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- W2028049009 abstract "Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 Å resolution structure of Rhodobacter capsulatus XDH reveals that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition. The NAD+ binding pocket of the bacterial XDH resembles that of the dehydrogenase form of the bovine enzyme rather than that of the oxidase form, which reduces O2 instead of NAD+. The drug allopurinol is used to treat XDH-catalyzed uric acid build-up occurring in gout or during cancer chemotherapy. As a hypoxanthine analog, it is oxidized to alloxanthine, which cannot be further oxidized but acts as a tight binding inhibitor of XDH. The 3.0 Å resolution structure of the XDH-alloxanthine complex shows direct coordination of alloxanthine to the molybdenum via a nitrogen atom. These results provide a starting point for the rational design of new XDH inhibitors." @default.
- W2028049009 created "2016-06-24" @default.
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- W2028049009 date "2002-01-01" @default.
- W2028049009 modified "2023-10-16" @default.
- W2028049009 title "Crystal Structures of the Active and Alloxanthine-Inhibited Forms of Xanthine Dehydrogenase from Rhodobacter capsulatus" @default.
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- W2028049009 doi "https://doi.org/10.1016/s0969-2126(01)00697-9" @default.
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