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D. A. Gudkov, Yu. A. Votchitseva, E. N. Efremenko, S. D. Varfolomeyev
Paraoxon Hydrolysis catalyzed
by organophosphate hydrolase containing the polyhistidine tag at the C-terminus
of protein molecule
Abstract
The non- Michaelis kinetics
of paraoxon hydrolysis catalyzed by the organophosphate hydrolase, containing
the hexahistidine tag at the C-terminus, was revealed. The appearance of
catalytically active metal-complex formed by the hexahistidine tag, introduced
into the genetically modified OPH structure, and the Co2+
ions, added to the reaction medium to activate the OPH being metalloenzyme,
additionally to the native active site was supposed.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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