A Novel Enzymatic Decarboxylation Proceeds via a Thiol Ester Intermediate
1995
It is proposed that arylmalonate decarboxylase (AMDase)-catalyzed decarboxylation proceeds via a thiol ester intermediate. Kinetics and CD spectra indicated that α-bromophenylacetate is a competitive inhibitor. TOF mass data indicated that the inhibitor bound with the enzyme through a thiol ester bond which was formed between a cysteine residue of the enzyme and the carboxyl group of the inhibitor. This result was also supported by reactivation of the enzyme by the addition of 2-mercaptoethanol, which is expected to cleave the enzyme–inhibitor bond via nucleophilic attack on the thiol ester linkage.
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