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- W2891492430 abstract "The conformation of NADP+ in glucose-6-phosphate-dehydrogenase—NADP+ binary complexes has been investigated using proton-proton transferred nuclear Overhauser enhancement measurements to determine inter-proton distance ratios between bound NADP+ protons. The enzymes from Saccharomyces cerevisiae (brewer's yeast and baker's yeast) and Hansenula jadinii (Candida utilis, Torula utilis) form binary complexes with NADP+ in which the glycosidic bond of the adenine moiety is in the anti conformation whereas that of the nicotinamide moiety exists as a syn (69–70%)/anti (30–40%) mixture. The enzymes have similar subunit sizes (Mr∼58000) and it is shown that they bind NADP+ in essentially similar conformations. Inactivation of the baker's yeast enzyme with acetylsalicylic acid caused little if any alteration in the conformation of bound NADP+, and the presence of NADP+ during inactivation afforded very little protection to the enzyme. Inactivation rates were, however, lower in the presence of glucose 6-phosphate. It is concluded that the ɛ-amino group of the lysine residue that is acetylated during the inactivation reaction with acetylsalicylic acid is not necessary for binary complex formation between the enzyme and NADP+, but that it is situated in a part of the molecule affected by formation of the enzyme—glucose-6-phosphate complex. The implication of the findings for the catalytic process, and related evolutionary aspects, are discussed briefly." @default.
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- W2891492430 date "1984-12-01" @default.
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- W2891492430 title "Glucose-6-phosphate dehydrogenase. A transferred nuclear Overhauser enhancement study of NADP+ conformations in enzyme-coenzyme binary complexes" @default.
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- W2891492430 doi "https://doi.org/10.1111/j.1432-1033.1984.tb08563.x" @default.
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