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Enzyme Name | UniProtKB | KEGG |
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| Q7SIC2 |
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Protein name | Quercetin 2,3-dioxygenase | Quercetin 2,3-dioxygenaseQuercetinaseFlavonol 2,4-oxygenase |
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Synonyms | EC 1.13.11.242,3QDQuercetinaseFlavonol 2,4-dioxygenase |
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UniProtKB:Accession Number | Q7SIC2 |
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Entry name | QDOI_ASPJA |
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Activity | Quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+. |
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Subunit | Homodimer. |
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Subcellular location |
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Cofactor | Binds 1 copper ion per subunit. |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[3] | p.7961 |
| [4] | Fig.5, p.7976 |
| [5] | Fig.4, p.16629-16630 |
| [6] | p.264-265 |
| [10] | Fig.3, p.782-784 |
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references | [1] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
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PubMed ID | 10876237 |
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Journal | Nat Struct Biol |
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Year | 2000 |
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Volume | 7 |
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Pages | 542-6 |
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Authors | Titus GP, Mueller HA, Burgner J, Rodriguez De Cordoba S, Penalva MA, Timm DE |
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Title | Crystal structure of human homogentisate dioxygenase. |
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Related PDB | 1ey2,1eyb |
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Related UniProtKB | Q93099 |
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[2] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). |
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PubMed ID | 11062559 |
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Journal | Nat Struct Biol |
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Year | 2000 |
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Volume | 7 |
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Pages | 1036-40 |
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Authors | Woo EJ, Dunwell JM, Goodenough PW, Marvier AC, Pickersgill RW |
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Title | Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. |
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Related PDB | 1fi2 |
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Related UniProtKB | P45850 |
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[3] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DIETHYLDITHIOCARBAMATE AND KOJIC ACID. |
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PubMed ID | 12069585 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 7955-62 |
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Authors | Steiner RA, Kooter IM, Dijkstra BW |
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Title | Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights. |
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Related PDB | 1gqg,1gqh |
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Related UniProtKB | Q7SIC2 |
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[4] |
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PubMed ID | 12069586 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 7963-8 |
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Authors | Steiner RA, Meyer-Klaucke W, Dijkstra BW |
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Title | Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin. |
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[5] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KAEMPFEROL AND QUERCETIN. |
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PubMed ID | 12486225 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 2002 |
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Volume | 99 |
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Pages | 16625-30 |
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Authors | Steiner RA, Kalk KH, Dijkstra BW |
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Title | Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. |
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Related PDB | 1h1i,1h1m |
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Related UniProtKB | Q7SIC2 |
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[6] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), MUTAGENESIS OF GLU-73. |
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PubMed ID | 11839311 |
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Journal | Structure |
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Year | 2002 |
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Volume | 10 |
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Pages | 259-68 |
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Authors | Fusetti F, Schroter KH, Steiner RA, van Noort PI, Pijning T, Rozeboom HJ, Kalk KH, Egmond MR, Dijkstra BW |
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Title | Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. |
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Related PDB | 1juh |
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Related UniProtKB | Q7SIC2 |
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[7] |
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PubMed ID | 14741339 |
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Journal | FEBS Lett |
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Year | 2004 |
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Volume | 557 |
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Pages | 45-8 |
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Authors | Bowater L, Fairhurst SA, Just VJ, Bornemann S |
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Title | Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. |
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[8] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
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PubMed ID | 15628860 |
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Journal | Biochemistry |
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Year | 2005 |
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Volume | 44 |
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Pages | 193-201 |
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Authors | Gopal B, Madan LL, Betz SF, Kossiakoff AA |
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Title | The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s). |
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Related PDB | 1y3t |
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Related UniProtKB | P42106 |
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[9] |
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PubMed ID | 16411777 |
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Journal | Biochemistry |
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Year | 2006 |
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Volume | 45 |
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Pages | 1009-16 |
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Authors | Schaab MR, Barney BM, Francisco WA |
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Title | Kinetic and spectroscopic studies on the quercetin 2,3-dioxygenase from Bacillus subtilis. |
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[10] |
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Journal | Coord Chem Rev |
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Year | 2010 |
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Volume | 254 |
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Pages | 781-793 |
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Authors | Pap JS, Kaizer J, Speier G |
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Title | Model systems for the CO-releasing flavonol 2,4-dioxygenase enzyme |
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comments | This enzyme belongs to the cupin superfamily. This enzymes, Quercetin 2,3-dioxygenase (EC=1.13.11.24), is high similarity to Oxalate oxidase 1 (EC=1.2.3.4, S00145 in EzCatDB, literature [2]) and a counterpart enzyme from Bacillus (D00843 in EzCatDB). According to the literature [3],[5] and [10], there are two alternative cordination forms fot the copper ion in this enzyme: (1) the cooper is ligated by three histidine residues and a water in a distorted tetrahedral geometry. (2) the copper is ligated by a glutamate residue along with the histidine residues and the water in a trigonal bipyramidal geometry. In substrate binding, the water can be replaced by the hydroxyl oxygen (O3 atom) of the substrate, quercetin. Moreover, the glutamate residue (Glu73 in 1gqg) acts as a general base to deprotonate the O3 atom, leading to the radical formation at the C2 atom. This activation seems to allow it react with the triplet dioxygen (see [5] and [10]).
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created | updated |
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2010-04-22 | 2011-05-18 |
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