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1h1m
From Proteopedia
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{{STRUCTURE_1h1m| PDB=1h1m | SCENE= }} | {{STRUCTURE_1h1m| PDB=1h1m | SCENE= }} | ||
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===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== | |
| - | + | [[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. | |
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==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]. | ||
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| + | ==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 10:31, 16 April 2014
Contents |
CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL
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
1h1m 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
