Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이강만 | - |
dc.date.accessioned | 2018-06-02T08:15:38Z | - |
dc.date.available | 2018-06-02T08:15:38Z | - |
dc.date.issued | 1997 | - |
dc.identifier.issn | 0253-6269 | - |
dc.identifier.other | OAK-16738 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/244595 | - |
dc.description.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. | - |
dc.language | English | - |
dc.title | I269S mutation in horse liver alcohol dehydrogenase S isoenzyme and its reactivity for steroids and retinoids | - |
dc.type | Article | - |
dc.relation.issue | 2 | - |
dc.relation.volume | 20 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.index | KCI | - |
dc.relation.startpage | 115 | - |
dc.relation.lastpage | 121 | - |
dc.relation.journaltitle | Archives of Pharmacal Research | - |
dc.identifier.scopusid | 2-s2.0-0011109223 | - |
dc.author.google | Ryu J.W. | - |
dc.author.google | Lee K.M. | - |
dc.contributor.scopusid | 이강만(7501506362) | - |
dc.date.modifydate | 20180601094926 | - |