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• W2024492890 abstract "We previously reported that the D39N mutant of Drosophila alcohol dehydrogenase (ADH), in which Asp‐39 is replaced with asparagine, has a 60‐fold increase in affinity for NADP + and a 1.5‐fold increase in k cat compared to wild‐type ADH [Chen et al. (1991) Eur. J. Biochem. 202, 263–267] and proposed that this part of ADH is close to the 2′‐phosphate on the ribose moiety of NADP + . Here we report the effect of replacing Ala‐46 with an argine residue, an A46R mutant, on binding of NADP + to ADH and its catalytic efficiency with the NADP + cofactor, and a modeling of the three‐dimensional structure of the NAD + ‐binding region of ADH. The A46R mutant has a 2.5‐fold lower K m(app)NADP + and a 3‐fold higher k cat with NADP + compared to wild‐type ADH; binding of NAD + to the mutant was unchanged and k cat with NAD + was lowered by about 30%. For the A46R mutant, the ratio of k cat / K m of NAD + to NADP + is 85, over ten‐fold lower than that for wild‐type ADH. Our model of the 3D structure of the NAD + ‐binding region of ADH shows that Ala‐46 is over 10 Å from the ribose moiety of NAD + , which would suggest that there is little interaction between this residue and NAD + and explain why its mutation to arginine has little effect on NAD + binding. However, the positive charge at residue 46 can neutralize some of the coulombic repulsion between Asp‐39 and the 2′‐phosphate on the ribose moiety of NADP + , which would increase its affinity for the A46R mutant. We also constructed a double mutant, D39N/A46R mutant, which we find has a 30‐fold lower K m(app)NADP + and 8‐fold higher k cat with NADP + as a cofactor compared to wild‐type ADH; binding of NAD + to this double mutant was lowered by 5‐fold and k cat was increased by 1.5‐fold. As a result, k cat / K m for the double mutant was the same for NAD + and NADP + . The principle effect of the two mutations in ADH is to alter its affinity for the nucleotide cofactor; k cat decreases slightly in A46R with NAD + and remains unchanged or increases in the other mutants." @default.
• W2024492890 created "2016-06-24" @default.
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• W2024492890 date "1994-12-14" @default.
• W2024492890 modified "2023-09-26" @default.
• W2024492890 title "Adding a positive charge at residue 46 of<i>Drosophila</i>alcohol dehydrogenase increases cofactor specificity for NADP⁺" @default.
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• W2024492890 doi "https://doi.org/10.1016/0014-5793(94)01234-2" @default.
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