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

Sally McCormick | Zendy; G. Tunnicliff | Zendy

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

Author(s) -

Sally McCormick,

G. Tunnicliff

Publication year - 2001

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2001_3940

Subject(s) - chemistry , cysteine , reagent , substrate (aquarium) , enzyme , escherichia coli , biochemistry , cofactor , kinetics , thiol , glutamate decarboxylase , reaction rate constant , stereochemistry , organic chemistry , biology , ecology , physics , quantum mechanics , gene

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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