Abstract
Abstract 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.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
