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
-
1.13.11.24
-
flavonols
-
dioxygenation
-
bicupins
-
o-heterocycle
-
oxygenolysis
-
synthesis
- 1.13.11.24
- flavonols
-
dioxygenation
-
bicupins
-
o-heterocycle
-
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
1.13.11.24 quercetin 2,3-dioxygenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.13.11.24 - quercetin 2,3-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,7,3',4'-tetrahydroxyflavone + O2
?
-
35% of the activity with quercetin, Co-QueD, 15% of the activity with quercetin, Ni-QueD
-
-
?
morin + O2
?
i.e. 3,5,7,2',4'-pentahydroxyflavone, 1.7% of the activity with quercetin
-
-
?
3,5,7,2',4'-pentahydroxyflavone + O2
?
-
5.5% of the activity with quercetin, Co-QueD, 0.9% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7,2',4'-pentahydroxyflavone + O2
?
Streptomyces sp. FLA / DSM 41951
-
5.5% of the activity with quercetin, Co-QueD, 0.9% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7,3',4',5'-hexahydroxyflavone + O2
?
-
77% of the activity with quercetin, Co-QueD, 46% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7,3',4',5'-hexahydroxyflavone + O2
?
Streptomyces sp. FLA / DSM 41951
-
77% of the activity with quercetin, Co-QueD, 46% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7,4'-tetrahydroxyflavone + O2
?
-
43% of the activity with quercetin, Co-QueD, 29% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7,4'-tetrahydroxyflavone + O2
?
Streptomyces sp. FLA / DSM 41951
-
43% of the activity with quercetin, Co-QueD, 29% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7-trihydroxyflavone + O2
?
-
13% of the activity with quercetin, Co-QueD, 16% of the activity with quercetin, Ni-QueD
-
-
?
3,5,7-trihydroxyflavone + O2
?
Streptomyces sp. FLA / DSM 41951
-
13% of the activity with quercetin, Co-QueD, 16% of the activity with quercetin, Ni-QueD
-
-
?
fisetin + O2
2-[[(3,4-dihydroxyphenyl)carbonyl]oxy]-4-hydroxybenzoate + CO
-
1.22% activity compared to quercetin
-
-
?
fisetin + O2
2-[[(3,4-dihydroxyphenyl)carbonyl]oxy]-4-hydroxybenzoate + CO
-
1.22% activity compared to quercetin
-
-
?
fisetin + O2
?
i.e. 3,7,3',4'-tetrahydroxyflavone, 23% of the activity with quercetin
-
-
?
fisetin + O2
?
Streptomyces sp. FLA / DSM 41951
i.e. 3,7,3',4'-tetrahydroxyflavone, 23% of the activity with quercetin
-
-
?
galangin + O2
2,4-dihydroxy-6-[(phenylcarbonyl)oxy]benzoate + CO
-
110% activity compared to quercetin
-
-
?
galangin + O2
2,4-dihydroxy-6-[(phenylcarbonyl)oxy]benzoate + CO
-
110% activity compared to quercetin
-
-
?
galangin + O2
?
i.e. 3,5,7-trihydroxyflavone, 28% of the activity with quercetin
-
-
?
galangin + O2
?
Streptomyces sp. FLA / DSM 41951
i.e. 3,5,7-trihydroxyflavone, 28% of the activity with quercetin
-
-
?
kaempferol + O2
?
activity is 2.18fold higher than with quercetin
-
-
?
kaempferol + O2
?
i.e. 3,5,7,4'-tetrahydroxyflavone. 70% of the activity with quercetin
-
-
?
myricetin + O2
?
i.e. 3,5,7,3',4',5'-hexahydroxyflavone. 49% of the activity with quercetin
-
-
?
myricetin + O2
?
Streptomyces sp. FLA / DSM 41951
i.e. 3,5,7,3',4',5'-hexahydroxyflavone. 49% of the activity with quercetin
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
transcription of queD is triggered by quercetin and its 3-O-rhamnosylglucoside rutin, but not by the flavonol morin (3,5,7,2',4'-pentahydroxyflavone), the presumed quercetin degradation products protocatechuate and 2,4,6-trihydroxybenzoate or the sugars rhamnose and glucose. Quercetin-induced queD expression is not influenced by the presence of Ni(II)
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
Streptomyces sp. FLA / DSM 41951
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
Streptomyces sp. FLA / DSM 41951
transcription of queD is triggered by quercetin and its 3-O-rhamnosylglucoside rutin, but not by the flavonol morin (3,5,7,2',4'-pentahydroxyflavone), the presumed quercetin degradation products protocatechuate and 2,4,6-trihydroxybenzoate or the sugars rhamnose and glucose. Quercetin-induced queD expression is not influenced by the presence of Ni(II)
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
the mechanism consists in four successive steps, the first one concerns addition of O2 on the C2 carbon atom, the second corresponds to the closure of the endoperoxo intermediate. In the two last steps, bonds are broken to produce the depside and carbon monoxide. Addition of dioxygen on the C2 atom (step 1) is associated to a pyramidalization at the C2 carbon atom and to a rotation of the B-ring with respect to the conjugated A-C rings. The second step is the rate limiting one and the free energy barriers characterized for the four flavonoids are very close, reaching about 24 kcal/mol. Differences in the values are not significant enough to be exploited to rationalize the nonlinear evolution of the degradation rate. Moreover, the relatively high energy value is expected to be lowered by taking into account the whole environment
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
cleavages of the C2-C3 and C3-C4 bonds of quercetin (Que) catalyzed by 2,4-QDs
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
quercetin dioxygenase catalyzes the oxidation of the flavonol quercetin with dioxygen, cleaving the central heterocyclic ring and releasing CO
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
Streptomyces sp. FLA / DSM 41951
-
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
?
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
quercetin is a flavonol
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
low activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
100% activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
100% activity
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
Streptomyces sp. FLA / DSM 41951
-
-
-
-
?
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
Streptomyces sp. FLA / DSM 41951
-
-
-
?
tamarixetin + O2
2,4-dihydroxy-6-[[(3-hydroxy-4-methoxyphenyl)carbonyl]oxy]benzoate + CO
-
82.4% activity compared to quercetin
-
-
?
tamarixetin + O2
2,4-dihydroxy-6-[[(3-hydroxy-4-methoxyphenyl)carbonyl]oxy]benzoate + CO
-
82.4% activity compared to quercetin
-
-
?
additional information
?
-
quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols
-
-
?
additional information
?
-
-
quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols
-
-
?
additional information
?
-
-
the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol
-
-
?
additional information
?
-
-
quercetin 2,3-dioxygenase activates molecular oxygen to catalyze the oxygenative ring-opening reaction of the O-heterocycle of quercetin to the corresponding depside (phenolic carboxylic acid esters) and carbon monoxide
-
-
?
additional information
?
-
-
a flavonolate ion (fla-, deprotonated substrate) is bound through the 3-hydroxy group to the copper(II) ion, which exhibits a distorted squarepyramidal geometry. The bound substrate is stabilized by Glu73 through a hydrogen-bonding interaction. Synthesis of a set of copper(II) complexes [CuIILn(AcO)] and their flavonolate adducts [CuIILn(fla)] with the series of carboxyl-group-containing ligands LnH, the treatment of the ligands with CuII(OAc)2xH2O gives the corresponding mononuclear copper(II) complexes [CuIILn(OAc)], dioxygenation of flavonol catalyzed by the binary complexes [CuIILn(AcO)] (multiturnover reaction), kinetics, overview
-
-
?
additional information
?
-
-
computational study on the dioxygenation reaction of the substrate flavonolate (fla) by a synthetic model complex and related species mimicking quercetin 2,4-dioxygenases, overview. The reaction mechanism obtained for the present biomimetic complexes is substantially different from the plausible enzymatic reaction. All model complexes favor a single electron transfer from flavonolate to dioxygen over a valence tautomerism, and a subsequent intersystem crossing and a ring-closure lead to a formation of a 1,2-dioxetane intermediate instead of undergoing a direct formation of a precursor endoperoxide. The generation of the 1,2-dioxetane intermediate is shown to be the rate-determining step and inclusion of a carboxylate co-ligand can enhance the reactivity, rendering this process barrier-free. Proposal of a pathway, which can circumvent a non-enzymatic reaction by involving conversion from the 1,2-dioxetane to the endoperoxide with lower barriers
-
-
?
additional information
?
-
-
the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol
-
-
?
additional information
?
-
-
Mn-QDO in absence of O2 shows ability to react with nitroxyl (HNO)-singly reduced form of NO. HNO is incorporated into quercetin in the same manneras dioxygen, yet the reaction is strictly regioselective, as the only product is 2-((3,4-dihydroxyphenyl)(imino)methoxy)-4,6-dihydroxybenzoate
-
-
?
additional information
?
-
-
high level of pirin leads to the resistance of poliovirus replication to quercetin by inactivating this flavonoid
-
-
?
additional information
?
-
flavonol, morin, 3,6-dihydroxyflavone and 3,7-dihydroxyflavone are transformed at a rate of less than 1% of that found for quercetin
-
-
?
additional information
?
-
-
flavonol, morin, 3,6-dihydroxyflavone and 3,7-dihydroxyflavone are transformed at a rate of less than 1% of that found for quercetin
-
-
?
additional information
?
-
-
the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol
-
-
?
additional information
?
-
-
the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol
-
-
?
additional information
?
-
Streptomyces sp. FLA / DSM 41951
-
the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol
-
-
?
