(citrate_(pro-3S)-lyase)_ligase

(citrate (pro-3S)-lyase) ligase

(citrate (pro-3S)-lyase) ligase

Class of enzymes

In enzymology, a [citrate (pro-3S)-lyase] ligase (EC 6.2.1.22) is an enzyme that catalyzes the chemical reaction

ATP + acetate + citrate (pro-3S)-lyase(thiol form) AMP + diphosphate + citrate (pro-3S)-lyase(acetyl form)
Quick Facts pro-3S)-lyase] ligase, Identifiers ...

The 3 substrates of this enzyme are ATP, acetate, and citrate (pro-3S)-lyase(thiol form), whereas its 3 products are AMP, diphosphate, and citrate (pro-3S)-lyase(acetyl form).

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetate:citrate (pro-3S)-lyase(thiol-form) ligase (AMP-forming). Other names in common use include citrate lyase ligase, citrate lyase synthetase, acetate: SH-acyl-carrier-protein enzyme ligase (AMP), acetate:HS-citrate lyase ligase, and acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming). This enzyme participates in two-component system - general.

References

    • 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. doi:10.1111/j.1432-1033.1982.tb06743.x. PMID 7128585.
    • 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. doi:10.1111/j.1432-1033.1985.tb09318.x. PMID 3935436.
    • Quentmeier A, Antranikian G (1985). "Characterization of citrate lyase from Clostridium sporosphaeroides". Arch. Microbiol. 141 (1): 85–90. doi:10.1007/BF00446745. PMID 3994485. S2CID 32612466.
    • 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. Bibcode:1974PNAS...71.1987S. doi:10.1073/pnas.71.5.1987. PMC 388369. PMID 4365579.


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