| Literature DB >> 16489921 |
Yu A Votchitseva1, E N Efremenko, T K Aliev, S D Varfolomeyev.
Abstract
The catalytic properties of organophosphate hydrolase (OPH) containing a hexahistidine tag His6 (His6-OPH) and purified to 98% homogeneity were investigated. The pH optimum of enzymatic activity and isoelectric point of His6-OPH, which were shown to be 10.5 and 8.5, respectively, are shifted to the alkaline range as compared to the same parameters of the native OPH. The recombinant enzyme possessed improved catalytic activity towards S-containing substrates: the catalytic efficiency of methylparathion hydrolysis by His6-OPH is 4.2 x 10(6) M(-1) x sec(-1), whereas by native OPH it is 3.5 x 10(5) M(-1) x sec(-1).Entities:
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Year: 2006 PMID： 16489921 DOI： 10.1134/s0006297906020088
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN： 0006-2979 Impact factor: 2.487