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
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1.13.11.24
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flavonols
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dioxygenation
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bicupins
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o-heterocycle
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oxygenolysis
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synthesis
- 1.13.11.24
- flavonols
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dioxygenation
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bicupins
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o-heterocycle
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oxygenolysis
- synthesis
Reaction
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
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Reaction
Reaction on EC 1.13.11.24 - quercetin 2,3-dioxygenase
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quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
EPR study, mechanism, N of His112 is the axial ligand of type II copper site
quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
hybrid density functional theory study on mechanism, dioxygen attack on copper is energetically preferred
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quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
structure-function analysis of the active site
quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
study on mobility and flexibility of substrate cavity, molecular dynamics simulations
quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
possible reaction mechanisms and pathways, kinetics, detailed overview
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quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
reaction mechanism, overview. Quantum mechanics/molecular mechanics (QM/MM) and QM-only study on the oxidative ring-cleaving reaction of quercetin catalyzed by quercetin 2,4-dioxygenase, i.e. 2,4-QD, which has a mononuclear type 2 copper center and incorporates two oxygen atoms at C2 and C4 positions of the substrate. Dioxygen is more likely to bind to a Cu2+ ion than to a substrate radical, involving the dissociation of the substrate from the copper ion. Then a Cu2+-alkylperoxo complex can be generated. Steric effects of the protein environment contribute to maintain the orientation of the substrate dissociated from the copper center. A prior rearrangement of the Cu2+-alkylperoxo complex and a subsequent hydrogen bond switching assisted by the movement of Glu73 can facilitate formation of an endoperoxide intermediate selectively. Reaction mechanism for endoperoxide formation, overview
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quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
the enzyme incorporates both atoms of dioxygen into the substrate by cleaving the central heterocycle ring and releasing CO. The enzyme activates quercetin through deprotonation and the proton acceptor-Glu69 needs to reorient for the reaction to proceed. Energy profiles and reaction schemes for nonenzymatic nitroxygenation of quercetin monoanion. Transient and intermediate structures, catalytic mechaanism, detailed overview
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