Enzyme dynamics point to stepwise conformational selection in catalysis

Buyong Ma*, Ruth Nussinov

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


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.

Original languageEnglish
Pages (from-to)652-659
Number of pages8
JournalCurrent Opinion in Chemical Biology
Issue number5
StatePublished - Oct 2010


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