Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents

Authors
McCormick, SJ Tunnicliff, G
Citation
Sj. Mccormick et G. Tunnicliff, Kinetics of inactivation of glutamate decarboxylase by cysteine-specific reagents, ACT BIOCH P, 48(2), 2001, pp. 573-578
Citations number
21
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ACTA BIOCHIMICA POLONICA
ISSN journal
0001527X → ACNP
Volume
48
Issue
2
Year of publication
2001
Pages
573 - 578
Database
ISI
SICI code
0001-527X(2001)48:2<573:KOIOGD>2.0.ZU;2-V
Abstract
Mercuric chloride, p-chloromercuribenzoate and 5,5'-dithiobis(2-nitrobenzoi c acid) irreversibly inhibited the activity of Escherichia coli glutamate d ecarboxylase. Their second order rate constants for inactivation are 0.463 muM(-1)min(-1), 0.034 muM(-1)min(-1) 0.018 muM(-1)min(-1), respectively. Th e characteristics of the inhibition by the three thiol-group reagents suppo rts the idea that cysteinyl residues at the binding sites for the cofactor and/or the substrate are important for enzyme activity in E. coli.