1h1i
From Proteopedia
(Difference between revisions)
m (Protected "1h1i" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | [[Image:1h1i.png|left|200px]] | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_1h1i", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_1h1i| PDB=1h1i | SCENE= }} | {{STRUCTURE_1h1i| PDB=1h1i | SCENE= }} | ||
- | |||
===CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE QUERCETN=== | ===CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE QUERCETN=== | ||
+ | {{ABSTRACT_PUBMED_12486225}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/QDOI_ASPJA QDOI_ASPJA]] Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds. | |
- | + | ||
- | + | ||
- | -- | + | |
- | + | ||
==About this Structure== | ==About this Structure== | ||
[[1h1i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_japonicus Aspergillus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1I OCA]. | [[1h1i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_japonicus Aspergillus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1I OCA]. | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Dioxygenase|Dioxygenase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:012486225</ref><references group="xtra"/> | + | <ref group="xtra">PMID:012486225</ref><references group="xtra"/><references/> |
[[Category: Aspergillus japonicus]] | [[Category: Aspergillus japonicus]] | ||
[[Category: Quercetin 2,3-dioxygenase]] | [[Category: Quercetin 2,3-dioxygenase]] |
Revision as of 10:40, 16 April 2014
Contents |
CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE QUERCETN
Template:ABSTRACT PUBMED 12486225
Function
[QDOI_ASPJA] Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
About this Structure
1h1i is a 4 chain structure with sequence from Aspergillus japonicus. Full crystallographic information is available from OCA.
See Also
Reference
- Steiner RA, Kalk KH, Dijkstra BW. Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16625-30. Epub 2002 Dec 16. PMID:12486225 doi:10.1073/pnas.262506299