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- W2373951406 abstract "Drosophila alcohol dehydrogenase (ADH) is an NAD + dependent dehydrogenase. Asp38, a conserved residue appears to interact with the hydroxyl groups of the ribose moiety in the AMP portion of NAD +. Mutating Asp38 of Drosophila ADH into Asn38 decreases K m(app)NADP 62 fold and increases K cat / K m(app)NADP 590 fold at pH9.8, when compared with wild type ADH. These results suggest that Asp38 is in the NAD + binding domain and its substituent, Asn38, allows Drosophila ADH to use both NAD + and NADP + as its cofactor. The observations from the experiments of thermal denaturation and kinetic measurement with pH also confirm that the repulsion between the negative charges of Asp38 and 2′ phosphate of NADP + is the major energy barrier for NADP + to serve as a cofactor for Drosophila ADH." @default.
- W2373951406 created "2016-06-24" @default.
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- W2373951406 date "2000-01-01" @default.
- W2373951406 modified "2023-09-24" @default.
- W2373951406 title "Asp38 and the Cofactor Specificity of Drosophila Alcohol Dehydrogenase" @default.
- W2373951406 hasPublicationYear "2000" @default.
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