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Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair
Umeå University, Faculty of Science and Technology, Chemistry.
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2004 (English)In: Nature Structural & Molecular Biology, Vol. 11, 945-9 p.Article in journal (Refereed) Published
Abstract [en]

A fundamental question is how enzymes can accelerate chemical reactions. Catalysis is not only defined by actual chemical steps, but also by enzyme structure and dynamics. To investigate the role of protein dynamics in enzymatic turnover, we measured residue-specific protein dynamics in hyperthermophilic and mesophilic homologs of adenylate kinase during catalysis. A dynamic process, the opening of the nucleotide-binding lids, was found to be rate-limiting for both enzymes as measured by NMR relaxation. Moreover, we found that the reduced catalytic activity of the hyperthermophilic enzyme at ambient temperatures is caused solely by a slower lid-opening rate. This comparative and quantitative study of activity, structure and dynamics revealed a close link between protein dynamics and catalytic turnover.

Place, publisher, year, edition, pages
2004. Vol. 11, 945-9 p.
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URN: urn:nbn:se:umu:diva-14785DOI: doi:10.1038/nsmb821OAI: oai:DiVA.org:umu-14785DiVA: diva2:154457
Available from: 2007-06-18 Created: 2007-06-18 Last updated: 2011-01-12Bibliographically approved

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Wolf-Watz, Magnus

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