Acetic Anhydride: an Intermediate. Analogue in the Acyl‐Exchange Reaction of Citramalate Lyase

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Abstract
1 Reactivation of deacetyl citramalate lyase by acetic anhydride proceeds through an enzymeanhydride complex prior to actual acetylation. The reaction is inhibited by citramalate which is competitive with acetic anhydride. 2 A corresponding complex is an intermediate in the carboxymethylation of deacetyl enzyme by iodoacetate. However, the inhibition of this reaction by S‐citramalate appears to be non‐competitive with iodoacetate. 3 The results lead to the conclusion that acetic anhydride can be regarded as a structural analogue of citramalic acetic anhydride, the proposed intermediate in the acyl exchange reaction on citramalate lease. 4 The formation of 6‐citryl thiolester from the 1‐thiolester via the cyclic citric anhydride provides a chemical model for enzymic acyl exchange. 5 The data suggest that anhydrides are of general importance in acyl exchange reactions of thiolesters.

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