1.13.11.24: quercetin 2,3-dioxygenase

This is an abbreviated version!
For detailed information about quercetin 2,3-dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.24

Reaction

quercetin
+
O2
=
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate
+
CO
+
H+

Synonyms

2,3-QD, 2,3QD, 2,4-QD, Co-QDO, Co-QueD, Cu2+-containing 2,4-QD, cupin domain-containing protein, Fe-QDO, Fe-QueD, flavonol 2,4-dioxygenase, flavonol 2,4-oxygenase, manganese quercetin 2,3-dioxygenase, manganese quercetin dioxygenase, Mn-QDO, Mn-QueD, Ni-QueD, nickel quercetinase, pirin, QDO, QdoI, QueD, quercetin 2,4-dioxygenase, quercetin dioxygenase, quercetinase, type III extradiol dioxygenase, VdQase, YxaG

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.24 quercetin 2,3-dioxygenase

Metals Ions

Metals Ions on EC 1.13.11.24 - quercetin 2,3-dioxygenase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Fe3+
enzyme-bound
HNO
-
nitrosyl hydride replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase resulting in the incorporation of both N and O atoms into the product. Turnover is demonstrated by consumption of quercetin and other related substrates under anaerobic conditions in the presence of HNO-releasing compounds and the enzyme. As with dioxygenase activity, a nonenzymatic base-catalyzed reaction of quercetin with HNO isobserved above pH 7, but no enhancement of this basal reactivity is found upon addition of divalent metal salts. Unique and regioselective N-containing products are characterized by MS analysis for both the enzymatic and nonenzymatic reactions
Iron
different coordination geometry in the two active sites of the dimer
additional information