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The kinetic characteristics of K228G mutant horse liver alcohol dehydrogenase

Title
The kinetic characteristics of K228G mutant horse liver alcohol dehydrogenase
Authors
Cho S.H.Ryu J.W.Lee K.M.
Ewha Authors
이강만
SCOPUS Author ID
이강만scopus
Issue Date
1999
Journal Title
Archives of Pharmacal Research
ISSN
0253-6269JCR Link
Citation
vol. 22, no. 1, pp. 13 - 17
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
The kinetic constants and the reaction mechanism of the K228G mutant horse liver alcohol dehydrogenase isoenzyme E (HLADH-E) were compared to the wild-type enzyme. All the Km and Ki constants of the mutant enzyme for NAD+, ethanol, acetaldehyde and NADH were larger than those of the wild-type enzyme. The dissociation constants for the NADH and NAD+ (Kiq and Kia) were greatly increased by 130- and 460-fold, respectively. The product inhibition patterns suggested that the reaction mechanism of the mutant enzyme was changed to Random Bi Bi. These results could attribute to the increase in the dissociation rate of coenzyme with the substitution at Lys-228 residue.
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약학대학 > 약학과 > Journal papers
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