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citrate lyase subunit alpha
In citrate-utilising prokaryotes, citrate lyase EC:4.1.3.6 cleaves intracellular citrate into acetate and oxaloacetate, and is organised as a functional complex consisting of alpha, beta, and gamma subunits. The gamma subunit serves as an acyl carrier protein (ACP), and has a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group. The citrate lyase is active only if this prosthetic group is acetylated; this acetylation is catalysed by an acetate:SH-citrate lyase ligase. The alpha subunit substitutes citryl for the acetyl group to form citryl-S-ACP. The beta subunit completes the reaction by cleaving the citryl to yield oxaloacetate and (regenerated) acetyl-S-ACP. This family represents the alpha subunit EC:2.8.3.10. [1]. 9457870. Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster. Bekal S, Van Beeumen J, Samyn B, Garmyn D, Henini S, Divies C, Prevost H;. J Bacteriol 1998;180:647-654. [2]. 7830578. Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression. Bott M, Dimroth P;. Mol Microbiol 1994;14:347-356. (from Pfam)
citrate lyase subunit alpha is the citrate:acetyl-ACP transferase subunit of citrate lyase that catalyzes the conversion of citrate to acetate and oxaloacetate; also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citrate
The alpha subunit of the holoenzyme citrate lyase (EC 4.1.3.6) becomes citrate CoA-transferase (EC 2.8.3.10) upon dissociation of the enzyme complex.
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