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Information on EC 1.14.13.9 - kynurenine 3-monooxygenase and Organism(s) Aedes aegypti and UniProt Accession Q86PM2

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IUBMB Comments
A flavoprotein (FAD).
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This record set is specific for:
Aedes aegypti
UNIPROT: Q86PM2
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The taxonomic range for the selected organisms is: Aedes aegypti
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cinnabar, kmo, kynurenine 3-monooxygenase, kynurenine 3-hydroxylase, kynurenine hydroxylase, kynurenine monooxygenase, kynurenine-3-monooxygenase, pfkmo, nadph-dependent flavin monooxygenase, kyn-ohase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
kynurenine hydroxylase
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kynurenine monooxygenase
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kynurenine 3-hydroxylase
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kynurenine hydroxylase
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-
-
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L-kynurenine-3-hydroxylase
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-
-
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oxygenase, kynurenine 3-mono-
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-
-
-
additional information
the enzyme is a member of the glutathione reductase structural family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9029-61-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-kynurenine + NADH + H+ + O2
3-hydroxy-L-kynurenine + NAD+ + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
show the reaction diagram
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
consensus domain sequence, probably FAD-containing
NADH
low activity, ineffective cofactor
NADPH
highly preferred cofactor with respect to NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chloride
mixed-type inhibition
pyridoxal 5'-phosphate
noncompetitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.89
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
5.17
NADH
recombinant enzyme, pH 7.5, 37°C
0.82
NADPH
recombinant enzyme, pH 7.5, 37°C
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.88
L-kynurenine
recombinant enzyme, pH 7.5, 37°C
0.85
NADH
recombinant enzyme, pH 7.5, 37°C
2.03
NADPH
recombinant enzyme, pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.2 - 24.5
chloride
0.17 - 0.27
pyridoxal 5'-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
yellow fever mosquito, black-eyed Liverpool strain
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme is hydrophobis and contains 2 transmembrane segments
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KMO_AEDAE
476
3
54232
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene kh, DNA and amino acid sequence analysis of wild-type and mutant genes, expression in Spodoptera frugiperda Sf9 cells as His-tagged, soluble protein via the baculovirus infection system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, Q.; Calvo, E.; Marinotti, O.; Fang, J.; Rizzi, M.; James, A.A.; Li, J.
Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti
Insect Mol. Biol.
12
483-490
2003
Aedes aegypti (Q86PM2), Aedes aegypti, Aedes aegypti Liverpool (Q86PM2)
Manually annotated by BRENDA team