| Coupled motions in enzyme catalysis. | |
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MedLine Citation:
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PMID: 20729130 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Recently, the hypothesis that protein motions are involved in enzymatic turnover has gained significant attention. We review cases where there is evidence that protein motions are rate-limiting in the overall catalytic cycle and examine experimental and theoretical evidence for how such motions enhance the probability of sampling the transition state configurations relative to the ground state. The impact of tunneling, the possible role of vibrational coupling and the value of conformational chemical landscapes are also scrutinized. |
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Authors:
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Vishal C Nashine; Sharon Hammes-Schiffer; Stephen J Benkovic |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Review Date: 2010-08-20 |
Journal Detail:
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Title: Current opinion in chemical biology Volume: 14 ISSN: 1879-0402 ISO Abbreviation: Curr Opin Chem Biol Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-10-12 Completed Date: 2011-01-19 Revised Date: 2013-05-28 |
Medline Journal Info:
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Nlm Unique ID: 9811312 Medline TA: Curr Opin Chem Biol Country: England |
Other Details:
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Languages: eng Pagination: 644-51 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Chemistry, The Pennsylvania State University, 414 Wartik Laboratory, University Park, PA 16802, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Biocatalysis* Enzymes / chemistry, metabolism* Humans Kinetics Magnetic Resonance Spectroscopy Molecular Dynamics Simulation Movement* |
| Grant Support | |
ID/Acronym/Agency:
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1R01GM092946/GM/NIGMS NIH HHS; GM56207/GM/NIGMS NIH HHS; R01 GM056207-12/GM/NIGMS NIH HHS; R01 GM092946/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Enzymes |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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