Article
Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.
Journal of molecular biology - 1 Mar 2002
Le Du M H, Lamoure C, Muller B H, Bulgakov O V, Lajeunesse E, Ménez A, Boulain J-C
Abstract excerpt
The crystal structure of three mutants of Escherichia coli alkaline phosphatase with catalytic activity (k(cat)) enhancement as compare to the wild-type enzyme is described in different states. The biological aspects of this study have been reported elsewhere. The structure of the first mutant, D330N, which is threefold more active than the wild-type enzyme, was determined with phosphate in the active site, or...
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