A Novel Enzymatic Decarboxylation Proceeds via a Thiol Ester Intermediate

Article abstract of DOI:10.1246/bcsj.68.2017

It is proposed that arylmalonate decarboxylase (AMDase)-catalyzed decarboxylation proceeds via a thiol ester intermediate.Kinetics and CD spectra indicated that α-bromohenylacetate is a competititve 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.