CaltechAUTHORS
Published April 8, 2005 | Version Published
Journal Article Open

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

Creators

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

Files

LASpeds05.pdf

Files (68.1 kB)

Name Size Download all
md5:9edc8f6a6af36555e52a1b6f877672dc
68.1 kB Preview Download

Additional details

Identifiers

Eprint ID
5627
Resolver ID
CaltechAUTHORS:LASpeds05

Funding

Howard Hughes Medical Institute (HHMI)
Ralph M. Parsons Foundation
Defense Advanced Research Projects Agency (DARPA)
Army Research Office (ARO)
IBM

Dates

Created
2006-10-26
Created from EPrint's datestamp field
Updated
2021-11-08
Created from EPrint's last_modified field