Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity.
نویسندگان
چکیده
Computational protein design methods were used to predict five variants of monofunctional Escherichia coli chorismate mutase expected to maintain catalytic activity. The variants were tested experimentally and three active site mutants exhibited catalytic activity similar to or greater than the wild-type enzyme. One mutant, Ala32Ser, showed increased catalytic efficiency.
منابع مشابه
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ورودعنوان ژورنال:
- Protein engineering, design & selection : PEDS
دوره 18 4 شماره
صفحات -
تاریخ انتشار 2005