Cho S H, Ryu J W, Lee K M
College of Pharmacy, Ewha Womans University, Seoul, Korea.
Arch Pharm Res. 1999 Feb;22(1):13-7. doi: 10.1007/BF02976429.
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.
