|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: 220.127.116.11
Enzymes and Genes:
|Klebsiella pneumoniae :||[citrate [pro-3S]-lyase] ligase
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 direction in which it was curated.
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): -31.734009 [Latendresse13]
Unification Links: KEGG:R04449
Relationship Links: BRENDA:EC:18.104.22.168 , ENZYME:EC:22.214.171.124 , IUBMB-ExplorEnz:EC:126.96.36.199 , UniProt:RELATED-TO:P44462 , UniProt:RELATED-TO:P45410 , UniProt:RELATED-TO:Q9CGB0 , UniProt:RELATED-TO:Q9RLT7
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
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