Properties of hexahistidine-tagged organophosphate hydrolase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-02

AUTHORS

Yu. A. Votchitseva, 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). More... »

PAGES

167-172

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0006297906020088

DOI

http://dx.doi.org/10.1134/s0006297906020088

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034565693

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16489921


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