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Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2794-9. Epub 2002 Feb 26.

Network of coupled promoting motions in enzyme catalysis.

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  • 1Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, PA 16802, USA.

Abstract

A network of coupled promoting motions in the enzyme dihydrofolate reductase is identified and characterized. The present identification is based on genomic analysis for sequence conservation, kinetic measurements of multiple mutations, and mixed quantum/classical molecular dynamics simulations of hydride transfer. The motions in this network span time scales of femtoseconds to milliseconds and are found on the exterior of the enzyme as well as in the active site. This type of network has broad implications for an expanded role of the protein fold in catalysis as well as ancillaries such as the engineering of altered protein function and the action of drugs distal to the active site.

PMID:
11867722
[PubMed - indexed for MEDLINE]
PMCID:
PMC122427
Free PMC Article
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