| Literature DB >> 15820980 |
Jonathan Kyle Lassila1, Jennifer R Keeffe, Peter Oelschlaeger, Stephen L Mayo.
Abstract
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.Entities:
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Year: 2005 PMID: 15820980 DOI: 10.1093/protein/gzi015
Source DB: PubMed Journal: Protein Eng Des Sel ISSN: 1741-0126 Impact factor: 1.650