1n5x
From Proteopedia
(Difference between revisions)
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===Xanthine Dehydrogenase from Bovine Milk with Inhibitor TEI-6720 Bound=== | ===Xanthine Dehydrogenase from Bovine Milk with Inhibitor TEI-6720 Bound=== | ||
{{ABSTRACT_PUBMED_12421831}} | {{ABSTRACT_PUBMED_12421831}} | ||
+ | |||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/XDH_BOVIN XDH_BOVIN]] 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. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:012421831</ref><ref group="xtra">PMID:000000000</ref><references group="xtra"/> | + | <ref group="xtra">PMID:012421831</ref><ref group="xtra">PMID:000000000</ref><references group="xtra"/><references/> |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Xanthine dehydrogenase]] | [[Category: Xanthine dehydrogenase]] |
Revision as of 06:57, 8 May 2013
Contents |
Xanthine Dehydrogenase from Bovine Milk with Inhibitor TEI-6720 Bound
Template:ABSTRACT PUBMED 12421831
Function
[XDH_BOVIN] 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.
About this Structure
1n5x is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
See Also
Reference
- Okamoto K, Eger BT, Nishino T, Kondo S, Pai EF, Nishino T. An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition. J Biol Chem. 2003 Jan 17;278(3):1848-55. Epub 2002 Nov 5. PMID:12421831 doi:10.1074/jbc.M208307200
- Steere AN, Byrne SL, Chasteen ND, Smith VC, Macgillivray RT, Mason AB. Evidence that His349 acts as a pH-inducible switch to accelerate receptor-mediated iron release from the C-lobe of human transferrin. J Biol Inorg Chem. 2010 Aug 14. PMID:20711621 doi:10.1007/s00775-010-0694-2 20711621 10.1007/s00775-010-0694-2