Information on EC 1.13.11.24 - quercetin 2,3-dioxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.13.11.24
-
RECOMMENDED NAME
GeneOntology No.
quercetin 2,3-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rutin degradation
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-
SYSTEMATIC NAME
IUBMB Comments
quercetin:oxygen 2,3-oxidoreductase (decyclizing)
The enzyme from Aspergillus sp. is a copper protein whereas that from Bacillus subtilis contains iron. Quercetin is a flavonol (5,7,3',4'-tetrahydroxyflavonol).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-67-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MTCC-1783
-
-
Manually annotated by BRENDA team
strain MTCC-1883
-
-
Manually annotated by BRENDA team
strain MTCC-1884
-
-
Manually annotated by BRENDA team
strain MTCC-2206
-
-
Manually annotated by BRENDA team
strain MTCC-2456
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-
Manually annotated by BRENDA team
PRL 1805
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-
Manually annotated by BRENDA team
DSM 821, grown on rutin
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,5,7,2',4'-pentahydroxyflavone + O2
?
show the reaction diagram
3,5,7,3',4',5'-hexahydroxyflavone + O2
?
show the reaction diagram
3,5,7,4'-tetrahydroxyflavone + O2
?
show the reaction diagram
3,5,7-trihydroxyflavone + O2
?
show the reaction diagram
3,7,3',4'-tetrahydroxyflavone + O2
?
show the reaction diagram
-
35% of the activity with quercetin, Co-QueD, 15% of the activity with quercetin, Ni-QueD
-
-
?
fisetin + O2
2-[[(3,4-dihydroxyphenyl)carbonyl]oxy]-4-hydroxybenzoate + CO
show the reaction diagram
fisetin + O2
?
show the reaction diagram
galangin + O2
2,4-dihydroxy-6-[(phenylcarbonyl)oxy]benzoate + CO
show the reaction diagram
galangin + O2
?
show the reaction diagram
kaempferol + O2
?
show the reaction diagram
morin + O2
?
show the reaction diagram
i.e. 3,5,7,2',4'-pentahydroxyflavone, 1.7% of the activity with quercetin
-
-
?
myricetin + O2
?
show the reaction diagram
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
show the reaction diagram
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
show the reaction diagram
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
show the reaction diagram
tamarixetin + O2
2,4-dihydroxy-6-[[(3-hydroxy-4-methoxyphenyl)carbonyl]oxy]benzoate + CO
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO
show the reaction diagram
quercetin + O2
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
show the reaction diagram
quercetin + O2
2-protocatechoylphloroglucinolcarboxylate + CO
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
a non-heme redox metalloenzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1Z,3Z)-N,N'-di(pyridin-2-yl)-1H-isoindole-1,3(2H)-diimine
-
-
1,10-phenanthroline
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0.21 mM, 46% residual activity
1H-2-benzyl-3-hydroxy-4-oxoquinolin
competitive
2,2'-dipyridyl
-
0.18 mM, 57% residual activity
2-(4-{bis[1-methyl-2-(propan-2-yl)-1H-imidazol-4-yl]methyl}-1-methyl-1H-imidazol-2-yl)-2-methylpropanoic acid
-
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2-mercaptoethanol
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2-{4-[hydroxy(di-1H-imidazol-4-yl)methyl]-1H-imidazol-2-yl}-2-methylpropanoic acid
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3-hydroxyflavone
-
competitive inhibition
8-hydroxyquinoline
alpha-alpha'-dipyridyl
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at 1 mM or more
alpha-naphthoquinoline
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chloro[(4-phenoxy-1,4,7-triazonan-1-yl-kappa3N1,N4,N7)acetato-kappaO]copper
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diethyldithiocarbamate
Diphenylthiocarbazone
-
-
Dithiol
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at microM concentrations or less
dithiothreitol
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Dithizone
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at microM concentrations or less
DTT
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Mn QueD: 96% activity remains after 15 min incubation with 1 mM reagent
ethylxanthate
H2O2
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Co QueD: 93% activity remains after 15 min incubation with 1 mM reagent, Mn QueD: 82% activity remains after 15 min incubation with 1 mM reagent
kojic acid
morin
-
competitive inhibition
NaCN
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Co QueD: 91% activity remains after 15 min incubation with 1 mM reagent, Mn QueD: 89% activity remains after 15 min incubation with 1 mM reagent
O-ethylxanthate
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6 mM, 51% residual activity
O-ethylxanthic acid
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Co QueD: 69% activity remains after 15 min incubation with 1 mM reagent, Mn QueD: 100% activity remains after 15 min incubation with 1 mM reagent
o-phenanthroline
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at 1 mM or more
Quinoline
-
-
Sodium ascorbate
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Mn QueD: 80% activity remains after 15 min incubation with 1 mM reagent
Sodium dithionite
-
-
Toluene-3,4-dithiol
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[3-(hydroxy-kappaO)-2-phenyl-4H-chromen-4-onato-kappaO4][bis(triphenylphosphane)]copper
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{N,N-bis[(1-methyl-1H-imidazol-4-yl-kappaN3)methyl]glycinato-kappa2N,O}(dichloro)ferrate(1-)
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
-
Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent
EDTA
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Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent
NaN3
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Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent, Mn QueD = 100% activity remains after 15 min incubation with 1 mM reagent
Sodium ascorbate
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Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent
Tiron
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0.8 mM, 25% activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085
fisetin
pH 6, 25C
0.02
galangin
pH 6, 25C
0.013
kaempferol
pH 6, 25C
0.079 - 0.15
oxygen
0.0008 - 0.019
quercetin
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56.7
fisetin
Penicillium olsonii
A7Y9J1
pH 6, 25C
33.3
galangin
Penicillium olsonii
A7Y9J1
pH 6, 25C
466.7
kaempferol
Penicillium olsonii
A7Y9J1
pH 6, 25C
12.5 - 19
O2
0.65 - 166.7
quercetin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33000
quercetin
Bacillus subtilis
-
pH 7.0, temperature not specified in the publication
137
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
1H-2-benzyl-3-hydroxy-4-oxoquinolin
pH 6, 25C
0.034
8-hydroxyquinoline
-
-
0.745
alpha-alpha'-dipyridyl
-
-
0.11
alpha-naphthoquinoline
-
-
0.00027
ethylxanthate
-
-
0.115
o-phenanthroline
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-
1.55
Quinoline
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0012
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native enzyme, using quercetin as substrate, at 25C, pH 7.5
0.0276
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recombinant enzyme, using fisetin as substrate, at 25C, pH 7.5
1.5
-
25C, pH 7.5
1.87
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recombinant enzyme, using tamarixetin as substrate, at 25C, pH 7.5
2.27
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recombinant enzyme, using quercetin as substrate, at 25C, pH 7.5
2.49
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recombinant enzyme, using galangin as substrate, at 25C, pH 7.5
4
-
Fe-QueD
28
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Co-QueD
144
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Ni-QueD
additional information
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high specific QueD activity is found in crude cell extracts when the growth medium is supplemented with NiCl2 or CoCl2, but not when Mn2+, Fe2+, Cu2+, or Zn2+ is added, the activity of the purified QueD proteins depends strongly on the nature of the metal ion cofactor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 6
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Britton-Robinson buffer, composed of H3PO4, acetic acid, H3BO3
5.5 - 6.7
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50 mM MES buffer
6 - 9
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50 mM MES-Tris buffer
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
calculated
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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HeLa cells contain higher content of pirin protein than normal kidney human epithelial or HEK-293 cells
Manually annotated by BRENDA team
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HeLa cells contain higher content of pirin protein than normal kidney human epithelial or HEK-293 cells
Manually annotated by BRENDA team
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HeLa cells contain higher content of pirin protein than normal kidney epithelial or HEK-293 cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23040
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calculated value of the hexahistidine-tagged QueD monomer
40000
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about 40000 Da, SDS-PAGE
45000
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SDS-PAGE
55100
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SDS-PAGE
56000
gel filtration
63000
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gel filtration
65000
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gel permeation chromatography, native Ni-QueD
65100
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gel permeation chromatography, native Co-QueD
110000
111400
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gel filtration
135000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
1 * 55000, SDS-PAGE
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copper-containing quercetin 2,3-dioxygenase, X-ray diffraction structure determination and analysis at 1.6 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
precipitates below
657272
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
storage in buffer, loss of 25% of activity during 48 h, high concentrations of ammonium chloride stabilize, ascorbic acid and cysteine do not
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 6 months, the enzyme retains 81% of its initial activity
4C, stable for several weeks
-
stable at -20C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel column equilibrated with 50 mM Tris.HCl, pH 7.5, and eluted with a NaCl gradient (0-600 mM). Ultrogel ACA 34 column, eluted with 50 mM Tris.HCl, pH 7.5, and 100 mM Nacl. DEAE-Sepharose column equilibrated with 50 mM Tris.HCl, pH 7,5, eluted with a gradient of NaCl (100-500 mM).
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metal chelate affinity chromatography
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partial purification by ammonium sulfate precipitation and DEAE Toyopearl column chromatography
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recombinant QueD protein with a C-terminal hexahistidine-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus awamori
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expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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expression in Escherichia coli BL21(DE3) (pLysS, pET23a-queD) as a His6-tagged protein
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expression of Fe-QDO in Escherichia coli
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overexpression in Escherichia coli or in in Streptomyces lividans TK23
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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optimization of enzyme production by variation of rutin concentration, nitrogen source and concentration, salt and metal salt concentration, yeast extract concentration and pH value. six-fold improvement of enzyme activity reaching a maximum activity of 0.000708 mM per min and ml of culture supernatant
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