Improved substrate specificity and dynamic range for glucose measurement of Escherichia coli PQQ glucose dehydrogenase by site directed mutagenesis
作者： K. Sode , K. Kojima
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摘要: Site directed mutagenesis study was carried out with Escherichia coli pyrroloquinoline quinone glucose dehydroge-nase (PQQGDH) by substitution of His775 either Asn (H775N) or Asp (H775D). The mutated PQQGDHs had different substrate specificity and catalytic activity from the wild type PQQGDH. K values H775N for 2-deoxy-D-glucose D-allose increased 10-fold. both D-mannose D-galactose were estimated much higher than 100 mM. H775D also showed increase in toward saccharides. As a result, these mutants possessed narrower E. value versus PQQGDH (25-fold), therefore is suitable direct measurement blood glucose. role coli. discussed.
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