1h1m: Difference between revisions

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[[Image:1h1m.png|left|200px]]
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{{STRUCTURE_1h1m|  PDB=1h1m  |  SCENE=  }}  
{{STRUCTURE_1h1m|  PDB=1h1m  |  SCENE=  }}  
===CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL===
===CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL===
{{ABSTRACT_PUBMED_12486225}}


 
==Function==
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[[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.
The line below this paragraph, {{ABSTRACT_PUBMED_12486225}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12486225}}


==About this Structure==
==About this Structure==
[[1h1m]] 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=1H1M OCA].  
[[1h1m]] 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=1H1M 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 13:31, 16 April 2014

Template:STRUCTURE 1h1m

CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROLCRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL

Template:ABSTRACT PUBMED 12486225

FunctionFunction

[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 StructureAbout this Structure

1h1m is a 4 chain structure with sequence from Aspergillus japonicus. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. ↑ 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

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