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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
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 + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
L-kynurenine + NADPH + O2
? + NADP+
o-hydroxybenzoyl-DL-alanine + NADPH + O2
? + NADP+
additional information
?
-
kynurenine + NADPH + O2

3-hydroxy-kynurenine + NADP+ + H2O
-
-
-
?
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
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
-
-
?
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 + 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
-
-
?
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
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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.
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + 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 + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
L-kynurenine + NADPH + O2
? + NADP+
additional information
?
-
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
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
(6-chloro-1H-indazol-1-yl)acetic acid
-
(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
(R,S)-2-amino-oxo-4-(3'-4'-dichlorophenyl)butanoic acid
-
-
(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%
2-amino-3-(6-chloro-1H-indazol-1-yl)propanoic acid
-
2-benzyl-4-(3,4-dichlorophenyl)-4-oxo-butanoic acid
-
-
2-hydroxy-4-(3,4-dichlorophenyl)-4-oxobutanoic acid
-
-
2-oxo acid derivatives
-
of the 3 branched chain amino acids
2-oxoglutarate
-
mixed type inhibitor
3,4-dichlorohippuric acid
-
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
3,4-dimethoxyhippuric acid
-
3,5-dibromo-L-kynurenine
potent competitive inhibitor
3-(1H-indazol-1-yl)propanoic acid
-
3-(5,6-dichloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(5,6-dichloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
-
3-(5-chloro-1,2-benzoxazol-3-yl)propanoic acid
-
3-(5-chloro-1H-indazol-1-yl)propanoic acid
-
3-(5-chloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(5-chloro-6-cyano-2-oxo-1,3-benzoxazol-3(2H)-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-1,3-benzoxazol-3(2H)-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-1,3-benzoxazol-3(2H)-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-1,3-benzoxazol-3(2H)-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-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
3-(5-chloro-7-methyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(5-cyano-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(5-methoxy-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
-
3-(6-bromo-1H-indazol-1-yl)propanoic acid
-
3-(6-chloro-1H-benzotriazol-1-yl)propanoic acid
-
3-(6-chloro-1H-indazol-1-yl)-2-hydroxypropanoic acid
-
3-(6-chloro-1H-indazol-1-yl)-2-methylpropanoic acid
-
3-(6-chloro-1H-indazol-1-yl)butanoic acid
-
3-(6-chloro-1H-indazol-1-yl)propanoic acid
-
3-(6-chloro-1H-indol-1-yl)propanoic acid
-
3-(6-chloro-3-methyl-1H-indazol-1-yl)propanoic acid
-
3-(6-chloro-3-oxo-3,4-dihydro-2H-1-benzopyran-4-yl)propanoic acid
-
3-(6-methyl-1H-indazol-1-yl)propanoic acid
-
3-nitrobenzoylalanine
-
-
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-(3,4-dichlorophenyl)-4-oxobutanoic acid
-
desamino FCE 28833
4-(6-chloro-1H-indazol-1-yl)butanoic acid
-
4-amino-N-[4-[2-fluoro-5-(trifluoromethyl)phenyl]thiazol-2-yl]benzenesulfonamide
-
50% inhibition at 19nM
5-bromo-3-chloro-DL-kynurenine
-
5-bromo-3-methyl-DL-kynurenine
-
7-chloro-3-methyl-1H-pyrrolo[3,2-c]quinoline-4-carboxylic acid
-
relatively potent and selective inhibitor
alpha-Ketoisocaproate
-
non competitive inhibition
anthranilic acid
-
22% inhibition at 2 mM and 11% inhibition at 0.2 mM
benzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
chloride
mixed-type inhibition
Cl-
-
70% inhibition with 0.1 M NaCl or KCl, competitive with respect to NADPH and non-competitive with respect to L-kynurenine
EDTA
-
68% inhibition at 2 mM
Kynurenic acid
-
13% inhibition at 2 mM and 5% inhibition at 0.2 mM
L-tryptophan
-
35% inhibition at 2 mM and 22% inhibition at 0.2 mM
m-nitrobenzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
p-chloromercuribenzoate
-
weak, 50% inhibition at 0.4 M
pyridoxal
-
less potent than pyridoxal phosphate
pyruvate
-
mixed type inhibitor
xanthurenic acid
-
48% inhibition at 2 mM and 13% inhibition at 0.2 mM
(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
(m-nitrobenzoyl)-alanine
-
50% inhibition at 0.9 micromolar
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
CN-

-
high concentration
CN-
-
inhibition at 0.01 M
GSK065

suitable for preclinical evaluation
GSK065
suitable for preclinical evaluation
GSK366

suitable for preclinical evaluation
GSK366
suitable for preclinical evaluation
GSK428

-
GSK775

-
GSK891

-
pyridoxal 5'-phosphate

noncompetitive
pyridoxal 5'-phosphate
-
non competitive inhibition
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
-
in vivo inhibition
UPF 648
-
in vivo inhibition
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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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
0.000025
4-(3,4-dichlorophenyl)-4-oxobutanoic acid
Homo sapiens
-
pH 7.4, 25°C
0.003
4-(6-chloro-1H-indazol-1-yl)butanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000007 - 0.0000023
GSK366
0.0000027 - 0.000003
GSK775
0.0000036 - 0.0000043
GSK891
0.000035
Ro 61-8048
Homo sapiens
-
pH 7.4, 25°C
0.0000003 - 0.000074
UPF 648
0.0000007
GSK366

Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.0000023
GSK366
Homo sapiens
pH 7.5, temperature not specified in the publication
0.00001
GSK428

Homo sapiens
pH 7.5, temperature not specified in the publication
0.00006
GSK428
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.0000027
GSK775

Homo sapiens
pH 7.5, temperature not specified in the publication
0.000003
GSK775
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.0000036
GSK891

Homo sapiens
pH 7.5, temperature not specified in the publication
0.0000043
GSK891
Pseudomonas fluorescens
pH 7.5, temperature not specified in the publication
0.0000003
UPF 648

Homo sapiens
-
pH 7.4, 25°C
0.000074
UPF 648
Saccharomyces cerevisiae
pH 8.0, 30°C
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Okamoto, H.; Hayaishi, O.
Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria
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Rattus norvegicus
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Rattus norvegicus, Rattus norvegicus Osborne-Mendel
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Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus
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Saccharomyces cerevisiae
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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
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Saccharomyces cerevisiae
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Saito, K.; Quearry, B.J.; Saito, M.; Nowak, T.S.Jr.; Markey S.P.; Heyes, M.P.
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Meriones unguiculatus, Homo sapiens, Macaca mulatta, Mus musculus, Rattus norvegicus
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Kynurenine-3-hydroxylase of Schistocera gregaria
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Schistocerca gregaria
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Subcellular localization and properties of kynurenine 3-hydroxylase from eggs of Ephestia kuhniella Z
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Ephestia kuehniella
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Shin, M.; Sano, K.; Umezawa, C.
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Saccharomyces pastorianus
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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
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Rattus norvegicus
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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
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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
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Rattus norvegicus
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Uemura, T.; Hirai, K.
Purification of L-kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver
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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
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Meriones unguiculatus, Rattus norvegicus
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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
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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.
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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
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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.
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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.
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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
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1994
Rattus norvegicus
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Allegri, G.; Bertazzo, A.; Biasiolo, M.; Costa, C.V.; Ragazzi, E.
Kynurenine pathway enzymes in different species of animals
Adv. Exp. Med. Biol.
527
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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
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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
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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.
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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.
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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