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KMID : 0617319930030010082
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Journal of Pharmacetical Sceiences Ewha Womans University
1993 Volume.3 No. 1 p.82 ~ p.86
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Kinetic Properties of Serine-51 Mutant Yeast Alcohol Dehydrogenase
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Lee Kang-Man
Ryu Ji-Won
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Abstract
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Histidine-51 (according to the ´E´ type horse liver alcohol dehydrogenase aminoacid sesquence) in yeast alcohol degyfrogenase was mutated to seine by site-directed mutagenesis and the characterics of kinetic constants of the mutant enzyme were compared to those of native enzyme. The mutant enzyme showed a linear pH dependency of log V and log(V/K_b), and almost constant log k_b values. The changes of pH dependency in mutant enzyme suggest that His-51 plays as acceptor in proton-relay system of accohol dehydrogenase reaction.
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