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

Zhao Xun Liang; Iason Tsigos; Vassilis Bouriotis; Judith P. Klinman

doi:10.1021/ja047087z

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

Zhao Xun Liang, Iason Tsigos, Vassilis Bouriotis, Judith P. Klinman^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

51 Citations (Scopus)

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.

Original language	English
Pages (from-to)	9500-9501
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	31
DOIs	https://doi.org/10.1021/ja047087z
Publication status	Published - Aug 11 2004
Externally published	Yes

ASJC Scopus Subject Areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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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.",

author = "Liang, {Zhao Xun} and Iason Tsigos and Vassilis Bouriotis and Klinman, {Judith P.}",

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T1 - Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases

AU - Liang, Zhao Xun

AU - Tsigos, Iason

AU - Bouriotis, Vassilis

AU - Klinman, Judith P.

PY - 2004/8/11

Y1 - 2004/8/11

N2 - 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.

AB - 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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ER -

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

Abstract

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