Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases.
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.
Departments of Chemistry and Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Zhao-Xun
ZX
Liang
Iason
I
Tsigos
Vassilis
V
Bouriotis
Judith P
JP
Klinman
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D019905:Benzyl Alcohol / Q000737:chemistry / Q000378:metabolism; D004789:Enzyme Activation; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D006859:Hydrogen / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D009016:Moraxella / Q000201:enzymology; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D013816:Thermodynamics
D009243:NAD; D006859:Hydrogen; D000426:Alcohol Dehydrogenase; D019905:Benzyl Alcohol