Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity.

Jonathan Kyle Lassila, Jennifer R Keeffe, Peter Oelschlaeger, Stephen L Mayo

Journal: Protein engineering, design & selection : PEDS 2005;18(4):161-3

PMID: 15820980

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.

Address: Biochemistry and Molecular Biophysics Option, Howard Hughes Medical Institute, Pasadena, CA 91125, USA.

DOI: 10.1093/protein/gzi015

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MeSH Terms: Alanine, Amino Acid Substitution, Catalysis, Catalytic Domain, Chorismate Mutase, Computational Biology, Escherichia coli, Mutation, Protein Engineering, Serine