight
- 17745.09 Da
- Kind
- Protein
- Organism
- Salmonella enteritidis
- Pharmacological action
- Unknown
- General Function
- Protein homodimerization activity
- Specific Function
- Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin...
- Gene Name
- Not Available
- Uniprot ID
- Q9R381
- Uniprot Name
- Aminoglycoside N(6')-acetyltransferase type 1
- Molecular Weight
- 16361.42 Da
- Kind
- Protein
- Organism
- Bacillus cereus (strain ATCC 14579 / DSM 31)
- Pharmacological action
- Unknown
- General Function
- Metal ion binding
- Specific Function
- Not Available
- Gene Name
- Not Available
- Uniprot ID
- Q81EE4
- Uniprot Name
- Acyl-CoA hydrolase
- Molecular Weight
- 19313.01 Da
- Kind
- Protein
- Organism
- Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
- Pharmacological action
- Unknown
- General Function
- Hydrolase activity
- Specific Function
- Not Available
- Gene Name
- Not Available
- Uniprot ID
- P44886
- Uniprot Name
- Uncharacterized acyl-CoA thioester hydrolase HI_0827
- Molecular Weight
- 16763.305 Da
- Kind
- Protein
- Organism
- Streptomyces lividans
- Pharmacological action
- Unknown
- General Function
- Beta-ketoacyl-acyl-carrier-protein synthase iii activity
- Specific Function
- Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid...
- Gene Name
- fabH
- Uniprot ID
- Q9F6D4
- Uniprot Name
- 3-oxoacyl-[acyl-carrier-protein] synthase 3
- Molecular Weight
- 35391.78 Da
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- General Function
- Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
- Specific Function
- Mycothiol synthase activity
- Gene Name
- mshD
- Uniprot ID
- P9WJM7
- Uniprot Name
- Mycothiol acetyltransferase
- Molecular Weight
- 33598.82 Da
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transcription factor binding
- Specific Function
- Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone a...
- Gene Name
- KAT2A
- Uniprot ID
- Q92830
- Uniprot Name
- Histone acetyltransferase KAT2A
- Molecular Weight
- 93924.72 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
- Pharmacological action
- Unknown
- General Function
- Hydrolase activity
- Specific Function
- Not Available
- Gene Name
- Not Available
- Uniprot ID
- Q9KEQ1
- Uniprot Name
- Acyl-CoA hydrolase
- Molecular Weight
- 17327.56 Da
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transcription factor binding
- Specific Function
- Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome cor...
- Gene Name
- KAT2B
- Uniprot ID
- Q92831
- Uniprot Name
- Histone acetyltransferase KAT2B
- Molecular Weight
- 93012.295 Da
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- General Function
- Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
- Specific Function
- 1,4-dihydroxy-2-naphthoyl-coa synthase activity
- Gene Name
- menB
- Uniprot ID
- P9WNP5
- Uniprot Name
- 1,4-dihydroxy-2-naphthoyl-CoA synthase
- Molecular Weight
- 34688.715 Da
- Kind
- Protein
- Organism
- Thermus thermophilus
- Pharmacological action
- Unknown
- General Function
- Transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
- Specific Function
- Not Available
- Gene Name
- cit
- Uniprot ID
- Q9LCX9
- Uniprot Name
- Citrate synthase
- Molecular Weight
- 42322.13 Da
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- General Function
- May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system (PubMed:9159528).
- Specific Function
- Aminoglycoside 2'-n-acetyltransferase activity
- Gene Name
- aac
- Uniprot ID
- P9WQG9
- Uniprot Name
- Aminoglycoside 2'-N-acetyltransferase
- Molecular Weight
- 20037.53 Da
- Kind
- Protein
- Organism
- Enterococcus faecium
- Pharmacological action
- Unknown
- General Function
- N-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- aac(6')-Ii
- Uniprot ID
- Q47764
- Uniprot Name
- Aac(6')-Ii protein
- Molecular Weight
- 20679.115 Da
- Kind
- Protein
- Organism
- Bacillus subtilis (strain 168)
- Pharmacological action
- Unknown
- General Function
- Magnesium ion binding
- Specific Function
- Activates the seven peptidyl carrier protein (PCP) domains of surfactin synthase SRF1/2/3 by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue. Required for cel...
- Gene Name
- sfp
- Uniprot ID
- P39135
- Uniprot Name
- 4'-phosphopantetheinyl transferase sfp
- Molecular Weight
- 26167.415 Da
- Kind
- Protein
- Organism
- Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
- Pharmacological action
- Unknown
- General Function
- N-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- Not Available
- Uniprot ID
- Q9HYX1
- Uniprot Name
- Uncharacterized protein
- Molecular Weight
- 21901.01 Da
- Kind
- Protein
- Organism
- Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
- Pharmacological action
- Unknown
- General Function
- Serine o-acetyltransferase activity
- Specific Function
- Not Available
- Gene Name
- cysE
- Uniprot ID
- P43886
- Uniprot Name
- Serine acetyltransferase
- Molecular Weight
- 29166.2 Da
- Kind
- Protein
- Organism
- Antarctic bacterium DS2-3R
- Pharmacological action
- Unknown
- General Function
- Citrate synthase activity
- Specific Function
- Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes...
- Gene Name
- gltA
- Uniprot ID
- O34002
- Uniprot Name
- 2-methylcitrate synthase
- Molecular Weight
- 41832.0 Da
- Kind
- Protein
- Organism
- Arthrobacter sp.
- Pharmacological action
- Unknown
- General Function
- 4-hydroxybenzoyl-coa thioesterase activity
- Specific Function
- Not Available
- Gene Name
- fcbC
- Uniprot ID
- Q04416
- Uniprot Name
- 4-hydroxybenzoyl-CoA thioesterase
- Molecular Weight
- 16394.32 Da
Enzymes
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- Actions
- Ligand
- General Function
- May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system (PubMed:9159528).
- Specific Function
- Aminoglycoside 2'-n-acetyltransferase activity
- Gene Name
- aac
- Uniprot ID
- P9WQG9
- Uniprot Name
- Aminoglycoside 2'-N-acetyltransferase
- Molecular Weight
- 20037.53 Da
References
- Vetting MW, Park CH, Hegde SS, Jacoby GA, Hooper DC, Blanchard JS: Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6')-Ib and its bifunctional, fluoroquinolone-active AAC(6')-Ib-cr variant. Biochemistry. 2008 Sep 16;47(37):9825-35. doi: 10.1021/bi800664x. Epub 2008 Aug 19. [Article]
- Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL: Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat Struct Biol. 2002 Sep;9(9):653-8. [Article]
Drug created at June 13, 2005 13:24 / Updated at June 12, 2020 16:52