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: 6.2.1.22

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 6.2.1.22

Enzymes and Genes:
[citrate [pro-3S]-lyase] ligase Inferred from experiment : citC ( Klebsiella pneumoniae )

In Pathway: citrate lyase activation

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: [citrate (pro-3S)-lyase] ligase

Enzyme Commission Synonyms: citrate lyase ligase, citrate lyase synθse, acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP), acetate:HS-citrate lyase ligase, acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming)

Standard Gibbs Free Energy (ΔrG in kcal/mol): -31.73413 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase.

Citations: [Schmellenkamp74, Quentmeier85, Antranikian85, Antranikian82]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R04449

Relationship Links: BRENDA:EC:6.2.1.22 , ENZYME:EC:6.2.1.22 , IUBMB-ExplorEnz:EC:6.2.1.22 , UniProt:RELATED-TO:P44462 , UniProt:RELATED-TO:P45410 , UniProt:RELATED-TO:Q9CGB0 , UniProt:RELATED-TO:Q9RLT7


References

Antranikian82: Antranikian G, Gottschalk G (1982). "Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes." Eur J Biochem 126(1);43-7. PMID: 7128585

Antranikian85: Antranikian G, Herzberg C, Gottschalk G (1985). "Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation." Eur J Biochem 153(2);413-20. PMID: 3935436

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

Quentmeier85: Quentmeier A, Antranikian G (1985). "Characterization of citrate lyase from Clostridium sporosphaeroides." Arch Microbiol 141(1);85-90. PMID: 3994485

Schmellenkamp74: Schmellenkamp H, Eggerer H (1974). "Mechanism of enzymic acetylation of des-acetyl citrate lyase." Proc Natl Acad Sci U S A 71(5);1987-91. PMID: 4365579


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 Fri Nov 28, 2014, biocyc14.