Lassila, Jonathan Kyle and Keeffe, Jennifer R. and Oelschlaeger, Peter and Mayo, Stephen L. (2005) Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity. Protein Engineering, Design and Selection, 18 (4). pp. 161-163. ISSN 1741-0126 http://resolver.caltech.edu/CaltechAUTHORS:LASpeds05
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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.
|Additional Information:||© The Author 2005. Published by Oxford University Press. Received March 2, 2005; accepted March 4, 2005. This work was supported by the Howard Hughes Medical Institute, the Ralph M. Parsons Foundation, the Defense Advanced Research Projects Agency, the Institute for Collaborative Biotechnologies (ARO) and an IBM Shared University Research Grant.|
|Subject Keywords:||enzyme design; chorismate mutase; protein design|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Lindsay Cleary|
|Deposited On:||26 Oct 2006|
|Last Modified:||26 Dec 2012 09:13|
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