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Pain Management in Elderly Patients

Chapter by: Akhtar, Shamsuddin; Rappa, Roberto; Ghori, Khurrum
in: ESSENTIALS OF PAIN MANAGEMENT by
pp. 699-713
ISBN: 978-0-387-87578-1
CID: 5367382

Labor pain

Chapter by: Rappa, Roberto; Chang, K
in: Pocket pain medicine by Urman, Richard D; Vadivelu, Nalini [Eds]
Philadelphia : Wolters Kluwer Health/Lippincott Williams & Wilkins, c2011
pp. ?-
ISBN: 9781608313365
CID: 5373592

Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus

Truglio, James J; Theis, Karsten; Leimkühler, Silke; Rappa, Roberto; Rajagopalan, K V; Kisker, Caroline
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 A 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 O(2) 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 A 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.
PMID: 11796116
ISSN: 0969-2126
CID: 5367372