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PEDS Advance Access published online on April 8, 2005
Protein Engineering Design and Selection, doi:10.1093/protein/gzi015
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© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org
Received March 2, 2005
Accepted March 4, 2005

Communication

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

Jonathan Kyle Lassila 1, Jennifer R. Keeffe 1, Peter Oelschlaeger 2, and Stephen L. Mayo 3*

1 Biochemistry and Molecular Biophysics Option, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA
2 Division of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA
3 Division of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA; Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA

* To whom correspondence should be addressed.
Stephen L. Mayo, E-mail: steve{at}mayo.caltech.edu


  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.

Keywords: enzyme design; chorismate mutase; protein design.
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