Báo cáo khóa học: Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding
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Mutants of a cobalt-containing nitrile hydratase (NHase, EC 4.2.1.84) fromPseudonocardia thermophilaJCM 3095 involved in substrate binding, catalysis and formation of the active center were constructed, and their characteristics and crystal structures were investigated. As expected fromthe structure of the substrate binding pocket, the wild-type enzyme showed significantly lower KmandKi values for aromatic substrates and inhibitors, respectively, than alipha-ticones.
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