3ax9: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_3ax9| PDB=3ax9 | SCENE= }} | {{STRUCTURE_3ax9| PDB=3ax9 | SCENE= }} | ||
===Bovine xanthine oxidase, protease cleaved form=== | |||
{{ABSTRACT_PUBMED_22145797}} | |||
=== | ==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== | ||
[[3ax9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AX9 OCA]. | [[3ax9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AX9 OCA]. | ||
==See Also== | |||
*[[Xanthine dehydrogenase|Xanthine dehydrogenase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:022145797</ref><references group="xtra"/> | <ref group="xtra">PMID:022145797</ref><references group="xtra"/><references/> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Eger, B T.]] | [[Category: Eger, B T.]] | ||
Revision as of 06:42, 29 September 2013
Bovine xanthine oxidase, protease cleaved form
Template:ABSTRACT PUBMED 22145797
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
3ax9 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
See Also
Reference
- Ishikita H, Eger BT, Okamoto K, Nishino T, Pai EF. Protein conformational gating of enzymatic activity in xanthine oxidoreductase. J Am Chem Soc. 2012 Jan 18;134(2):999-1009. Epub 2011 Dec 29. PMID:22145797 doi:https://dx.doi.org/10.1021/ja207173p