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- W379396519 abstract "Summary In vivo random mutagenesis was used to enhance the thermal stability of Saccharomyces pastorianus hexokinase. Four thermostable mutants were isolated, and the following amino acid substitutions were identified: Glu53 to Val, Ala161 to Val, Ser255 to Pro, and Gly408 to Asp. The wildtype and mutant enzymes were purified and characterized. The properties of mutants were similar to those of the wild type but they showed improved thermal activity. Analysis of multiple mutants constructed by site-directed mutagenesis showed that all the mutations brought an additive effect to the other mutations. These mutational effects were discussed in terms of the three-dimensional structure of Saccharomyces cerevisiae hexokinase." @default.
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- W379396519 date "2009-01-01" @default.
- W379396519 modified "2023-09-24" @default.
- W379396519 title "Improvement of thermal stability of Saccharomyces pastorianus hexokinase by random mutagenesis and a structural interpretation" @default.
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