Literature DB >> 15291528

Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases.

Zhao-Xun Liang1, Iason Tsigos, Vassilis Bouriotis, Judith P Klinman.   

Abstract

The hydride transfer catalyzed by thermophilic alcohol dehydrogenase (htADH) exhibits sharply different kinetic and activation parameters from that catalyzed by the more flexible psychrophilic alcohol dehydrogenase (psADH). In addition, the hydride transfer in htADH is affected by mutating two distal residues that are suggested to be responsible for the decreased local protein flexibility in htADH. These observations provide support for the view that protein dynamics is tightly coupled to the hydrogen-transfer processes in these enzymes.

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Year:  2004        PMID： 15291528     DOI： 10.1021/ja047087z

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


  25 in total

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Review 6.  The effect of temperature on enzyme activity: new insights and their implications.

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Journal:  J Biol Chem       Date:  2013-03-22       Impact factor: 5.157

Review 9.  Evolutionary aspects of enzyme dynamics.

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10.  An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organisms.

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Journal:  Biochemistry       Date:  2009-08-25       Impact factor: 3.162
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