Metabolic Modeling Tutorial
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BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 3.1.2.18

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

EC Number: 3.1.2.18

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

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 reaction:
propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (3.1.2.18)

Direct generic reaction:
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+ (3.1.2.20)

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): 312.0276 Inferred by computational analysis [Latendresse13]

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

Citations: [Alexson88, Alexson89]

Unification Links: KEGG:R00383

Relationship Links: BRENDA:EC:3.1.2.18 , ENZYME:EC:3.1.2.18 , IUBMB-ExplorEnz:EC:3.1.2.18 , Rhea:RELATED-TO:16781


References

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 SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc12.