Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc 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:
acyl-CoA thioesterase Inferred from experiment : yciA ( Escherichia coli K-12 substr. MG1655 )
thioesterase II Inferred from experiment : tesB ( Escherichia coli K-12 substr. MG1655 )
acyl-coA hydrolase (long chain) Inferred from experiment : CESdD1 ( Canis lupus familiaris )

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

decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (3.1.2.2)

arachidoyl-CoA + H2O → arachidate + coenzyme A + H+ (3.1.2.2)

palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (3.1.2.2)

stearoyl-CoA + H2O → stearate + coenzyme A + H+ (3.1.2.2)

myristoyl-CoA + H2O → myristate + coenzyme A + H+ (3.1.2.2)

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

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

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: ?

Instance reaction of [a medium-chain acyl-CoA + H2O → a medium-chain carboxylate + coenzyme A + H+] (3.1.2.19):
i4: lauroyl-CoA + H2O → laurate + coenzyme A + H+ (3.1.2.2)

Instance reactions of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (3.1.2.20):
i1: propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (3.1.2.18)

i2: decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (3.1.2.2)

i3: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (3.1.2.2)

i5: arachidoyl-CoA + H2O → arachidate + coenzyme A + H+ (3.1.2.2)

i6: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (3.1.2.2)

i7: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (3.1.2.2)

Unification Links: KEGG:R00383

Relationship Links: BRENDA:EC:3.1.2.20 , ENZYME:EC:3.1.2.20 , IUBMB-ExplorEnz:EC:3.1.2.20 , Rhea:RELATED-TO:16781 , UniProt:RELATED-TO:O00154


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

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 Thu Nov 20, 2014, BIOCYC14A.