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1h1m
From Proteopedia
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Revision as of 13:20, 30 October 2007
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CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL
Overview
Quercetin 2,3-dioxygenase (2,3QD) is the only firmly established copper, dioxygenase known so far. Depending solely on a mononuclear Cu center, it, catalyzes the breakage of the O-heterocycle of flavonols, producing more, easily degradable phenolic carboxylic acid ester derivatives. In the, enzymatic process, two CC bonds are broken and concomitantly carbon, monoxide is released. The x-ray structures of Aspergillus japonicus 2,3QD, anaerobically complexed with the substrate kaempferol and the natural, substrate quercetin have been determined at 1.90- and 1.75-A resolution, respectively. Flavonols coordinate to the copper ion as monodentate, ligands through their 3OH group. They occupy a shallow and overall, hydrophobic cavity proximal to the metal center. As a result of a van der, Waals ... [(full description)]
About this Structure
1H1M is a [Single protein] structure of sequence from [Aspergillus japonicus] with NAG, CU, KMP and MPD as [ligands]. Active as [Quercetin 2,3-dioxygenase], with EC number [1.13.11.24]. Structure known Active Site: CUA. Full crystallographic information is available from [OCA].
Reference
Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase., Steiner RA, Kalk KH, Dijkstra BW, Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16625-30. Epub 2002 Dec 16. PMID:12486225
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Categories: Aspergillus japonicus | Quercetin 2,3-dioxygenase | Single protein | Dijkstra, B.W. | Steiner, R.A. | CU | KMP | MPD | NAG | Copper | Dioxygenase | Flavonol | Oxidoreductase
