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- W1981294291 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." @default.
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- W1981294291 date "1976-04-01" @default.
- W1981294291 modified "2023-09-26" @default.
- W1981294291 title "Acetic Anhydride: an Intermediate. Analogue in the Acyl-Exchange Reaction of Citramalate Lyase" @default.
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- W1981294291 doi "https://doi.org/10.1111/j.1432-1033.1976.tb10296.x" @default.
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