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KMID : 0043319950180020100
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Archives of Pharmacal Research
1995 Volume.18 No. 2 p.100 ~ p.104
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The Role of Lys-228 Residue in Horse Liver Alcohol Dehy-drogenase 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 glycineby site-directed mutagenesis. The specific activity of the mutant enzyme was increased about 4-fold nad Michaelis constants for increased by about 350-and 50-fold, respectively. The wild-type enzyme and K228TG mutant enzyme were treated with ethylacetimidate. Acetimidylation of the wild-type enzyme increased the activity about 10-fold, but the mutant enzyme ws 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 .
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KEYWORD
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Lys-228, Horse liver alcohol dehydrogenase, Site-directed mutagenesis, Glycine
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