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KMID : 0617319950050010060
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Journal of Pharmacetical Sceiences Ewha Womans University
1995 Volume.5 No. 1 p.60 ~ p.64
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The Role of Lys-228 Residue in Horse Liver Alcohol Dehydrogenase Activity
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Cho, Sun Hyoung
Ryu, Ji Won/Lee, Kang Man
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Abstract
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Lys-228 in horse liver alcohol dehydrogenase isoenzyme E (HLADH-E) was mutated to glycine by site-directed mutagenesis. The specific activity of the mutant enzyme was increased about 4-fold and Michaelis constants for NAD^+ (K_d) and NADH (K_q) increased by about 350 and 50-fold, respectively. The wild-type enzyme and K228G mutant enzyme were treated with ethylacetimidate. Acetimidylation of the wild-type enzyme increased the activity about 10-fold, but the mutant enzyme was little affected. These results confirm that Lys-228 residue plays an important role in the activity of the enzyme through forming the hydrogen bond with adenosine ribose of NAD^+.
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