Structural highlights
Function
[XDH_RAT] Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.[1]
Publication Abstract from PubMed
Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 A and of the reduced bovine milk enzyme at 2.1 A, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine.
Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate.,Okamoto K, Kawaguchi Y, Eger BT, Pai EF, Nishino T J Am Chem Soc. 2010 Nov 15. PMID:21077683[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Asai R, Nishino T, Matsumura T, Okamoto K, Igarashi K, Pai EF, Nishino T. Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase. J Biochem. 2007 Apr;141(4):525-34. Epub 2007 Feb 14. PMID:17301076 doi:10.1093/jb/mvm054
- ↑ Okamoto K, Kawaguchi Y, Eger BT, Pai EF, Nishino T. Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate. J Am Chem Soc. 2010 Nov 15. PMID:21077683 doi:10.1021/ja1077574
