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Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store

MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Canis lupus familiaris: acyl-coA hydrolase (long chain): CESdD1
Escherichia coli K-12 substr. MG1655: acyl-CoA thioesterase: yciA
thioesterase II: tesB

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reaction:
propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (

Direct generic reaction:
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+ (

Enzyme Commission Primary Name: ADP-dependent short-chain-acyl-CoA hydrolase

Enzyme Commission Synonyms: short-chain acyl coenzyme A hydrolase, propionyl coenzyme A hydrolase, propionyl-CoA hydrolase, propionyl-CoA thioesterase, short-chain acyl-CoA hydrolase, short-chain acyl-CoA thioesterase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 312.0276Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Requires ADP; inhibited by NADH. Maximum activity is shown with propanoyl-CoA.

Citations: [Alexson88, Alexson89]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (
i1: propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (

i2: lauroyl-CoA + H2O → laurate + coenzyme A + H+ (

i3: decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (

i4: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (

i5: 3-oxo-myristoyl-CoA + H2O → 3-oxo-myristate + coenzyme A + H+ (3.1.2.-)

i6: icosanoyl-CoA + H2O → arachidate + coenzyme A + H+ (

i7: docosapentaenoyl-CoA + H2O → (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentenoate + coenzyme A + H+ (3.1.2.-)

i8: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (

i9: docosahexaenoyl-CoA + H2O = docosahexaenoate + coenzyme A + H+ (

i10: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (

i11: (R)-3-hydroxybutanoyl-CoA + H2O → (R)-3-hydroxybutanoate + coenzyme A + H+ (no EC#)

i12: (S)-3-hydroxybutanoyl-CoA + H2O → (S)-3-hydroxybutanoate + coenzyme A + H+ (no EC#)

i13: palmitoleoyl-CoA + H2O → palmitoleate + coenzyme A + H+ (3.1.2.-)

i14: oleoyl-CoA + H2O → oleate + coenzyme A + H+ (

i15: a 3-oxoacyl-CoA + H2O → a 3-oxoacid + coenzyme A + H+ (3.1.2.-)

i16: a long-chain acyl-CoA + H2O → a long-chain fatty acid + coenzyme A + H+ (

i17: a medium-chain acyl-CoA + H2O → a medium-chain carboxylate + coenzyme A + H+ (

i18: a 2,3,4-saturated fatty acyl CoA + H2O → a 2,3,4-saturated fatty acid + coenzyme A + H+ (

i19: a short-chain acyl-CoA + H2O → a short-chain carboxylate + coenzyme A + H+ (

Unification Links: KEGG:R00383

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, Rhea:RELATED-TO:16781


Alexson88: Alexson SE, Nedergaard J (1988). "A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria." J Biol Chem 263(27);13564-71. PMID: 2901416

Alexson89: Alexson SE, Svensson LT, Nedergaard J (1989). "NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat." Biochim Biophys Acta 1005(1);13-9. PMID: 2570608

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc13.