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PMID: 3589666 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Computer simulations of the diffusion of a substrate to an active site of an enzyme.

Science (New York, N.Y.) ·Vol. 236 ·No. 4807 ·1987-06-12 ·Pages 1460-3

Sharp K, Fine R, Honig B

Abstract

Computer simulations of the diffusion of a substrate to an enzyme active site were performed. They included the detailed shape of the protein and an accurate description of its electrostatic potential. Application of the method to the diffusion of the superoxide anion to the protein superoxide dismutase revealed that the electric field of the enzyme enhances the association rate of the anion by a factor of 30 or more. Calculated changes in the association rate as a function of ionic strength and amino acid modification paralleled the observed behavior. Design principles of superoxide dismutase are considered with respect to insights provided by the simulations. A possible means of enhancing the enzyme turnover rate through site-directed mutagenesis is proposed.

MeSH Terms
Binding Sites Computer Simulation Diffusion Enzymes/metabolism Kinetics Mathematics Mutation Superoxide Dismutase/metabolism
Chemicals
Enzymes Superoxide Dismutase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sharp K
Fine R
Honig B
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1987-06-12
Pages
1460-3
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM30518 · United States
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