Purification and Properties of Citrate Lyase Ligase from Streptococcus diacetilactis

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Abstract
Citrate lyase ligase (acetate: SH-[acyl-carrier protein] enzyme ligase (AMP)) from Streptococcus diacetilactis was purified 920-fold with a yield of 6.3%. The molecular weight of the enzyme was estimated to be 41000; the ligase consisted of one polypeptide chain. The acetylation of 1 mol of deacetyl-citrate lyase to enzymatically active citrate lyase required 6 mol ATP. The formation of AMP and pyrophosphate in the acetylation reaction was demonstrated. Citrate lyase ligase was specific for the lyase from S. diacetilactis and did not acetylate lyases from Rhodopseudomonas gelatinosa and Enterobacter aerogenes. The substrates acetate and ATP could be replaced by propionate and dATP, respectively. The reaction rates for ATP, acetate and deacetyl-citrate lyase followed Michaelis-Menten kinetics (Km values: 26 μM for ATP, 25 mM for acetate and 38 nM for deacetyl-citrate lyase).

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