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KMID : 0617319930030010090
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Journal of Pharmacetical Sceiences Ewha Womans University
1993 Volume.3 No. 1 p.90 ~ p.94
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Substitution of Asp-223 Residue to Leu in Yeast Alcohol Dehydrogenase and Coenzyme Specificity
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Abstract
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Yeast alcohol dehydrogenase (YADH) has an acidic residue that interacts with the 2´- and 3´-hydroxyl groups of the adenosine ribose of the NAD^+ coenzyme. The acidic residue of Asp-223 (according to horse liver alcohol dehydrogenase amino acid sequence) is supposed to determine the coenzyme specificity for NAD^+ rather than NADP^+ and ethanol were decreased 3.5- and 4.8-fold compared to wild-type enzyme, respectively. Contrastively, catalytic specificity for NADP^+ was increased 13-fold. As a result, the mutant YADH also employed NADP^+ as a coenzyme.
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