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Enzyme dynamics point to stepwise conformational selection in catalysis

  1. Author:
    Ma, B. Y.
    Nussinov, R.

  2. Author Address

    [Ma, Buyong; Nussinov, Ruth] SAIC Frederick Inc, Basic Sci Program, Ctr Canc Res Nanobiol Program, NCI Frederick, Ft Detrick, MD 21702 USA. [Nussinov, Ruth] Tel Aviv Univ, Sackler Sch Med, Dept Human Genet & Mol Med, Sackler Inst Mol Med, IL-69978 Tel Aviv, Israel.;Ma, BY, SAIC Frederick Inc, Basic Sci Program, Ctr Canc Res Nanobiol Program, NCI Frederick, Ft Detrick, MD 21702 USA.;mabuyong@mail.nih.gov ruthnu@helix.nih.gov
    1. Year: 2010
    2. Date: Oct
  2. Journal: Current Opinion in Chemical Biology
    1. 14
    2. 5
    3. Pages: 652-659
  4. Type of Article: Review
  5. ISSN: 1367-5931
  1. 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.

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External Sources

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  2. DOI: 10.1016/j.cbpa.2010.08.012
  3. View record in Web of Science®
  4. WOS: 000283916300014

Library Notes

  1. Fiscal Year: FY2010-2011
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