Bulletin of the Chemical Society of Japan p. 2017 - 2020 (1995)
Update date:2022-08-16
Topics:
Kawasaki, Takayasu
Watanabe, Masakatsu
Ohta, Hiromichi
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.
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