You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Record Information
Version4.0
StatusExpected but not Quantified
Creation Date2006-05-22 14:17:31 UTC
Update Date2020-06-15 17:04:52 UTC
HMDB IDHMDB0002009
Secondary Accession Numbers
  • HMDB0059627
  • HMDB02009
  • HMDB59627
Metabolite Identification
Common NameCrotonoyl-CoA
DescriptionCrotonoyl-CoA (CAS: 992-67-6) is an important component in several metabolic pathways, notably fatty acid and amino acid metabolism. It is the substrate of acyl-coenzyme A oxidases 1, 2, and 3 (EC 1.3.3.6) corresponding to palmitoyl, branched-chain, and pristanoyl, respectively. In peroxisomal fatty acid beta-oxidation, these enzymes produce hydrogen peroxide. Abnormalities in this group of enzymes are linked to coma, dehydration, diabetes, fatty liver, hyperinsulinemia, hyperlipidemia, and leukodystrophy. Crotonoyl-CoA is also a substrate of a group of enzymes called acyl-coenzyme A dehydrogenases (EC 1.3.99-, 1.3.99.2, 1.3.99.3) in the metabolism of fatty acids or branched-chain amino acids in the mitochondria (PMID: 7698750 ). Acyl-coenzyme A dehydrogenase has been 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, and 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 (EC 4.2.1.17) in the mitochondria during lysine degradation and tryptophan metabolism as well as benzoate degradation via CoA ligation. Crotonoyl-CoA is the product of this enzyme in butanoate metabolism. Moreover, it is produced from multiple enzymes in the butanoate metabolism pathway, including 3-hydroxybutyryl-CoA dehydratase (EC 4.2.1.55), glutaconyl-CoA decarboxylase (EC 4.1.1.70), vinylacetyl-CoA delta-isomerase (EC 5.3.3.3), and trans-2-enoyl-CoA reductase (NAD+) (EC 1.3.1.44). In lysine degradation and tryptophan metabolism, crotonoyl-CoA is produced by glutaryl-coenzyme A dehydrogenase (EC 1.3.99.7). This enzyme is linked to glutaric aciduria type I, metabolic diseases, movement disorders, myelinopathy, and nervous system diseases.
Structure
Data?1588781937
Synonyms
ValueSource
Crotonyl-CoAChEBI
trans-But-2-enoyl-CoAChEBI
trans-Butyr-2-enoyl-CoAChEBI
2-Butenoyl-CoAKegg
But-2-enoyl-CoAKegg
(2E)-But-2-enoyl-CoAKegg
Crotonyl-coenzyme AHMDB
(e)-But-2-enoyl-CoAChEBI
Crotonoyl-CoAHMDB
Crotonoyl-coenzyme AHMDB
Crotonyl coenzyme AHMDB
trans-2-Butenoyl-CoAHMDB
trans-2-Butenoyl-coenzyme AHMDB
trans-Crotonoyl-CoAHMDB
trans-Crotonoyl-coenzyme AHMDB
trans-Crotonyl CoAHMDB
Chemical FormulaC25H40N7O17P3S
Average Molecular Weight835.608
Monoisotopic Molecular Weight835.141423115
IUPAC Name(2R)-4-({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)-N-[2-({2-[(2E)-but-2-enoylsulfanyl]ethyl}-C-hydroxycarbonimidoyl)ethyl]-2-hydroxy-3,3-dimethylbutanimidic acid
Traditional Name(2R)-4-[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]-N-[2-({2-[(2E)-but-2-enoylsulfanyl]ethyl}-C-hydroxycarbonimidoyl)ethyl]-2-hydroxy-3,3-dimethylbutanimidic acid
CAS Registry Number38795-21-0
SMILES
C\C=C\C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(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
InChI Identifier
InChI=1S/C25H40N7O17P3S/c1-4-5-16(34)53-9-8-27-15(33)6-7-28-23(37)20(36)25(2,3)11-46-52(43,44)49-51(41,42)45-10-14-19(48-50(38,39)40)18(35)24(47-14)32-13-31-17-21(26)29-12-30-22(17)32/h4-5,12-14,18-20,24,35-36H,6-11H2,1-3H3,(H,27,33)(H,28,37)(H,41,42)(H,43,44)(H2,26,29,30)(H2,38,39,40)/b5-4+/t14-,18-,19-,20+,24-/m1/s1
InChI KeyKFWWCMJSYSSPSK-PAXLJYGASA-N
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
Substituents
  • 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 Descriptors
Ontology
Disposition

Route of exposure:

Source:

Biological location:

Process

Naturally occurring process:

Role

Industrial application:

Biological role:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility3.67 g/LALOGPS
logP-0.11ALOGPS
logP-4.2ChemAxon
logS-2.4ALOGPS
pKa (Strongest Acidic)0.82ChemAxon
pKa (Strongest Basic)6.43ChemAxon
Physiological Charge-4ChemAxon
Hydrogen Acceptor Count19ChemAxon
Hydrogen Donor Count9ChemAxon
Polar Surface Area370.61 ŲChemAxon
Rotatable Bond Count21ChemAxon
Refractivity183.57 m³·mol⁻¹ChemAxon
Polarizability75.89 ųChemAxon
Number of Rings3ChemAxon
BioavailabilityNoChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00kr-1921000110-de694ebfa0837735d1beSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000l-1911000000-5b106b3a07df5c8c3755Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1920000000-2ecd1925643a7cc3e17fSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00lr-7920142560-10f7deae9d59f3fd3b6dSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-6910110000-fc85ca4055cec31805dcSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-057i-5900100000-a22910037b80042e1f67Spectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Membrane
  • Mitochondria
  • Peroxisome
Biospecimen LocationsNot Available
Tissue Locations
  • Liver
Pathways
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 IDFDB022792
KNApSAcK IDNot Available
Chemspider ID4593713
KEGG Compound IDC00877
BioCyc IDCROTONYL-COA
BiGG IDNot Available
Wikipedia LinkNot Available
METLIN IDNot Available
PubChem Compound5497143
PDB IDNot Available
ChEBI ID15473
Food Biomarker OntologyNot Available
VMH IDNot Available
References
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 ]
  11. Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B: Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 1994 Nov 15;24(2):280-7. [PubMed:7698750 ]
  12. Simons K, Toomre D: Lipid rafts and signal transduction. Nat Rev Mol Cell Biol. 2000 Oct;1(1):31-9. [PubMed:11413487 ]
  13. Watson AD: Thematic review series: systems biology approaches to metabolic and cardiovascular disorders. Lipidomics: a global approach to lipid analysis in biological systems. J Lipid Res. 2006 Oct;47(10):2101-11. Epub 2006 Aug 10. [PubMed:16902246 ]
  14. Sethi JK, Vidal-Puig AJ: Thematic review series: adipocyte biology. Adipose tissue function and plasticity orchestrate nutritional adaptation. J Lipid Res. 2007 Jun;48(6):1253-62. Epub 2007 Mar 20. [PubMed:17374880 ]
  15. Lingwood D, Simons K: Lipid rafts as a membrane-organizing principle. Science. 2010 Jan 1;327(5961):46-50. doi: 10.1126/science.1174621. [PubMed:20044567 ]
  16. Gunstone, Frank D., John L. Harwood, and Albert J. Dijkstra (2007). The lipid handbook with CD-ROM. CRC Press.

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

Enzymes

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:
ACAA2
Uniprot ID:
P42765
Molecular weight:
41923.82
General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Not Available
Gene Name:
ACAA1
Uniprot ID:
P09110
Molecular weight:
34664.46
General function:
Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Specific function:
Not Available
Gene Name:
HADHB
Uniprot ID:
P55084
Molecular weight:
51293.955
General function:
Involved in oxidoreductase activity
Specific function:
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Gene Name:
ALDH6A1
Uniprot ID:
Q02252
Molecular weight:
57839.31
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
ACADL
Uniprot ID:
P28330
Molecular weight:
47655.275
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
ACADS
Uniprot ID:
P16219
Molecular weight:
44296.705
Reactions
Butyryl-CoA + electron-transfer flavoprotein → Crotonoyl-CoA + reduced electron-transfer flavoproteindetails
Butyryl-CoA + NAD → Crotonoyl-CoA + NADH + Hydrogen Iondetails
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
This enzyme is specific for acyl chain lengths of 4 to 16.
Gene Name:
ACADM
Uniprot ID:
P11310
Molecular weight:
46587.98
Reactions
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
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:
ACOX1
Uniprot ID:
Q15067
Molecular weight:
70135.205
Reactions
Butyryl-CoA + FAD → FADH + Crotonoyl-CoAdetails
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:
ACOX2
Uniprot ID:
Q99424
Molecular weight:
76826.14
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Not Available
Gene Name:
IVD
Uniprot ID:
P26440
Molecular weight:
43055.325

Transporters

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:
SLC27A1
Uniprot ID:
Q6PCB7
Molecular weight:
71107.5

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