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I269S mutation in horse liver alcohol dehydrogenase S isoenzyme and its reactivity for steroids and retinoids

Title
I269S mutation in horse liver alcohol dehydrogenase S isoenzyme and its reactivity for steroids and retinoids
Authors
Ryu J.W.Lee K.M.
Ewha Authors
이강만
SCOPUS Author ID
이강만scopus
Issue Date
1997
Journal Title
Archives of Pharmacal Research
ISSN
0253-6269JCR Link
Citation
vol. 20, no. 2, pp. 115 - 121
Indexed
SCIE; SCOPUS; KCI scopus
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(I269S) enzyme to ethanol was increased 49-fold. All turnover numbers of I269S enzyme toward 9 primary alcohols were increased. The mutant enzyme showed 3.6, 4.6, 11.6-fold higher catalytic efficiency for 5β-androstane-3,17-dione, 5β-cholanic acid-3-one and retinal than wild-type, respectively. The reaction mechanism of I269S enzyme was ordered bi bi as wild-type's. These results indicate that the hydrophobic interaction of Ile-269 residue with coenzyme plays an important role in dissociation of coenzyme from enzyme-coenzyme complex, which has been known as the rate limiting step of ADH reaction.
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약학대학 > 약학과 > Journal papers
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