EC 6.2.1.22 - [citrate (pro-3S)-lyase] ligase

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IntEnz Enzyme Nomenclature
EC 6.2.1.22

Names

Accepted name:
[citrate (pro-3S)-lyase] ligase
Other names:
acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP)
acetate:HS-citrate lyase ligase
acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming)
citrate lyase ligase
citrate lyase synthetase
[citrate-(pro-3S)-lyase](thiol-form)
Systematic name:
acetate:holo-[citrate-(pro-3S)-lyase] ligase (AMP-forming)

Reaction

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008771
UniProtKB/Swiss-Prot:

References

  1. Antranikian, G. and Gottschalk, G.
    Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes.
    Eur. J. Biochem. 126 : 43-47 (1982). [PMID: 7128585]
  2. Antranikian, G., Herzberg, C. and Gottschalk, G.
    Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation.
    Eur. J. Biochem. 153 : 413-420 (1985). [PMID: 3935436]
  3. Quentmeier, A. and Antranikian, G.
    Characterization of citrate lyase from Clostridium sporosphaeroides.
    Arch. Microbiol. 141 : 85-90 (1985). [PMID: 3994485]
  4. Schmellenkamp, H. and Eggerer, H.
    Mechanism of enzymic acetylation of des-acetyl citrate lyase.
    Proc. Natl. Acad. Sci. USA 71 : 1987-1991 (1974). [PMID: 4365579]

[EC 6.2.1.22 created 1989]