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Curr Opin Chem Biol. 2010 Oct;14(5):652-9. doi: 10.1016/j.cbpa.2010.08.012. Epub 2010 Sep 6.

Enzyme dynamics point to stepwise conformational selection in catalysis.

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  • 1Basic Science Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. mabuyong@mail.nih.gov

Abstract

Recent data increasingly reveal that conformational dynamics are indispensable to enzyme function throughout the catalytic cycle, in substrate recruiting, chemical transformation, and product release. Conformational transitions may involve conformational selection and induced fit, which can be viewed as a special case in the catalytic network. NMR, X-ray crystallography, single-molecule FRET, and simulations clearly demonstrate that the free enzyme dynamics already encompass all the conformations necessary for substrate binding, preorganization, transition-state stabilization, and product release. Conformational selection and substate population shift at each step of the catalytic turnover can accommodate enzyme specificity and efficiency. Within such a framework, entropy can have a larger role in conformational dynamics than in direct energy transfer in dynamically promoted catalysis.

Copyright © 2010 Elsevier Ltd. All rights reserved.

PMID:
20822947
[PubMed - indexed for MEDLINE]
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