Archives of Pharmacal Research
- Volume 20 Issue 2
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- Pages.115-121
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- 1997
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- 0253-6269(pISSN)
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- 1976-3786(eISSN)
1269S mutation in horse liver alcohol dehydrogenase S isoenzyme and its reactivity for steroids and retinoids
- Ryu, Ji-Won (College of Pharmacy, Ewha Womans University) ;
- Lee, Kang-Man (College of Pharmacy, Ewha Womans University)
- Published : 1997.04.01
Abstract
Ile-269 in horse liver alcohol dehydrogenase isoenzyme S(HLADH-S) was mutated to serine by phosphorothioate-based site-directed mutagenesis in order to study the role of the residue in coenzyme binding. The specific activity of the mutant(1269S) enzyme to ethanol was increased 49-fold. All turnover numbers of 1269S enzyme toward 9 primary alcohols were increased. The mutant enzyme showed 3.6, 4.6, 11.6-fold higher catalytic efficiency for
Keywords
- 1269S;
- Horse liver alcohol dehydrogenase S isoenzyme;
- Site-directed mutagenesis;
- Coenzyme binding site;
- Steroids;
- Retinoids