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  1. 1 Acta Biochimica Polonica

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  1. 1 2001

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  1. 1 McCormick S. J.

  2. 1 Tunnicliff G.

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

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McCormick S. J., Tunnicliff G.
Acta Biochimica Polonica
|
2001
|
vol. 48
|
issue 2
573-578
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.
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