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Record Information
StatusExpected but not Quantified
Creation Date2006-05-22 14:17:31 UTC
Update Date2020-02-26 21:23:43 UTC
Secondary Accession Numbers
  • HMDB02009
Metabolite Identification
Common NameCrotonoyl-CoA
DescriptionCrotonoyl-CoA is an important component in several metabolic pathways, notably fatty acid and amino acid metabolism. It is the substrate of a group of enzymes acyl-Coenzyme A oxidases 1, 2, 3 (E.C.: corresponding to palmitoyl, branched chain, and pristanoyl, respectively, in the peroxisomal fatty acid beta-oxidation, producing hydrogen peroxide. Abnormality of this group of enzymes is linked to coma, dehydration, diabetes, fatty liver, hyperinsulinemia, hyperlipidemia, and leukodystrophy. It is also a substrate of a group of enzymes called acyl-Coenzyme A dehydrogenase (E.C.:1.3.99-, including, in the metabolism of fatty acids or branched chain amino acids in the mitochondria (Rozen et al., 1994). Acyl-Coenzyme A dehydrogenase ( has shown to contribute to kidney-associated diseases, such as adrenogential syndrome, kidney failure, kidney tubular necrosis, homocystinuria, as well as other diseases including cretinism, encephalopathy, hypoglycemia, medium chain acyl-CoA dehydrogenase deficiency. The gene (ACADS) also plays a role in theta oscillation during sleep. In addition, crotonoyl-CoA is the substrate of enoyl coenzyme A hydratase (E.C. in the mitochondria during lysine degradation and tryptophan metabolism, benzoate degradation via CoA ligation; in contrast it is the product of this enzyme in the butanoate metabolism. Moreover, it is produced from multiple enzymes in the butanoate metabolism pathway, including 3-Hydroxybutyryl-CoA dehydratase (E.C.:, glutaconyl-CoA decarboxylase (E.C.:, vinylacetyl-CoA Δ-isomerase (E.C.:, and trans-2-enoyl-CoA reductase (NAD+) (E.C.: In lysine degradation and tryptophan metabolism, crotonoyl CoA is produced by glutaryl-Coenzyme A dehydrogenase (E.C.: lysine and tryptophan metabolic pathway. This enzyme is linked to type-1glutaric aciduria, metabolic diseases, movement disorders, myelinopathy, and nervous system diseases.
2-Butenoyl-coenzyme AHMDB
But-2-enoyl-coenzyme AHMDB
Crotonyl-coenzyme AHMDB
S-But-2-enoylcoenzyme AHMDB
trans-But-2-enoyl-coenzyme AHMDB
Chemical FormulaC25H40N7O17P3S
Average Molecular Weight835.608
Monoisotopic Molecular Weight835.141423115
IUPAC Name{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-2-{[({[(3-{[2-({2-[(2E)-but-2-enoylsulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}-3-hydroxy-2,2-dimethylpropoxy)(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl)oxy]methyl}-4-hydroxyoxolan-3-yl]oxy}phosphonic acid
Traditional Name[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-2-({[(3-{[2-({2-[(2E)-but-2-enoylsulfanyl]ethyl}carbamoyl)ethyl]carbamoyl}-3-hydroxy-2,2-dimethylpropoxy(hydroxy)phosphoryl)oxy(hydroxy)phosphoryl]oxy}methyl)-4-hydroxyoxolan-3-yl]oxyphosphonic acid
CAS Registry Number102680-35-3
InChI Identifier
Chemical Taxonomy
Description belongs to the class of organic compounds known as 2-enoyl coas. These are organic compounds containing a coenzyme A substructure linked to a 2-enoyl chain.
KingdomOrganic compounds
Super ClassLipids and lipid-like molecules
ClassFatty Acyls
Sub ClassFatty acyl thioesters
Direct Parent2-enoyl CoAs
Alternative Parents
  • Coenzyme a or derivatives
  • Purine ribonucleoside 3',5'-bisphosphate
  • Purine ribonucleoside bisphosphate
  • Purine ribonucleoside diphosphate
  • Ribonucleoside 3'-phosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Beta amino acid or derivatives
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • Pentose monosaccharide
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Aminopyrimidine
  • Imidolactam
  • N-acyl-amine
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Monosaccharide
  • Pyrimidine
  • Alkyl phosphate
  • Fatty amide
  • Phosphoric acid ester
  • Tetrahydrofuran
  • Imidazole
  • Azole
  • Heteroaromatic compound
  • Carbothioic s-ester
  • Secondary alcohol
  • Thiocarboxylic acid ester
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Amino acid or derivatives
  • Sulfenyl compound
  • Thiocarboxylic acid or derivatives
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Carboxylic acid derivative
  • Organosulfur compound
  • Organic oxygen compound
  • Hydrocarbon derivative
  • Carbonyl group
  • Organic nitrogen compound
  • Primary amine
  • Organopnictogen compound
  • Organic oxide
  • Organooxygen compound
  • Organonitrogen compound
  • Alcohol
  • Amine
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic 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 Solubility3.67 g/LALOGPS
pKa (Strongest Acidic)0.83ChemAxon
pKa (Strongest Basic)4.95ChemAxon
Physiological Charge-4ChemAxon
Hydrogen Acceptor Count17ChemAxon
Hydrogen Donor Count9ChemAxon
Polar Surface Area363.63 ŲChemAxon
Rotatable Bond Count21ChemAxon
Refractivity182.53 m³·mol⁻¹ChemAxon
Polarizability73.19 ųChemAxon
Number of Rings3ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash KeyView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-1901000120-017aeb03ebd91e701248Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-1912000000-1727557fedacd67ecc0cSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-2911000000-476bc5abc1a151d6d872Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00lr-7930140550-fee62adcd8bdf1cc9ba2Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00o0-6910100010-21179bc614a07310997eSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-057i-6900100000-973d74ae97aba1d99ab1Spectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Membrane
  • Mitochondria
  • Peroxisome
Biospecimen LocationsNot Available
Tissue Locations
  • Liver
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
FoodDB IDFDB022792
KNApSAcK IDNot Available
Chemspider ID4444072
KEGG Compound IDC00877
BioCyc IDNot Available
BiGG ID36265
Wikipedia LinkNot Available
PubChem Compound5280381
PDB IDNot Available
ChEBI ID15473
Food Biomarker OntologyNot Available
VMH IDNot Available
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Kalousek F, Darigo MD, Rosenberg LE: Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits. J Biol Chem. 1980 Jan 10;255(1):60-5. [PubMed:6765947 ]
  2. Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ: Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry. 2004 Aug 3;43(30):9674-84. [PubMed:15274622 ]
  3. Dwyer TM, Rao KS, Westover JB, Kim JJ, Frerman FE: The function of Arg-94 in the oxidation and decarboxylation of glutaryl-CoA by human glutaryl-CoA dehydrogenase. J Biol Chem. 2001 Jan 5;276(1):133-8. [PubMed:11024031 ]
  4. Babidge W, Millard S, Roediger W: Sulfides impair short chain fatty acid beta-oxidation at acyl-CoA dehydrogenase level in colonocytes: implications for ulcerative colitis. Mol Cell Biochem. 1998 Apr;181(1-2):117-24. [PubMed:9562248 ]
  5. Lenich AC, Goodman SI: The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver. J Biol Chem. 1986 Mar 25;261(9):4090-6. [PubMed:3081514 ]
  6. Gregersen N, Brandt NJ, Christensen E, Gron I, Rasmussen K, Brandt S: Glutaric aciduria: clinical and laboratory findings in two brothers. J Pediatr. 1977 May;90(5):740-5. [PubMed:853337 ]
  7. Hyman DB, Tanaka K: Specific glutaryl-CoA dehydrogenating activity is deficient in cultured fibroblasts from glutaric aciduria patients. J Clin Invest. 1984 Mar;73(3):778-84. [PubMed:6423663 ]
  8. Hodgins MB: Possible mechanisms of androgen resistance in 5 alpha-reductase deficiency: implications for the physiological roles of 5 alpha-reductases. J Steroid Biochem. 1983 Jul;19(1B):555-9. [PubMed:6887883 ]
  9. Saenger AK, Nguyen TV, Vockley J, Stankovich MT: Thermodynamic regulation of human short-chain acyl-CoA dehydrogenase by substrate and product binding. Biochemistry. 2005 Dec 13;44(49):16043-53. [PubMed:16331964 ]
  10. Finocchiaro G, Ito M, Tanaka K: Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver. J Biol Chem. 1987 Jun 15;262(17):7982-9. [PubMed:3597357 ]

Only showing the first 10 proteins. There are 114 proteins in total.


General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Abolishes BNIP3-mediated apoptosis and mitochondrial damage.
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:
General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in oxidoreductase activity
Specific function:
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
Uniprot ID:
Molecular weight:
Butyryl-CoA + electron-transfer flavoprotein → Crotonoyl-CoA + reduced electron-transfer flavoproteindetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
This enzyme is specific for acyl chain lengths of 4 to 16.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.
Gene Name:
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General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
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
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Molecular weight:

Only showing the first 10 proteins. There are 114 proteins in total.