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

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. doi:10.1093/protein/gzi015.

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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.

Item Type:Article
Related URLs:
URLURL TypeDescription
Keeffe, Jennifer R.0000-0002-5317-6398
Oelschlaeger, Peter0000-0001-5949-9297
Mayo, Stephen L.0000-0002-9785-5018
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.
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Ralph M. Parsons FoundationUNSPECIFIED
Defense Advanced Research Projects Agency (DARPA)UNSPECIFIED
Army Research Office (ARO)UNSPECIFIED
Subject Keywords:enzyme design; chorismate mutase; protein design
Issue or Number:4
Record Number:CaltechAUTHORS:LASpeds05
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:5627
Deposited By: Lindsay Cleary
Deposited On:26 Oct 2006
Last Modified:08 Nov 2021 20:27

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