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

• Authors: Sara J McCormick , Godfrey Tunnicliff
• Languages of publication: EN

Abstracts

EN

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 μM-1min-1, 0.034 μM-1min-1, 0.018 μM-1min-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.

Keywords

EN

mercuric chloride; Escherichia coli; DTNB; cysteinyl residues; p-chloromercuribenzoate; glutamate decarboxylase; inactivation; sulfhydryl groups

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2001
• Volume: 48
• Issue: 2
• Pages: 573-578

Dates

published

2001

received

2000-11-30

revised

2001-01-29

accepted

2001-05-15

Contributors

author

Sara J McCormick

• Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 8600 University Boulevard, Evansville, IN 47712, U.S.A.

author

Godfrey Tunnicliff

• Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 8600 University Boulevard, Evansville, IN 47712, U.S.A.

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