PMID:11732626
| Citation |
McCormick, SJ and Tunnicliff, G (2001) Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents. Acta Biochim. Pol. 48:573-8 |
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| 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. |
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| Keywords |
Binding Sites; Cysteine/chemistry; Dithionitrobenzoic Acid/pharmacology; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Glutamate Decarboxylase/antagonists & inhibitors; Glutamate Decarboxylase/chemistry; Kinetics; Mercuric Chloride/pharmacology; Sulfhydryl Reagents/pharmacology; p-Chloromercuribenzoic Acid/pharmacology |
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