Abstract
Thymidine phosphorylase (deoA) and purine nucleoside phosphorylase (deoD) genes from the extremophilic bacterium Halomonas chromatireducens AGD 8-3 have been cloned. Expression plasmids were constructed, and highly efficient recombinant producer strains were obtained for these proteins. Recombinant nucleoside phosphorylases were isolated by ion-exchange chromatography in a homogeneous state, and their physical and enzymatic properties were studied. It was shown that the studied thymidine phosphorylase (HrTPP) and purine nucleoside phosphorylase (HrPNP) form the dimeric and hexameric forms, respectively. It was shown that the specific activity of HrTPP from the extremophilic bacterium H. chromatireducens AGD 8-3 was higher relative to thymidine (in comparison with its counterpart from E. coli).
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