| http://purl.uniprot.org/citations/11796116 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11796116 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11796116 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11796116 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.org/dc/terms/identifier | "doi:10.1016/S0969-2126(01)00697-9"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0969-2126(01)00697-9"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Kisker C."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Kisker C."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Truglio J.J."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Truglio J.J."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Rajagopalan K.V."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Rajagopalan K.V."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Leimkuhler S."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Leimkuhler S."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Theis K."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Theis K."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Rappa R."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/author | "Rappa R."xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/pages | "115-125"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/pages | "115-125"xsd:string |
| http://purl.uniprot.org/citations/11796116 | http://purl.uniprot.org/core/title | "Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus."xsd:string |