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PEDS Advance Access originally published online on April 8, 2005
Protein Engineering Design and Selection 2005 18(4):161-163; 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

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

Jonathan Kyle Lassila1, Jennifer R. Keeffe1, Peter Oelschlaeger2 and Stephen L. Mayo2,3,4

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

4 To whom correspondence should be addressed. E-mail: steve{at}mayo.caltech.edu

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

Received March 2, 2005; accepted March 4, 2005.

Edited by Don Hilvert


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This article has been cited by other articles:


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