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Information on EC 1.14.13.9 - kynurenine 3-monooxygenase
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1.14.13.9 kynurenine 3-monooxygenaseIUBMB Comments
A flavoprotein (FAD).
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Word Map
- 1.14.13.9
- mercury
- hg
-
kynurenic
- 3-hydroxykynurenine
-
quinolinic
- kynureninase
-
2,3-dioxygenase
- indoleamine
-
cronbach
-
3-hydroxyanthranilic
- huntington
-
paint
-
bartlett
-
realgar
-
ochre
-
quin
- methylmercury
-
xanthurenic
-
calcite
-
geochemical
-
ommochrome
-
artwork
-
mineralogical
-
excitotoxins
-
vermilion
-
slovenia
-
archaeological
-
micro-raman
-
roman
- medicine
- pharmacology
- analysis
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
cinnabar, kmo, kynurenine 3-monooxygenase, kynurenine 3-hydroxylase, kynurenine hydroxylase, kynurenine monooxygenase, kyn-ohase, l-kynurenine 3-monooxygenase, l-kynurenine-3-hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bna4
cinnabar
KMO
kynurenine 3-hydroxylase
kynurenine hydroxylase
kynurenine monooxygenase
L-kynurenine,NADPH2:oxygen oxidoreductase (3-hydroxylating)
additional information
additional information
the enzyme is a member of the glutathione reductase structural family
additional information
the enzyme is a member of the glutathione reductase structural family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9029-61-2
-
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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
5-bromo-L-kynurenine + NADPH + H+ + O2
5-bromo-3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
5-chloro-L-kynurenine + NADPH + H+ + O2
5-chloro-3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the enzyme is involved in the kynurenine pathway of tryptophan metabolsim, overview
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme activity depends on the reduction state of the enzyme
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme activity depends on the reduction state of the enzyme
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
?
L-kynurenine + NADH + H+ + O2
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
?
L-kynurenine + NADH + H+ + O2
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is involved in tryptophan catabolism
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
prolonged kynurenine 3-hydroxylase inhibition reduces development of levodopa-induced dyskinesias in Parkinsonian monkeys, enzyme regulation and involvement in Parkinson's disease, overview
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is not involved in regulation of 3-hydroxy-L-kynurenine level in vivo
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
function of the enzyme may change from a role in immunosuppression at the maternal-fetal interface in early pregnancy to one associated with regulation of fetoplacental blood flow or placental metabolism in late gestation
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
binding of L-kynurenine to the oxidized enzyme is relatively slow and involves at least two reversible steps
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
r
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
no reaction with D-isomer
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
no reaction with D-isomer
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
NADH is less effective
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in injured brain regions following cerebral ischemia
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in the spinal cord with experimental allergic encephalopathy
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
key enzyme in the kynurenine pathway of tryptophan degradation
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
rate limiting step in the pyridine nucleotide biosynthesis from tryptophan
-
?
o-hydroxybenzoyl-DL-alanine + NADPH + O2
? + NADP+
-
about 25% of the activity with L-kynurenine
-
?
o-hydroxybenzoyl-DL-alanine + NADPH + O2
? + NADP+
-
about 25% of the activity with L-kynurenine
-
?
additional information
?
-
enzyme is involved in eye pigmentation
-
?
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease by aggregation in nuclear and cytoplasmic inclusion bodies
-
?
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, newborn mice delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
?
additional information
?
-
-
catalyzes NADH- and NADPH-linked reductions of low molecular weight acceptors such as 2,6-dichlorophenolindophenol and ferricyanide
-
?
additional information
?
-
-
age affects the enzyme activities of tryptophan metabolism along the kynurenine pathway, one of the various tryptophan metabolic routes, kynurenine 3-monooxygenase activity progressively decreases with age in liver and kidney of newborn to mature rats, quantitative overview
-
?
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, rat pups delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
?
additional information
?
-
-
the enzyme is responsible for driving formation of neurotoxic and neuroprotective kynurenine metabolites, regulation mechanism, overview
-
?
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease in humans by aggregation in nuclear and cytoplasmic inclusion bodies
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the enzyme is involved in the kynurenine pathway of tryptophan metabolsim, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is involved in tryptophan catabolism
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
prolonged kynurenine 3-hydroxylase inhibition reduces development of levodopa-induced dyskinesias in Parkinsonian monkeys, enzyme regulation and involvement in Parkinson's disease, overview
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is not involved in regulation of 3-hydroxy-L-kynurenine level in vivo
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
function of the enzyme may change from a role in immunosuppression at the maternal-fetal interface in early pregnancy to one associated with regulation of fetoplacental blood flow or placental metabolism in late gestation
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in injured brain regions following cerebral ischemia
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in the spinal cord with experimental allergic encephalopathy
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
key enzyme in the kynurenine pathway of tryptophan degradation
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
rate limiting step in the pyridine nucleotide biosynthesis from tryptophan
-
-
?
additional information
?
-
enzyme is involved in eye pigmentation
-
-
?
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease by aggregation in nuclear and cytoplasmic inclusion bodies
-
-
?
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, newborn mice delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
-
?
additional information
?
-
-
age affects the enzyme activities of tryptophan metabolism along the kynurenine pathway, one of the various tryptophan metabolic routes, kynurenine 3-monooxygenase activity progressively decreases with age in liver and kidney of newborn to mature rats, quantitative overview
-
-
?
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, rat pups delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
-
?
additional information
?
-
-
the enzyme is responsible for driving formation of neurotoxic and neuroprotective kynurenine metabolites, regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease in humans by aggregation in nuclear and cytoplasmic inclusion bodies
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
dependent on, the Gly-X-Gly-X-X-Gly motif, residues 27-32, and the hydrophobic amino acid residues at positions 23, 25, 36, 39, 46, and 48 are indispensable for correct folding of the beta1-alpha-beta2-structure of the dinucleotide binding domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S,2S)-2-(3,4-dichlorobenzoyl)-cyclopropane-1-carboxylic acid
-
KMO inhibitor UPF 648, totally blocks KMO at 0.1 and 0.01 mM and is still highly active at 0.001 mM (81% inhibition). It reduces 3-hydroxykynurenine synthesis by 64% without affecting kynurenic acid formation. In neuron-depleted striata, UPF 648 decreases both 3-hydroxykynurenine and quinolinic acid production by 77% and 66%, respectively and also raises kynurenic acid synthesis by 27%. 0.1 mM UPF 648 blocks KMO in both lesioned and contralateral striatum, but does not interfere with KAT activity in either tissue
(R)-3-(5-chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
-
(R,S)-2-amino-oxo-4-(3',4'-dichlorophenyl)butanoic acid
-
FCE 28833, 50% inhibition at 0.2 microM, blocks not only the cerebral but also the peripheral enzyme
(S)-3-(5-Chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
-
(S)-9-(4-aminopiperazine-1-yl)-8-fluoro-3-methyl-6-oxo-2,3,5,6-tetrahydro-4H-1-oxa-3a-azaphenalene-5-carboxylic acid
-
does not affect KMO activity significantly, 1 mM inhibits by 17%
3-(5,6-dichloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
-
3-(5-chloro-6-cyclopropoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
3-(5-chloro-6-ethoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
3-(5-chloro-6-ethyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
3-(5-chloro-6-methoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
-
3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
3-[2-methylidene-5-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-(propan-2-yl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-(pyridin-2-ylmethoxy)-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridazin-3-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzothiazol-3-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-[(1R)-1-(pyrimidin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-2-oxo-6-[(propan-2-yl)oxy]-1,3-benzoxazol-3(2H)-yl]propanoic acid
-
3-[5-chloro-2-oxo-6-[1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-2-oxo-6-[2-(pyrrolidin-1-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-6-(2-methoxyethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-(2-methylpropyl)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-(cyclobutylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-(cyclopropylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-6-(cyclopropyloxy)-2-oxo-1,3-benzoxazol-3(2H)-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(1,3-oxazol-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(4-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
-
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(6-methylpyridazin-3-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(6-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[5-chloro-6-[(1R)-1-(pyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
3-[6-(benzyloxy)-5-chloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
3-[6-chloro-3-oxo-7-[(1R)-1-(pyridin-2-yl)ethoxy]-3,4-dihydro-2H-1,4-benzoxazin-4-yl]propanoic acid
-
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indazol-1-yl]propanoic acid
-
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indol-1-yl]-propanoic acid
-
4-amino-N-[4-[2-fluoro-5-(trifluoromethyl)phenyl]thiazol-2-yl]benzenesulfonamide
-
50% inhibition at 19nM
7-chloro-3-methyl-1H-pyrrolo[3,2-c]quinoline-4-carboxylic acid
-
relatively potent and selective inhibitor
benzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
Cl-
-
70% inhibition with 0.1 M NaCl or KCl, competitive with respect to NADPH and non-competitive with respect to L-kynurenine
m-nitrobenzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
(m-nitrobenzoyl)-alanine
-
mNBA, leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
(m-nitrobenzoyl)-alanine
-
mNBA, leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
(m-nitrobenzoyl)-alanine
-
various pyrrolo[3,2-c]quinoline derivates cause enzyme inhibition
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
Ro-61-8048, 50% inhibition at 37 nM
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
inhibition after oral or intraperitoneal administration
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
i.e. Ro 61-8048, high-affinity low molecular inhibitor
Ro 61-8048
noncompetitive. Theinhibitor is bound in the tunnel at the interface where the N- and C-terminal domains associate
UPF 648
UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine
additional information
kynurenines substituted with a halogen at the 5-position are excellent substrates, with values of kcat and kcat/Km comparable to or higher than kynurenine. Kynurenines substituted in the 3-position are competitive inhibitors, with KI values lower than the Km for kynurenine. Bromination also enhances inhibition. A pharmacophore model of kynurenine monooxygenase is developed, and predicted that 3,4-dichlorohippuric acid would be an inhibitor
-
additional information
-
kynurenines substituted with a halogen at the 5-position are excellent substrates, with values of kcat and kcat/Km comparable to or higher than kynurenine. Kynurenines substituted in the 3-position are competitive inhibitors, with KI values lower than the Km for kynurenine. Bromination also enhances inhibition. A pharmacophore model of kynurenine monooxygenase is developed, and predicted that 3,4-dichlorohippuric acid would be an inhibitor
-
additional information
-
inhibition by various 2-amino-4-aryl-4-oxobut-2-enoic acids and esters at 10 micromolar; inhibition by various 4-aryl-2-hyroxy-4-oxobut-2-enoic acids and esters at 10 micromolar
-
additional information
the molecular mechanism of action of three classes of inhibitors with differentiated binding modes and kinetics is reported. Two inhibitor classes trap the catalytic flavin in a tilting conformation. This correlates with picomolar affinities, increased residence times and an absence of the peroxide production
-
additional information
-
the specific enzyme activity is not affected by cloricromene in vitro and in vivo in liver and kidney
-
additional information
-
targeted inhibition of KMO is a viable strategy for achieving local elevation of kynurenate concentrations
-
additional information
development and optimization of a series of inhibitors
-
additional information
the molecular mechanism of action of three classes of inhibitors with differentiated binding modes and kinetics is reported. Two inhibitor classes trap the catalytic flavin in a tilting conformation. This correlates with picomolar affinities, increased residence times and an absence of the peroxide production
-
additional information
-
inhibition by N-(4-phenylthiazol-2-yl)benzenesulfonamides with various modifications
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
a systemic inflammatory challenge stimulates KMO expression in brain, increased enzyme expression is observed in rat brain 24 h post lipopolysaccharide treatment, without any change in kynurenine aminotransferase II expression
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
5-bromo-L-kynurenine
pH and temperature not specified in the publication
0.002
5-chloro-L-kynurenine
pH and temperature not specified in the publication
0.067
L-kynurenine
pH and temperature not specified in the publication
0.153
L-kynurenine
pH 7, 37°C, full length 12His-tagged enzyme, FLAG tag removed during affinity purification
0.0087
NADPH
pH 7, 37°C, full length 12His-tagged enzyme, FLAG tag removed during affinity purification
additional information
additional information
-
steady-state kinetics and ligand perturbation of flavin fluorescence, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
5-bromo-L-kynurenine
pH and temperature not specified in the publication
0.8
5-chloro-L-kynurenine
pH and temperature not specified in the publication
2
L-kynurenine
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
133.3
5-bromo-L-kynurenine
pH and temperature not specified in the publication
400
5-chloro-L-kynurenine
pH and temperature not specified in the publication
29.9
L-kynurenine
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000095
(R,S)-2-amino-oxo-4-(3'-4'-dichlorophenyl)butanoic acid
-
competitive inhibitor
0.034
3,4-dichlorohippuric acid
pH and temperature not specified in the publication
0.0000048
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
competitive inhibitor
1
3,4-dimethoxyhippuric acid
pH and temperature not specified in the publication
0.0015
3,5-dibromo-L-kynurenine
pH and temperature not specified in the publication
0.0138
3-chloro-DL-kynurenine
pH and temperature not specified in the publication
0.0086
3-methyl-DL-kynurenine
pH and temperature not specified in the publication
0.011
5-bromo-3-chloro-DL-kynurenine
pH and temperature not specified in the publication
0.0102
5-bromo-3-methyl-DL-kynurenine
pH and temperature not specified in the publication
0.0135
Ro 61-8048
pH and temperature not specified in the publication
11.2
chloride
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
0.17
pyridoxal 5'-phosphate
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
0.27
pyridoxal 5'-phosphate
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
(6-chloro-1H-indazol-1-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000025
(R)-3-(5-chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00025
(S)-3-(5-Chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0025
2-amino-3-(6-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0063
3-(1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000063
3-(5,6-dichloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000063
3-(5,6-dichloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000025
3-(5-chloro-1,2-benzoxazol-3-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.001
3-(5-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000013
3-(5-chloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0001
3-(5-chloro-6-cyano-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000032
3-(5-chloro-6-cyclopropoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-(5-chloro-6-ethoxy-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000005
3-(5-chloro-6-ethoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00001
3-(5-chloro-6-ethyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00001
3-(5-chloro-6-ethyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000013
3-(5-chloro-6-methoxy-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000013
3-(5-chloro-6-methoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000013
3-(5-chloro-6-methyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000126
3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000063
3-(5-chloro-7-methyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00063
3-(5-cyano-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.001
3-(5-methoxy-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000398
3-(6-bromo-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0005
3-(6-chloro-1H-benzotriazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0006
3-(6-chloro-1H-indazol-1-yl)-2-hydroxypropanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0025
3-(6-chloro-1H-indazol-1-yl)-2-methylpropanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.005
3-(6-chloro-1H-indazol-1-yl)butanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00005
3-(6-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00013
3-(6-chloro-1H-indol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.002
3-(6-chloro-3-methyl-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000079
3-(6-chloro-3-oxo-3,4-dihydro-2H-1-benzopyran-4-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0032
3-(6-methyl-1H-indazol-1-yl)propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.005
3-[2-methylidene-5-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0001
3-[5-chloro-2-oxo-6-(propan-2-yl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-2-oxo-6-(pyridin-2-ylmethoxy)-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000398
3-[5-chloro-2-oxo-6-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000013
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridazin-3-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000002
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzothiazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-[5-chloro-2-oxo-6-[(1R)-1-(pyrimidin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000079
3-[5-chloro-2-oxo-6-[(propan-2-yl)oxy]-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-2-oxo-6-[1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000794
3-[5-chloro-2-oxo-6-[2-(pyrrolidin-1-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000032
3-[5-chloro-6-(2-methoxyethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000013
3-[5-chloro-6-(2-methylpropyl)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000025
3-[5-chloro-6-(cyclobutylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00001
3-[5-chloro-6-(cyclopropylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-(cyclopropyloxy)-2-oxo-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-[(1R)-1-(1,3-oxazol-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00000398
3-[5-chloro-6-[(1R)-1-(4-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00000316
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000025
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00000316
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000002
3-[5-chloro-6-[(1R)-1-(6-methylpyridazin-3-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-[5-chloro-6-[(1R)-1-(6-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-[5-chloro-6-[(1R)-1-(pyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000025
3-[6-(benzyloxy)-5-chloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-[6-chloro-3-oxo-7-[(1R)-1-(pyridin-2-yl)ethoxy]-3,4-dihydro-2H-1,4-benzoxazin-4-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.00000316
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indazol-1-yl]propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.000005
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indol-1-yl]-propanoic acid
Pseudomonas fluorescens
pH and temperature not specified in the publication
0.003
4-(6-chloro-1H-indazol-1-yl)butanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000007
GSK366
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.00006
GSK428
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.000003
GSK775
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.0000043
GSK891
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
0.0025
additional information
additional information
-
specific activity in organs of rats with experimental allergic encephalopathy
additional information
-
specific activities of apoenzyme and holoenzyme with different electron acceptors
additional information
-
enzyme activity with different cofactors and under anaerobic conditions
additional information
-
enzyme activity at different temperatures in different strains
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
yellow fever mosquito, black-eyed Liverpool strain
SwissProt
brenda
male, 4-month-old diabetic/hyperlipidemic New Zealand White rabbits
-
-
brenda
-
348514, 348516, 348517, 348518, 348521, 348525, 348527, 348529, 348530, 348531, 348534, 348536, 657495, 675556, 705250
-
-
brenda
mutant E105 has an enzymatic defect of kynurenine 3-hydroxylase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in first and second trimester of the placenta, within the fetal villus
brenda
-
especially in stromal and glandular epithelium in the first trimester decidua
brenda
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
brenda
additional information
-
-
brenda
additional information
constitutive expression of the enzyme in all developmental stages from egg via larva and pupa to adult mosquito
brenda
additional information
-
constitutive expression of the enzyme in all developmental stages from egg via larva and pupa to adult mosquito
brenda
additional information
-
enzyme expression analysis in untreated and in brain after induction of inflammation, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme is hydrophobis and contains 2 transmembrane segments
brenda
-
enzyme is hydrophobis and contains 2 transmembrane segments
brenda
the C terminus of the enzyme contains a putative outer mitochondrial membrane-targeting sequence and this portion of the molecule is required enzyme function
brenda
the C terminus of the enzyme contains a putative outer mitochondrial membrane-targeting sequence and this portion of the molecule is required enzyme function
brenda
the C-terminal region functions as a mitochondrial targeting signal
brenda
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
additional information
drug target
contents of L-tryptophan and monoamines and their metabolites are measured in the serum and hippocampus of kynurenine 3-monooxygenase KO mice. It is investigated whether antidepressants improve the depressive-like behaviors in kynurenine 3-monooxygenase KO mice. KO mice show antidepressants-responsive depressive-like behaviors and monoaminergic dysfunctions via abnormality of kynurenine metabolism with good validities as model for major depressive disorder
drug target
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington’s and Alzheimer’s. It is a target for acute pancreatitis multiple organ dysfunction syndrome
drug target
kynurenine represents a branch point of the kynurenine pathway, being converted into the neurotoxin 3-hydroxykynurenine via kynurenine monooxygenase, neuroprotectant kynurenic acid, and anthranilic acid. As a result of this branch point, kynurenine monooxygenase is an attractive drug target for several neurodegenerative and/or neuroinflammatory diseases, especially Huntington's, Alzheimer's, and Parkinson's diseases
drug target
the enzyme is a clinical candidate for the treatment of acute pancreatitis
drug target
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
drug target
the enzyme is a potential therapeutic target for neurodegenerative and neurologic disorders
drug target
the enzyme is a therapeutic target in several disease states, including Huntington's disease
malfunction
adaptive—and possibly regulatory-changes in mice with a targeted deletion of kynurenine 3-monooxygenase (Kmo-/-) are investigated kynurenine 3-monooxygenase-deficient mice are characterized using six behavioral assays relevant for the study of schizophrenia. Elimination of kynurenine 3-monooxygenase in mice is associated with multiple gene and functional alterations that appear to duplicate aspects of the psychopathology of several neuropsychiatric disorder
malfunction
contents of L-tryptophan and monoamines and their metabolites are measured in the serum and hippocampus of kynurenine 3-monooxygenase KO mice. It is investigated whether antidepressants improve the depressive-like behaviors in kynurenine 3-monooxygenase KO mice. A deficiency in kynurenine 3-monooxygenase appears to be implicated in antidepressant-responsive depression-like behaviors. In the kynurenine 3-monooxygenase KO mice, there are abnormal kynurenine pathway metabolites and monoamines. The abnormal monoamines in addition to the abnormal kynurenine pathway metabolites may play an important role in the pathophysiology of major depressive disorder
malfunction
human polymorphism in the C-terminal region of the enzyme results in an Arg452Cys mutation, statistically linked to bipolar disorder and schizophrenia
malfunction
the white egg 1 (w-1) mutant, which is characterized by white eyes and white eggs, is deficient in Bombyx kynurenine 3-monooxygenase activity. To investigate whether the w-1 mutant phenotype is rescued by introducing the wild-type kynurenine 3-monooxygenase gene, transgenic silkworms with the wild-type Bombyx kynurenine 3-monooxygenase gene under the control of either the cytoplasmic actin gene promoter or the native kynurenine 3-monooxygenase gene promoter are constructed. The results indicate that the wild-type kynurenine 3-monooxygenase gene can be used as a marker gene for visually screening transgenic silkworms
metabolism
enzyme of the kynurenine pathway, which is the major catabolic route of tryptophan
metabolism
the enzyme is central to the kynurenine pathway of tryptophan metabolism
metabolism
the enzyme is involved in kynurenine pathway. It catalyzes the decisive step in production of metabolites as quinolinic acid
metabolism
the enzyme is very important in kynurenine pathway because it catalyzes the decisive step in production of metabolites as quinolinic acid
physiological function
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
physiological function
the white egg 1 mutant, which is characterized by white eyes and white eggs, is deficient in Bombyx kynurenine 3-monooxygenase activity.Expression of the wild-type gene under control of either the cytoplasmic actin gene promoter (A3KMO) or the native KMO gene promoter (KKMO) leads to adults with brown eyes, and the eggs laid by the transgenic females are also brown. The A3KMO silkworm lines express the transcript in the mid-gut, fat bodies, and Malpighian tubules. The KKMO line expresses the transcript only in the fat bodies and Malpighian tubules. The intensity of eye and egg color in the transgenic lines is proportional to the KMO expression level
physiological function
adaptive-and possibly regulatory-changes in mice with a targeted deletion of kynurenine 3-monooxygenase (Kmo-/-) are investigated kynurenine 3-monooxygenase-deficient mice are characterized using six behavioral assays relevant for the study of schizophrenia. Elimination of kynurenine 3-monooxygenase in mice is associated with multiple gene and functional alterations that appear to duplicate aspects of the psychopathology of several neuropsychiatric disorder
additional information
the C-terminal region of pig liver KMO plays a dual role. First, it is required for the enzymatic activity. Second, it functions as a mitochondrial targeting signal
additional information
-
the C-terminal region of pig liver KMO plays a dual role. First, it is required for the enzymatic activity. Second, it functions as a mitochondrial targeting signal
Show AA Sequence and Transmembrane Helices (3580 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
55760
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
?
-
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
additional information
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal
additional information
-
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained by hanging-drop vapor diffusion at 20°C. Crystal structures of the complex of the full-length enzyme with the substrate L-kynurenine and in complex with L-kynurenine and Ro 61-8048 at a resolution of 1.85 and 2.34 A, respectively. The crystals of the enzyme-L-kynurenine complex belong to the space group P2(1) with 1 enzyme molecule in the asymmetric unit. The crystal structure of the enzyme–L-kynurenine-Ro61-8048 complex belongs to the space group P2(1)2(1)2(1) with 1 pfKMO molecule in the asymmetric unit. The crystal structure of the SeMet enzyme derivative belongs to the space group P2(1) with 2 enzyme molecules in the asymmetric unit
crystal structure, in the free form and in complex with the tight-binding inhibitor UPF 648. UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E366Q
2% of the enzyme activity compared with that of the wild-type enzyme
M367A
2% of the enzyme activity compared with that of the wild-type enzyme
M367L
13% of the enzyme activity compared with that of the wild-type enzyme
N363A
28% of the enzyme activity compared with that of the wild-type enzyme
N465A
about 80% of the enzyme activity compared with that of the wild-type enzyme
R85K
1% of the enzyme activity compared with that of the wild-type enzyme
Y398A
1% of the enzyme activity compared with that of the wild-type enzyme
Y398F
1% of the enzyme activity compared with that of the wild-type enzyme
Y99F
7% of the enzyme activity compared with that of the wild-type enzyme
E372A
about 15% of the enzyme activity compared with that of the wild-type enzyme
E372Q
about 5% of the enzyme activity compared with that of the wild-type enzyme
M373L
about 60% of the enzyme activity compared with that of the wild-type enzyme
N369A
about 65% of the enzyme activity compared with that of the wild-type enzyme
Q424A
mutation does not greatly affect enzyme activity. Ro 61-8048 shows no inhibition to the pfKMO mutant enzyme
Y404F
about 40% of the enzyme activity compared with that of the wild-type enzyme
Y98F
about 1% of the enzyme activity compared with that of the wild-type enzyme
additional information
additional information
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
additional information
-
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
additional information
-
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
additional information
-
enzyme deficiency leads to the white eyes and white eggs w-1 phenotype in mutant silkworms, it can be partially rescued by expression of wild-type enzyme under control of either the cytoplasmic actin gene promoter, A3KMO, or the native KMO gene promoter, KKMO, phenotypes, overview
additional information
enzyme deficiency leads to the white eyes and white eggs w-1 phenotype in mutant silkworms, it can be partially rescued by expression of wild-type enzyme under control of either the cytoplasmic actin gene promoter, A3KMO, or the native KMO gene promoter, KKMO, phenotypes, overview
additional information
-
enzyme deficiency leads to the white eyes and white eggs w-1 phenotype in mutant silkworms, it can be partially rescued by expression of wild-type enzyme under control of either the cytoplasmic actin gene promoter, A3KMO, or the native KMO gene promoter, KKMO, phenotypes, overview
additional information
the enzyme is systematically truncated according to the sequence alignments and the predicted secondary structures. For the truncations 1-377, 1-379, and 1-394, which have 1 or 2 more predicted alpha-helices than that of the 1-372/374, no or weak protein expression is detected. Although for the truncation 1-430 that has the C-terminal hydrophobic tail removed, no enzymatic activities can be detected but the protein expression is normal. The results indicate that the C-terminal portion is important for both the folding and the enzymatic activity
additional information
-
the enzyme is systematically truncated according to the sequence alignments and the predicted secondary structures. For the truncations 1-377, 1-379, and 1-394, which have 1 or 2 more predicted alpha-helices than that of the 1-372/374, no or weak protein expression is detected. Although for the truncation 1-430 that has the C-terminal hydrophobic tail removed, no enzymatic activities can be detected but the protein expression is normal. The results indicate that the C-terminal portion is important for both the folding and the enzymatic activity
additional information
construction of C-terminal truncation mutants KMODELTAC10, KMODELTAC20, KMODELTAC30, KMODELTAC50, and KMODELTAC70, that are all localized in the cytosol after recombinant expression in COS-7 cells, exept for KMODELTAC10. Two forms of C-terminal truncation, KMODELTAC10D and KMODELTAC20D retain almost full activity but KMODELTAC30D shows 1.6fold higher activity than the wild-type. The activities of KMODELTAC50 and KMODELTAC70 is highly reduced, overview. The quantity of expressed KMODELTA30D in COS-7 cellsis 1.3fold higher than the wild-type KMO
additional information
-
construction of C-terminal truncation mutants KMODELTAC10, KMODELTAC20, KMODELTAC30, KMODELTAC50, and KMODELTAC70, that are all localized in the cytosol after recombinant expression in COS-7 cells, exept for KMODELTAC10. Two forms of C-terminal truncation, KMODELTAC10D and KMODELTAC20D retain almost full activity but KMODELTAC30D shows 1.6fold higher activity than the wild-type. The activities of KMODELTAC50 and KMODELTAC70 is highly reduced, overview. The quantity of expressed KMODELTA30D in COS-7 cellsis 1.3fold higher than the wild-type KMO
additional information
construction of mutants lacking functional enzyme via RNA interference, RNAi, the gene is unlinked to known eye-color mutants
additional information
-
construction of mutants lacking functional enzyme via RNA interference, RNAi, the gene is unlinked to known eye-color mutants
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
disulfide reductants like dithiothreitol or 2-mercaptoethanol stabilize the enzyme
-
enzyme is protected against inactivation in the solubilized state by the presence of DTT, Triton X-100, and FAD in 0.1 M Tris-acetate buffer at pH 8.1
-
purified recombinant enzyme is highly unstable, activity decreases directly after purification also at -80°C
solubilized enzyme is appreciably stabilized in 0.05 M Tris-acetate buffer, pH 8.1, 1 mM DTT, 0.2 M mannitol, 0.2% Triton X-100, 0.005 mM FAD
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
recombinant enzyme 8.8fold from Escherichia coli strain by ammonium sulfate fractionation and ion exchange chromatography to homogeneity
-
recombinant enzyme from Sf9 insect cells by solubilization with Triton X-100 and affinity chromatography
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AsK3H, DNA and amino acid sequence determination and analysis, functional expression in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, membrane associated
DNA and amino acid sequence determnination and analysis, sequence comparisons, expression of FLAG-tagged wild-type enzyme and of C-terminal truncation mutants in COS-7 cells. The FLAG tag directs the wild-type enzyme to mitochondria but also to the cytosol and the plasma mambrane, overview
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
gene Tccn, homology-based cloning, DNA and amino acid sequence determination and analysis, gene structure analysis, the Tccn gene is located on linkage group 2
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
comprehensive panel of biochemical and cell-based assays that use liquid chromatography/tandem mass spectrometry to quantify unlabeled kynurenine and 3-hydroxykynurenine and application to measure kynurenine monooxygenase inhibition in cell and tissue extracts, as well as cellular assays
medicine
molecular biology
pharmacology
medicine
-
the enzyme is an attractive target for the treatment of ischemic stroke
medicine
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
medicine
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington's and Alzheimer's. It is a target for acute pancreatitis multiple organ dysfunction syndrome
medicine
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington's and Alzheimer's. It is a target for acute pancreatitis multiple organ dysfunction syndrome (AP-MODS)
medicine
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
medicine
the enzyme is a potential therapeutic target for neurodegenerative and neurologic disorders
medicine
-
the enzyme is an attractive target for the treatment of ischemic stroke
molecular biology
development of a transformant selection system for Tribolium castaneum on the basis of mutant rescue
molecular biology
wild-type KMO gene can be used as a marker gene for visually screening transgenic silkworms
molecular biology
the wild-type enzyme gene can be used as a marker gene for visually screening transgenic silkworms
molecular biology
-
wild-type KMO gene can be used as a marker gene for visually screening transgenic silkworms
pharmacology
kynurenine represents a branch point of the kynurenine pathway, being converted into the neurotoxin 3-hydroxykynurenine via kynurenine monooxygenase, neuroprotectant kynurenic acid, and anthranilic acid. As a result of this branch point, kynurenine monooxygenase is an attractive drug target for several neurodegenerative and/or neuroinflammatory diseases, especially Huntington's, Alzheimer's, and Parkinson's diseases
pharmacology
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okamoto, H.; Hayaishi, O.
Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria
Biochem. Biophys. Res. Commun.
29
394-399
1967
Rattus norvegicus
brenda
Saito, Y.; Hayaishi, O.; Rothenberg, S.
Studies on oxygenases: Enzymatic formation of 3-hydroxy-L-kynurenine from L-kynurenine
J. Biol. Chem.
229
921-934
1957
Rattus norvegicus, Rattus norvegicus Osborne-Mendel
brenda
Nisimoto, Y.; Takeuchi, F.; Shibata, Y.
Molecular properties of L-kynurenine 3-hydroxylase from rat liver mitochondria
J. Biochem.
81
1413-1425
1977
Rattus norvegicus
brenda
Nisimoto, Y.; Takeuchi, F.; Shibata, Y.
Isolation of L-kynurenine 3-hydroxylase from the mitochondrial outer membrane of rat liver
J. Biochem.
78
573-581
1975
Rattus norvegicus
brenda
Nishimoto, Y.; Takeuchi, F.; Shibata, Y.
Purification of L-kynurenine 3-hydroxylase by affinity chromatography
J. Chromatogr.
169
357-364
1979
Rattus norvegicus
brenda
McLean-Bowen, C.A.; Parks, L.W.
Corresponding changes in kynurenine hydroxylase activity, membrane fluidity, and sterol composition in Saccharomyces cerevisiae mitochondria
J. Bacteriol.
145
1325-1333
1981
Saccharomyces cerevisiae
brenda
Schott, H.H.; Staudinger, H.
The regulatory function of L-kynurenine 3-hydroxylase (EC 1.14.1.2) for the biosynthesis of pyridine nucleotides in anaerobically and aerobically grown Saccharomyces cerevisiae
Hoppe-Seyler's Z. Physiol. Chem.
352
1654-1658
1971
Saccharomyces cerevisiae
brenda
Saito, K.; Quearry, B.J.; Saito, M.; Nowak, T.S.Jr.; Markey S.P.; Heyes, M.P.
Kynurenine 3-hydroxylase in brain: species activity differences and effect of gerbil cerebral ischemia
Arch. Biochem. Biophys.
307
104-109
1993
Meriones unguiculatus, Homo sapiens, Macaca mulatta, Mus musculus, Rattus norvegicus
brenda
Pinamonti, S.; Chiarelli-Alvisi, G.
Kynurenine-3-hydroxylase of Schistocera gregaria
Insect Biochem.
4
9-16
1974
Schistocerca gregaria
-
brenda
Stratakis, E.
Subcellular localization and properties of kynurenine 3-hydroxylase from eggs of Ephestia kuhniella Z
J. Comp. Physiol.
141
451-456
1981
Ephestia kuehniella
-
brenda
Shin, M.; Sano, K.; Umezawa, C.
Inhibition of L-kynurenine 3-hydroxylase from Saccharomyces carlsbergensis by alpha-keto acid derivatives of branched chain amino acids
J. Nutr. Sci. Vitaminol.
28
191-201
1982
Saccharomyces pastorianus
brenda
Giordani A.; Pevarello P.; Cini, M.; Bormetti, R.; Greco, F.; Toma, S.; Speciale, C.; Varasi, M.
4-phenyl-4-oxo-butanoic acid derivatives inhibitors of kynurenine 3-hydroxylase
Bioorg. Med. Chem. Lett.
8
2907-2012
1998
Rattus norvegicus
brenda
Speciale, C.; Cini, M.; Wu, H.Q.; Salvati, P.; Schwarcz, R.; Molinari, A.; Calabresi, M.; Varasi, M.
Kynurenic acid-enhancing and anti-ischemic effects of the potent kynurenine 3-hydroxylase inhibitor FCE28833 in rodents
Adv. Exp. Med. Biol.
398
221-227
1996
Rattus norvegicus
brenda
Rover, S.; Cesura, A.M.; Huguenin, P.; Kettler, R.; Szente, A.
Synthesis and biochemical evaluation of N-(4-phenylthiazol-2-yl)benzenesulfonamides as high-affinity inhibitors of kynurenine 3-hydroxylase
J. Med. Chem.
40
4378-4385
1997
Rattus norvegicus
brenda
Uemura, T.; Hirai, K.
Purification of L-kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver
Adv. Exp. Med. Biol.
467
619-623
1999
Sus scrofa
brenda
Cozzi, A.; Carpenedo, R.; Moroni, F.
Kynurenine hydroxylase inhibitors reduce ischemic brain damage: studies with (m-nitrobenzoyl)-alanine (mNBA) and 3,4-dimethoxy-[-N-4-(nitrophenyl)thiazol-2yl]-benzenesulfonamide (Ro 61-8048) in models of focal or global brain ischemia
J. Cereb. Blood Flow Metab.
19
771-777
1999
Meriones unguiculatus, Rattus norvegicus
brenda
Heidempergher, F.; Pevarello, P.; Pillan, A.; Pinciroli, V.; Torre, A.D.; Speciale, C.; Marconi, M.; Cini, M.; Toma, S.; Greco, F.; Varasi, M.
Pyrrolo[3,2-c]quinoline derivates: a new class of kynurenine-3-hydroxylase inhibitors
Farmaco
54
152-160
1999
Rattus norvegicus
brenda
Breton, J.; Avanzi, N.; Magagnin, S.; Covini, N.; Magistrelli, G.; Cozzi, L.; Isacchi, A.
Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase
Eur. J. Biochem.
267
1092-1099
2000
Rattus norvegicus
brenda
Chiarugi, A.; Cozzi, A.; Massacesik L.; Moroni, F.
Kynurenine 3-momo-oxygenase activity and neurotoxic kynurenine metabolites increase in the spinal cord of rats with experimental allergic encephalomyelitis
Neuroscience
102
687-695
2001
Rattus norvegicus
brenda
Drysdale, M.J.; Hind, S.L.; Jansen, M.; Reinhard, J.F.Jr
Synthesis and SAR of 4-aryl-2-hydroxy-4-oxobut-2-enoic acids and esters and 2-amino-4-aryl-4-oxobut-2-enoic acids and esters: Potent inhibitors of kynurenine-3-hydroxylase as potential neuroprotective agents
J. Med. Chem.
43
123-127
2000
Homo sapiens
brenda
Urenjak, J.; Obrenowitch, T.P.
Kynurenine 3-hydroxylase inhibition in rats: Effects on extracellular kynurenic acid concentration and N-methyl-D-aspartate-induced depolarisation in the striatum
J. Neurochem.
75
2427-2433
2000
Rattus norvegicus
brenda
Alberati-Giani, D.; Cesuura, A.M.; Broger, C.; Warren, W.D.; Rover, S.; Malherbe, P.
Cloning and functional expression of human kynurenine 3-monooxygenase
FEBS Lett.
410
407-412
1997
Homo sapiens
brenda
Pellicciari, R.; Natalini, B.; Costantino, G.; Mahmoud, M.R.; Mattoli, L.; Sadeghpour, B.M.; Moroni, F.; Chiarugi, A.; Carpenedo, R.
Modulation of the kynurenine pathway in search for new neruoprotective agents. Synthesis and preliminary evaluation of (m-nitrobenzoys)alanine, a potent inhibitor of kynurenine-3-hydroxylase
J. Med. Chem.
37
647-655
1994
Rattus norvegicus
brenda
Allegri, G.; Bertazzo, A.; Biasiolo, M.; Costa, C.V.; Ragazzi, E.
Kynurenine pathway enzymes in different species of animals
Adv. Exp. Med. Biol.
527
455-463
2003
Cavia porcellus, Oryctolagus cuniculus, Mus musculus, Rattus norvegicus
brenda
Lorenzen, M.D.; Brown, S.J.; Denell, R.E.; Beeman, R.W.
Cloning and characterization of the Tribolium castaneum eye-color genes encoding tryptophan oxygenase and kynurenine 3-monooxygenase
Genetics
160
225-234
2002
Drosophila melanogaster (A1Z745), Tribolium castaneum (Q95NP6), Tribolium castaneum
brenda
Hirai, M.; Kiuchi, M.; Wang, J.; Ishii, A.; Matsuoka, H.
cDNA cloning, functional expression and characterization of kynurenine 3-hydroxylase of Anopheles stephensi (Diptera: Culicidae)
Insect Mol. Biol.
11
497-504
2002
Anopheles stephensi (Q8ISJ5), Anopheles stephensi
brenda
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)
brenda
Giorgini, F.; Guidetti, P.; Nguyen, Q.; Bennett, S.C.; Muchowski, P.J.
A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease
Nat. Genet.
37
526-531
2005
Saccharomyces cerevisiae, Homo sapiens
brenda
Ligam, P.; Manuelpillai, U.; Wallace, E.M.; Walker, D.
Localisation of indoleamine 2,3-dioxygenase and kynurenine hydroxylase in the human placenta and decidua: implications for role of the kynurenine pathway in pregnancy
Placenta
26
498-504
2005
Homo sapiens
brenda
Comai, S.; Costa, C.V.; Ragazzi, E.; Bertazzo, A.; Allegri, G.
The effect of age on the enzyme activities of tryptophan metabolism along the kynurenine pathway in rats
Clin. Chim. Acta
360
67-80
2005
Rattus norvegicus
brenda
Ceresoli-Borroni, G.; Guidetti, P.; Amori, L.; Pellicciari, R.; Schwarcz, R.
Perinatal kynurenine 3-hydroxylase inhibition in rodents: pathophysiological implications
J. Neurosci. Res.
85
845-854
2007
Mus musculus, Rattus norvegicus
brenda
Ragazzi, E.; Costa, C.V.; Comai, S.; Bertazzo, A.; Caparrotta, L.; Allegri, G.
Cloricromene effect on the enzyme activities of the tryptophan-nicotinic acid pathway in diabetic/hyperlipidemic rabbits
Life Sci.
78
785-794
2006
Oryctolagus cuniculus
brenda
Crozier, K.R.; Moran, G.R.
Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400
Protein Expr. Purif.
51
324-333
2007
Pseudomonas fluorescens, Pseudomonas fluorescens 17400
brenda
Gregoire, L.; Rassoulpour, A.; Guidetti, P.; Samadi, P.; Bedard, P.J.; Izzo, E.; Schwarcz, R.; Di Paolo, T.
Prolonged kynurenine 3-hydroxylase inhibition reduces development of levodopa-induced dyskinesias in Parkinsonian monkeys
Behav. Brain Res.
186
161-167
2008
Macaca fascicularis
brenda
Quan, G.; Kobayashi, I.; Kojima, K.; Uchino, K.; Kanda, T.; Sezutsu, H.; Shimada, T.; Tamura, T.
Rescue of white egg 1 mutant by introduction of the wild-type Bombyx kynurenine 3-monooxygenase gene
Insect Sci.
14
85-92
2007
Bombyx mori, Bombyx mori (Q95NK3), Bombyx mori C108
-
brenda
Connor, T.J.; Starr, N.; OSullivan, J.B.; Harkin, A.
Induction of indolamine 2,3-dioxygenase and kynurenine 3-monooxygenase in rat brain following a systemic inflammatory challenge: a role for IFN-gamma?
Neurosci. Lett.
441
29-34
2008
Rattus norvegicus
brenda
Crozier-Reabe, K.R.; Phillips, R.S.; Moran, G.R.
Kynurenine 3-monooxygenase from Pseudomonas fluorescens: substrate-like inhibitors both stimulate flavin reduction and stabilize the flavin-peroxo intermediate yet result in the production of hydrogen peroxide
Biochemistry
47
12420-12433
2008
Pseudomonas fluorescens
brenda
Amori, L.; Guidetti, P.; Pellicciari, R.; Kajii, Y.; Schwarcz, R.
On the relationship between the two branches of the kynurenine pathway in the rat brain in vivo
J. Neurochem.
109
316-325
2009
Rattus norvegicus
brenda
Hirai, K.; Kuroyanagi, H.; Tatebayashi, Y.; Hayashi, Y.; Hirabayashi-Takahashi, K.; Saito, K.; Haga, S.; Uemura, T.; Izumi, S.
Dual role of the carboxyl-terminal region of pig liver L-kynurenine 3-monooxygenase: mitochondrial-targeting signal and enzymatic activity
J. Biochem.
148
639-650
2010
Sus scrofa (Q9MZS9), Sus scrofa
brenda
Stephens, G.L.; Wang, Q.; Swerdlow, B.; Bhat, G.; Kolbeck, R.; Fung, M.
Kynurenine 3-monooxygenase mediates inhibition of Th17 differentiation via catabolism of endogenous aryl hydrocarbon receptor ligands
Eur. J. Immunol.
43
1727-1734
2013
Mus musculus
brenda
Winkler, D.; Beconi, M.; Toledo-Sherman, L.M.; Prime, M.; Ebneth, A.; Dominguez, C.; Munoz-Sanjuan, I.
Development of LC/MS/MS, high-throughput enzymatic and cellular assays for the characterization of compounds that inhibit kynurenine monooxygenase (KMO)
J. Biomol. Screen.
18
879-889
2013
Homo sapiens
brenda
Amaral, M.; Levy, C.; Heyes, D.J.; Lafite, P.; Outeiro, T.F.; Giorgini, F.; Leys, D.; Scrutton, N.S.
Structural basis of kynurenine 3-monooxygenase inhibition
Nature
496
382-385
2013
Saccharomyces cerevisiae (P38169), Saccharomyces cerevisiae
brenda
Tashiro, T.; Murakami, Y.; Mouri, A.; Imamura, Y.; Nabeshima, T.; Yamamoto, Y.; Saito, K.
Kynurenine 3-monooxygenase is implicated in antidepressants-responsive depressive-like behaviors and monoaminergic dysfunctions
Behav. Brain Res.
317
279-285
2017
Mus musculus (Q91WN4)
brenda
Erhardt, S.; Pocivavsek, A.; Repici, M.; Liu, X.C.; Imbeault, S.; Maddison, D.C.; Thomas, M.A.R.; Smalley, J.L.; Larsson, M.K.; Muchowski, P.J.; Giorgini, F.; Schwarcz, R.
Adaptive and behavioral changes in kynurenine 3-monooxygenase knockout mice relevance to psychotic disorders
Biol. Psychiatry
82
756-765
2017
Mus musculus (Q91WN4), Mus musculus
brenda
Phillips, R.S.; Anderson, A.D.; Gentry, H.G.; Guener, O.F.; Bowen, J.P.
Substrate and inhibitor specificity of kynurenine monooxygenase from Cytophaga hutchinsonii
Bioorg. Med. Chem. Lett.
27
1705-1708
2017
Cytophaga hutchinsonii (Q11PP7), Cytophaga hutchinsonii
brenda
Liddle, J.; Beaufils, B.; Binnie, M.; Bouillot, A.; Denis, A.A.; Hann, M.M.; Haslam, C.P.; Holmes, D.S.; Hutchinson, J.P.; Kranz, M.; McBride, A.; Mirguet, O.; Mole, D.J.; Mowat, C.G.; Pal, S.; Rowland, P.; Trottet, L.; Uings, I.J.; Walker, A.L.; Webster, S.P.
The discovery of potent and selective kynurenine 3-monooxygenase inhibitors for the treatment of acute pancreatitis
Bioorg. Med. Chem. Lett.
27
2023-2028
2017
Homo sapiens (O15229)
brenda
Smith, J.R.; Jamie, J.F.; Guillemin, G.J.
Kynurenine-3-monooxygenase a review of structure, mechanism, and inhibitors
Drug Discov. Today
21
315-324
2016
Homo sapiens (O15229), Rattus norvegicus (O88867), Pseudomonas fluorescens (Q84HF5), Sus scrofa (Q9MZS9)
brenda
Gao, J.; Yao, L.; Xia, T.; Liao, X.; Zhu, D.; Xiang, Y.
Biochemistry and structural studies of kynurenine 3-monooxygenase reveal allosteric inhibition by Ro 61-8048
FASEB J.
32
2036-2045
2017
Homo sapiens (O15229), Homo sapiens, Pseudomonas fluorescens (Q84HF5), Pseudomonas fluorescens
brenda
Quan, G.; Kobayashi, I.; Kojima, K.; Uchino, K.; Kanda, T.; Sezutsu, H.; Shimada, T.; Tamura, T.
Rescue of white egg 1 mutant by introduction of the wild-type Bombyx kynurenine 3-monooxygenase gene
Insect Sci.
14
85-92
2007
Bombyx mori (Q95NK3)
-
brenda
Walker, A.L.; Ancellin, N.; Beaufils, B.; Bergeal, M.; Binnie, M.; Bouillot, A.; Clapham, D.; Denis, A.; Haslam, C.P.; Holmes, D.S.; Hutchinson, J.P.; Liddle, J.; McBride, A.; Mirguet, O.; Mowat, C.G.; Rowland, P.; Tiberghien, N.; Trottet, L.; Uings, I.; Webster, S.P.; Zheng, X.; Mole, D.J.
Development of a series of kynurenine 3-monooxygenase inhibitors leading to a clinical candidate for the treatment of acute pancreatitis
J. Med. Chem.
60
3383-3404
2017
Pseudomonas fluorescens (Q84HF5)
brenda
Hutchinson, J.P.; Rowland, P.; Taylor, M.R.D.; Christodoulou, E.M.; Haslam, C.; Hobbs, C.I.; Holmes, D.S.; Homes, P.; Liddle, J.; Mole, D.J.; Uings, I.; Walker, A.L.; Webster, S.P.; Mowat, C.G.; Chung, C.W.
Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase
Nat. Commun.
8
15827
2017
Homo sapiens (O15229), Pseudomonas fluorescens (Q84HF5)
brenda
Gonzalez Esquivel, D.; Ramirez-Ortega, D.; Pineda, B.; Castro, N.; Rios, C.; Perez de la Cruz, V.
Kynurenine pathway metabolites and enzymes involved in redox reactions
Neuropharmacology
112
331-345
2017
Homo sapiens (O15229), Rattus norvegicus (O88867)
brenda
Wilson, K.; Mole, D.; Binnie, M.; Homer, N.; Zheng, X.; Yard, B.; Iredale, J.; Auer, M.; Webster, S.
Bacterial expression of human kynurenine 3-monooxygenase Solubility, activity, purification
Protein Expr. Purif.
95
96-103
2014
Homo sapiens (O15229), Homo sapiens
brenda
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