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Escherichia coli K-12 substr. MG1655 Reaction: 3.1.2.20

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.1.2.20

Enzymes and Genes:
thioesterase II Inferred from experiment : tesB
acyl-CoA thioesterase Inferred from experiment : yciA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

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

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

a 2,3,4-saturated fatty acyl CoA[periplasmic space] + H2O[periplasmic space] → a 2,3,4-saturated fatty acid[periplasmic space] + coenzyme A[periplasmic space] + H+[periplasmic space] (3.1.2.2)

Enzyme Commission Primary Name: acyl-CoA hydrolase

Enzyme Commission Synonyms: acyl coenzyme A thioesterase, acyl coenzyme A hydrolase, thioesterase B, thioesterase II, acyl-CoA thioesterase

Enzyme Commission Summary:
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase).

Citations: [Alexson89]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (3.1.2.20):
i1: (R)-3-hydroxybutanoyl-CoA + H2O → (R)-3-hydroxybutanoate + coenzyme A + H+ (no EC#)

i2: (S)-3-hydroxybutanoyl-CoA + H2O → (S)-3-hydroxybutanoate + coenzyme A + H+ (no EC#)

i3: a 2,3,4-saturated fatty acyl CoA[periplasmic space] + H2O[periplasmic space] → a 2,3,4-saturated fatty acid[periplasmic space] + coenzyme A[periplasmic space] + H+[periplasmic space] (3.1.2.2)

Relationship Links: BRENDA:EC:3.1.2.20 , ENZYME:EC:3.1.2.20 , IUBMB-ExplorEnz:EC:3.1.2.20


References

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


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Thu Jul 2, 2015, biocyc13.