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2001 | 48 | 2 | 573-578
Article title

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

Content
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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.
Year
Volume
48
Issue
2
Pages
573-578
Physical description
Dates
published
2001
received
2000-11-30
revised
2001-01-29
accepted
2001-05-15
References
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Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv48i2p573kz
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