Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents.

S J McCormick; G Tunnicliff

doi:10.18388/abp.2001_3940

Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents.

S J McCormick Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Evansville, IN 47712, USA.;
G Tunnicliff

DOI: https://doi.org/10.18388/abp.2001_3940

Abstract

Mercuric chloride, p-chloromercuribenzoate and 5,5'-dithiobis(2-nitrobenzoic acid) irreversibly inhibited the activity of Escherichia coli glutamate decarboxylase. Their second order rate constants for inactivation are 0.463 microM(-1) min(-1), 0.034 microM(-1) min(-1), 0.018 microM(-1) min(-1), respectively. The characteristics of the inhibition by the three thiol-group reagents supports the idea that cysteinyl residues at the binding sites for the cofactor and/or the substrate are important for enzyme activity in E. coli.

Published

2001-06-30

Issue

Vol. 48 No. 2 (2001)

Section

Articles

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