Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이강만 | - |
dc.date.accessioned | 2018-06-02T08:15:23Z | - |
dc.date.available | 2018-06-02T08:15:23Z | - |
dc.date.issued | 1995 | - |
dc.identifier.issn | 0253-6269 | - |
dc.identifier.other | OAK-16886 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/244509 | - |
dc.description.abstract | 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(a)) 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+. | - |
dc.language | English | - |
dc.title | The role of Lys-228 residue in horse liver alcohol dehydrogenase activity | - |
dc.type | Article | - |
dc.relation.issue | 2 | - |
dc.relation.volume | 18 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.index | KCI | - |
dc.relation.startpage | 100 | - |
dc.relation.lastpage | 104 | - |
dc.relation.journaltitle | Archives of Pharmacal Research | - |
dc.identifier.scopusid | 2-s2.0-0028822393 | - |
dc.author.google | Cho S.H. | - |
dc.author.google | Ryu J.W. | - |
dc.author.google | Lee K.M. | - |
dc.contributor.scopusid | 이강만(7501506362) | - |
dc.date.modifydate | 20180601095307 | - |