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
1.13.11.24
-
RECOMMENDED NAME
GeneOntology No.
quercetin 2,3-dioxygenase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
rutin degradation
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
flavonol 2,4-dioxygenase
-
-
-
flavonol 2,4-oxygenase
-
-
-
-
manganese quercetin dioxygenase
-
-
pirin
-
-
QdoI
Bacillus subtilis 168
-
-
-
QueD
A2VA43
;
-
quercetin dioxygenase
-
-
quercetinase
-
-
-
-
quercetinase
-
-
quercetinase
Aspergillus flavus MTCC-1783, Aspergillus flavus MTCC-1883, Aspergillus flavus MTCC-1884, Aspergillus flavus MTCC-2206, Aspergillus flavus MTCC-2456
-
-
-
quercetinase
-
-
quercetinase
-
-
quercetinase
A7Y9J1
-
quercetinase
-
-
quercetinase
-
;
-
type III extradiol dioxygenase
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9075-67-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
PRL 1805
-
-
Manually annotated by BRENDA team
strain MTCC-1783; strain MTCC-1883; strain MTCC-1884; strain MTCC-2206; strain MTCC-2456
-
-
Manually annotated by BRENDA team
Aspergillus flavus MTCC-1783
strain MTCC-1783
-
-
Manually annotated by BRENDA team
Aspergillus flavus MTCC-1883
strain MTCC-1883
-
-
Manually annotated by BRENDA team
Aspergillus flavus MTCC-1884
strain MTCC-1884
-
-
Manually annotated by BRENDA team
Aspergillus flavus MTCC-2206
strain MTCC-2206
-
-
Manually annotated by BRENDA team
Aspergillus flavus MTCC-2456
strain MTCC-2456
-
-
Manually annotated by BRENDA team
Aspergillus flavus PRL 1805
PRL 1805
-
-
Manually annotated by BRENDA team
IFO-4408, grown on quercetin
-
-
Manually annotated by BRENDA team
DSM 821, grown on rutin
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
-
-
-
Manually annotated by BRENDA team
medium improvement for production of enzyme
-
-
Manually annotated by BRENDA team
strain FLA
SwissProt
Manually annotated by BRENDA team
strain FLA, DSM 41951
-
-
Manually annotated by BRENDA team
strain FLA
SwissProt
Manually annotated by BRENDA team
strain FLA, DSM 41951
-
-
Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
a non-heme redox metalloenzyme
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.004
-
1H-2-benzyl-3-hydroxy-4-oxoquinolin
A7Y9J1, -
pH 6, 25C
0.034
-
8-hydroxyquinoline
-
-
0.745
-
alpha-alpha'-dipyridyl
-
-
0.11
-
alpha-naphthoquinoline
-
-
0.00027
-
ethylxanthate
-
-
0.115
-
o-phenanthroline
-
-
1.55
-
Quinoline
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
A7Y9J1, -
quercetin oxidation
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Aspergillus flavus MTCC-1783, Aspergillus flavus MTCC-1883, Aspergillus flavus MTCC-1884, Aspergillus flavus MTCC-2206, Aspergillus flavus MTCC-2456, Aspergillus flavus PRL 1805
-
-
-
-
Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
containing 27.5% carbohydrate
glycoprotein
-
-
glycoprotein
Aspergillus flavus PRL 1805
-
containing 27.5% carbohydrate
-
glycoprotein
-
-
glycoprotein
-
N-linked oligo-mannose type glycan chains, 46-54% carbohydrate
glycoprotein
A7Y9J1, -
the purified enzyme is a mixture of at least four glycoforms
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for several weeks
-
stable at -20C
-
4C, 6 months, the enzyme retains 81% of its initial activity
A7Y9J1, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E76A
-
site-directed mutagenesis of Ni-QueD, exhibits marginal quercetinase activity of 0.014 unit/mg, corresponding to a more than 10000fold decrease in specific activity, Glu76 of QueD is part of the strictly conserved cupin motif and thus is assumed to be a ligand to the metal center
E76A
-
site-directed mutagenesis of Ni-QueD, exhibits marginal quercetinase activity of 0.014 unit/mg, corresponding to a more than 10000fold decrease in specific activity, Glu76 of QueD is part of the strictly conserved cupin motif and thus is assumed to be a ligand to the metal center
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
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