Published April 8, 2005
| Published
Journal Article
Open
Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity
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.
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.Attached Files
Published - LASpeds05.pdf
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LASpeds05.pdf
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Additional details
- Eprint ID
- 5627
- Resolver ID
- CaltechAUTHORS:LASpeds05
- Howard Hughes Medical Institute (HHMI)
- Ralph M. Parsons Foundation
- Defense Advanced Research Projects Agency (DARPA)
- Army Research Office (ARO)
- IBM
- Created
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2006-10-26Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field