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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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: ?

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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