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Aquifex aeolicus VF5 Reaction: 4.1.3.34

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

EC Number: 4.1.3.34

Enzymes and Genes:
citrate synthase Inferred by computational analysis : gltA

In Pathway: reductive TCA cycle II

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

Mass balance status: Balanced.

Enzyme Commission Primary Name: citryl-CoA lyase

Enzyme Commission Synonyms: (3S)-citryl-CoA oxaloacetate-lyase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 9.082886 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein.

Citations: [Lill82, Dimroth77]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:4.1.3.34 , ENZYME:EC:4.1.3.34 , IUBMB-ExplorEnz:EC:4.1.3.34

Credits:
Imported from MetaCyc 08-Aug-2014 by Subhraveti P , SRI International


References

Dimroth77: Dimroth P, Loyal R, Eggerer H (1977). "Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate." Eur J Biochem 80(2);479-88. PMID: 336371

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

Lill82: Lill U, Schreil A, Eggerer H (1982). "Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase." Eur J Biochem 125(3);645-50. PMID: 6749502


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