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Record Information
StatusExpected but not Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2021-09-14 14:59:15 UTC
Secondary Accession Numbers
  • HMDB01206
Metabolite Identification
Common NameAcetyl-CoA
DescriptionAcetyl-CoA, also known as acetyl coenzyme A or accoa, belongs to the class of organic compounds known as o-glucuronides. These are glucuronides in which the aglycone is linked to the carbohydrate unit through an O-glycosidic bond. Thus, acetyl-CoA is considered to be a fatty ester lipid molecule. Acetyl-CoA is a very hydrophobic molecule, practically insoluble (in water), and relatively neutral. Acetyl-CoA exists in all living species, ranging from bacteria to humans. In humans, acetyl-CoA is involved in the metabolic disorder called the long chain acyl-coa dehydrogenase deficiency (lcad) pathway. An acyl-CoA having acetyl as its S-acetyl component. Outside of the human body, Acetyl-CoA has been detected, but not quantified in, several different foods, such as amaranths, lemon verbena, strawberries, lingonberries, and carobs. This could make acetyl-CoA a potential biomarker for the consumption of these foods.
Acetyl coenzyme AChEBI
S-Acetyl-coenzyme AChEBI
Ac-coenzyme AHMDB
Ac-S-coenzyme AHMDB
Acetyl-coenzyme AHMDB
Acetyl-S-coenzyme AHMDB
Acetylcoenzyme AHMDB
S-Acetate CoAHMDB
S-Acetate coenzyme AHMDB
S-Acetyl coenzyme AHMDB
coenzyme A, AcetylHMDB
Acetyl CoAHMDB
CoA, AcetylHMDB
Chemical FormulaC23H38N7O17P3S
Average Molecular Weight809.571
Monoisotopic Molecular Weight809.125773051
IUPAC Name{[(2R,3S,4R,5R)-2-({[({[(3R)-3-[(2-{[2-(acetylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy](hydroxy)phosphoryl}oxy)(hydroxy)phosphoryl]oxy}methyl)-5-(6-amino-9H-purin-9-yl)-4-hydroxyoxolan-3-yl]oxy}phosphonic acid
Traditional Nameacetyl-CoA
CAS Registry Number72-89-9
InChI Identifier
Chemical Taxonomy
Description Belongs to the class of organic compounds known as o-glucuronides. These are glucuronides in which the aglycone is linked to the carbohydrate unit through an O-glycosidic bond.
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassCarbohydrates and carbohydrate conjugates
Direct ParentO-glucuronides
Alternative Parents
  • 1-o-glucuronide
  • O-glucuronide
  • Glycosyl compound
  • O-glycosyl compound
  • Pyrrolidinylpyridine
  • Alkaloid or derivatives
  • Beta-hydroxy acid
  • Hydroxy acid
  • Monosaccharide
  • Oxane
  • Pyran
  • Pyridine
  • Pyrrolidone
  • 2-pyrrolidone
  • N-alkylpyrrolidine
  • Pyrrolidine
  • Tertiary carboxylic acid amide
  • Heteroaromatic compound
  • Secondary alcohol
  • Carboxamide group
  • Lactam
  • Azacycle
  • Organoheterocyclic compound
  • Carboxylic acid
  • Oxacycle
  • Carboxylic acid derivative
  • Polyol
  • Acetal
  • Monocarboxylic acid or derivatives
  • Organopnictogen compound
  • Organic nitrogen compound
  • Carbonyl group
  • Alcohol
  • Organic oxide
  • Hydrocarbon derivative
  • Organonitrogen compound
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External DescriptorsNot Available

Route of exposure:


Biological location:


Naturally occurring process:


Industrial application:

Biological role:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
Water Solubility4.3 g/LALOGPS
pKa (Strongest Acidic)0.82ChemAxon
pKa (Strongest Basic)4.01ChemAxon
Physiological Charge-4ChemAxon
Hydrogen Acceptor Count17ChemAxon
Hydrogen Donor Count9ChemAxon
Polar Surface Area363.63 ŲChemAxon
Rotatable Bond Count20ChemAxon
Refractivity172.21 m³·mol⁻¹ChemAxon
Polarizability70.62 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon


Spectrum TypeDescriptionSplash KeyDeposition DateView
MSMass Spectrum (Electron Ionization)splash10-0005-9122344100-644f231d6328f99749182021-09-05View Spectrum


Spectrum TypeDescriptionSplash KeyDeposition DateView
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, positivesplash10-0fb9-0035910000-cecfaf54528fc3ef9f002020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, positivesplash10-0ufr-0005900000-491971eb7a5c2b3275542020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-0a4i-0900000000-1b259612c3897ed851f02020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-08i0-0001901200-8d4f5232c27f2875cf8b2020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-08i0-0000901200-33f8d3ced8c83336df0c2020-07-21View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-1901000300-57c996f08055dba75dd72015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0902000000-dffb00601bfc54014ae42015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-2901000000-155f0890adf4c76dca852015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0arr-6820231930-984ae0f98e0d17e4a7fc2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-003r-3910100000-87da6b6d742efbc6e74a2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-057i-5900000000-8701decc3b2311880b972015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0a4i-0000000090-fd17a06b039262f964632021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-05vx-9100203430-9e39d5da3afdd3a15f912021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-00b9-9101401200-719cb55952a06d96d3c82021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-0000000090-02de4c2ee732e6d50b2d2021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-01p9-1901002440-79ee9e61778bd08a750f2021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0udi-0209000000-84f7f68fc2e83a8ae7702021-09-07View Spectrum
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Membrane
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Golgi apparatus
  • Peroxisome
Biospecimen LocationsNot Available
Tissue Locations
  • Adipose Tissue
  • Brain
  • Platelet
  • Prostate
  • Skeletal Muscle
  • Spleen
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB022491
KNApSAcK IDC00007259
Chemspider ID392413
KEGG Compound IDC00024
BiGG ID33558
Wikipedia LinkAcetyl-CoA
PubChem Compound444493
PDB IDNot Available
ChEBI ID15351
Food Biomarker OntologyNot Available
MarkerDB IDNot Available
Synthesis ReferenceTucek, S. The synthesis of acetyl coenzyme A and acetylcholine from citrate and acetate in the nerve endings of mammalian brain. Biochimica et Biophysica Acta, General Subjects (1966), 117(1), 278-80.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Michno A, Skibowska A, Raszeja-Specht A, Cwikowska J, Szutowicz A: The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus. Metabolism. 2004 Jan;53(1):66-72. [PubMed:14681844 ]
  2. Al-Buheissi SZ, Patel HR, Meinl W, Hewer A, Bryan RL, Glatt H, Miller RA, Phillips DH: N-Acetyltransferase and sulfotransferase activity in human prostate: potential for carcinogen activation. Pharmacogenet Genomics. 2006 Jun;16(6):391-9. [PubMed:16708048 ]
  3. Griffin MJ, Sul HS: Insulin regulation of fatty acid synthase gene transcription: roles of USF and SREBP-1c. IUBMB Life. 2004 Oct;56(10):595-600. [PubMed:15814457 ]
  4. Putman CT, Spriet LL, Hultman E, Dyck DJ, Heigenhauser GJ: Skeletal muscle pyruvate dehydrogenase activity during acetate infusion in humans. Am J Physiol. 1995 May;268(5 Pt 1):E1007-17. [PubMed:7762627 ]
  5. Szutowicz A, Tomaszewicz M, Jankowska A, Madziar B, Bielarczyk H: [Mechanisms of selective vulnerability of cholinergic neurons to neurotoxic stimuli]. Postepy Hig Med Dosw. 1999;53(2):263-75. [PubMed:10355292 ]
  6. Ingebretsen OC, Bakken AM, Farstad M: The content of coenzyme A, acetyl-CoA and long-chain acyl-CoA in human blood platelets. Clin Chim Acta. 1982 Dec 23;126(3):307-13. [PubMed:7151284 ]
  7. Michno A, Raszeja-Specht A, Jankowska-Kulawy A, Pawelczyk T, Szutowicz A: Effect of L-carnitine on acetyl-CoA content and activity of blood platelets in healthy and diabetic persons. Clin Chem. 2005 Sep;51(9):1673-82. Epub 2005 Jul 14. [PubMed:16020499 ]
  8. Constantin-Teodosiu D, Peirce NS, Fox J, Greenhaff PL: Muscle pyruvate availability can limit the flux, but not activation, of the pyruvate dehydrogenase complex during submaximal exercise in humans. J Physiol. 2004 Dec 1;561(Pt 2):647-55. Epub 2004 Oct 7. [PubMed:15579544 ]
  9. Crystal HA, Davies P: Cortical substance P-like immunoreactivity in cases of Alzheimer's disease and senile dementia of the Alzheimer type. J Neurochem. 1982 Jun;38(6):1781-4. [PubMed:6176686 ]
  10. Wysocki SJ, Wilkinson SP, Hahnel R, Wong CY, Panegyres PK: 3-Hydroxy-3-methylglutaric aciduria, combined with 3-methylglutaconic aciduria. Clin Chim Acta. 1976 Aug 2;70(3):399-406. [PubMed:947633 ]
  11. Evans MK, Savasi I, Heigenhauser GJ, Spriet LL: Effects of acetate infusion and hyperoxia on muscle substrate phosphorylation after onset of moderate exercise. Am J Physiol Endocrinol Metab. 2001 Dec;281(6):E1144-50. [PubMed:11701427 ]
  12. Peters SJ: Regulation of PDH activity and isoform expression: diet and exercise. Biochem Soc Trans. 2003 Dec;31(Pt 6):1274-80. [PubMed:14641042 ]
  13. Roe CR, Sweetman L, Roe DS, David F, Brunengraber H: Treatment of cardiomyopathy and rhabdomyolysis in long-chain fat oxidation disorders using an anaplerotic odd-chain triglyceride. J Clin Invest. 2002 Jul;110(2):259-69. [PubMed:12122118 ]
  14. Skibowska A, Raszeja-Specht A, Szutowicz A: Platelet function and acetyl-coenzyme A metabolism in type 1 diabetes mellitus. Clin Chem Lab Med. 2003 Sep;41(9):1136-43. [PubMed:14598862 ]
  15. Girard J: [Contribution of free fatty acids to impairment of insulin secretion and action. mechanism of beta-cell lipotoxicity]. Med Sci (Paris). 2005 Dec;21 Spec No:19-25. [PubMed:16598900 ]
  16. Szutowicz A, Jankowska A, Tomaszewicz M: [Disturbances of glucose metabolism in epilepsy and other neurodegenerative diseases]. Neurol Neurochir Pol. 2000;34 Suppl 8:59-66. [PubMed:11780590 ]
  17. Spriet LL, MacLean DA, Dyck DJ, Hultman E, Cederblad G, Graham TE: Caffeine ingestion and muscle metabolism during prolonged exercise in humans. Am J Physiol. 1992 Jun;262(6 Pt 1):E891-8. [PubMed:1616022 ]
  18. Constantin-Teodosiu D, Carlin JI, Cederblad G, Harris RC, Hultman E: Acetyl group accumulation and pyruvate dehydrogenase activity in human muscle during incremental exercise. Acta Physiol Scand. 1991 Dec;143(4):367-72. [PubMed:1815472 ]
  19. Boden G, Jadali F, White J, Liang Y, Mozzoli M, Chen X, Coleman E, Smith C: Effects of fat on insulin-stimulated carbohydrate metabolism in normal men. J Clin Invest. 1991 Sep;88(3):960-6. [PubMed:1885781 ]
  20. Blank ML, Smith ZL, Fitzgerald V, Snyder F: The CoA-independent transacylase in PAF biosynthesis: tissue distribution and molecular species selectivity. Biochim Biophys Acta. 1995 Feb 9;1254(3):295-301. [PubMed:7857969 ]

Only showing the first 10 proteins. There are 179 proteins in total.


General function:
Involved in catalytic activity
Specific function:
Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism.
Gene Name:
Uniprot ID:
Molecular weight:
3-Hydroxy-3-methylglutaryl-CoA → Acetyl-CoA + Acetoacetic aciddetails
General function:
Involved in ATP citrate synthase activity
Specific function:
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.
Gene Name:
Uniprot ID:
Molecular weight:
ADP + Phosphate + Acetyl-CoA + Oxalacetic acid → Adenosine triphosphate + Citric acid + Coenzyme Adetails
Adenosine triphosphate + Citric acid + Coenzyme A → ADP + Phosphate + Acetyl-CoA + Oxalacetic aciddetails
General function:
Involved in transcription cofactor activity
Specific function:
Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity.
Gene Name:
Uniprot ID:
Molecular weight:
Acetyl-CoA + [histone] → Coenzyme A + acetyl-[histone]details
General function:
Involved in catalytic activity
Specific 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.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
Acetyl-CoA → Coenzyme A + Acetoacetyl-CoAdetails
Acetyl-CoA + Butyryl-CoA → Coenzyme A + 3-Oxohexanoyl-CoAdetails
General function:
Involved in transcription cofactor activity
Specific function:
Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300.
Gene Name:
Uniprot ID:
Molecular weight:
Acetyl-CoA + [histone] → Coenzyme A + acetyl-[histone]details
General function:
Involved in N-acetyltransferase activity
Specific function:
Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine.
Gene Name:
Uniprot ID:
Molecular weight:
Acetyl-CoA + an alkane-alpha,omega-diamine → Coenzyme A + an N-acetyldiaminedetails
Acetyl-CoA + Putrescine → Coenzyme A + N-Acetylputrescinedetails
General function:
Involved in malonyl-CoA decarboxylase activity
Specific function:
Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids.
Gene Name:
Uniprot ID:
Molecular weight:
Malonyl-CoA → Acetyl-CoA + CO(2)details
Malonyl-CoA → Acetyl-CoA + Carbon dioxidedetails
General function:
Involved in acetyl-CoA carboxylase activity
Specific function:
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Gene Name:
Uniprot ID:
Molecular weight:
Adenosine triphosphate + Acetyl-CoA + Hydrogen carbonate → ADP + Phosphate + Malonyl-CoAdetails
Acetyl-CoA + Carboxybiotin-carboxyl-carrier protein → Malonyl-CoA + Holo-[carboxylase]details
General function:
Involved in catalytic activity
Specific function:
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Gene Name:
Uniprot ID:
Molecular weight:


General function:
Lipid transport and metabolism
Specific function:
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids
Gene Name:
Uniprot ID:
Molecular weight:

Only showing the first 10 proteins. There are 179 proteins in total.