Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 14, Issue 5, Pages 652-659Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2010.08.012
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Funding
- National Cancer Institute, National Institutes of Health [HHSN261200800001E]
- NIH, NCI, Center for Cancer Research
- NATIONAL CANCER INSTITUTE [ZIABC010441] Funding Source: NIH RePORTER
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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.
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