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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
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
Q9MZS9
-
-
-
?
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
Q95NK3
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
Q11PP7
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
O15229
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
Q9MZS9
-
-
-
?
L-kynurenine + NADPH + O2

3-hydroxy-L-kynurenine + NADP+ + H2O
Q86PM2
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
Q86PM2
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
Q8ISJ5
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

?
-
A1Z745
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, 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;
P38169
pH 8.0, 30°C
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Acquired Immunodeficiency Syndrome
Tryptophan metabolism in relation to amino acid alterations during typhoid fever.
Alzheimer Disease
Development of a Rapid Fluorescence-Based High-Throughput Screening Assay to Identify Novel Kynurenine 3-Monooxygenase Inhibitor Scaffolds.
Alzheimer Disease
Structural basis of kynurenine 3-monooxygenase inhibition.
Astrocytoma
Central Nervous System Infection with Borna Disease Virus Causes Kynurenine Pathway Dysregulation and Neurotoxic Quinolinic Acid Production.
Brain Edema
[Effects of Cinnabar and Realgar in Angong Niuhuang powder on heat shock protein, nitric oxide synthase and inflammatory cytokines in contusion cerebral edema]
Brain Edema
[Effects of cinnabar and realgar in angong niuhuang powder on lactate dehydrogenase and its isoenzymes in rats with infectious cerebral edema]
Brain Ischemia
Kynurenine 3-hydroxylase in brain: species activity differences and effect of gerbil cerebral ischemia.
Brain Ischemia
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.
Brain Ischemia
[Absorption and distribution of mercury and arsenic from realgar and cinnabar of angong niuhuang pill in normal rats and rats with cerebral ischemia]
Carcinoma, Hepatocellular
Prognostic significance of kynurenine 3-monooxygenase and effects on proliferation, migration, and invasion of human hepatocellular carcinoma.
Central Nervous System Neoplasms
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Chorea
The kynurenine 3-hydroxylase inhibitor Ro 61-8048 improves dystonia in a genetic model of paroxysmal dyskinesia.
Dyskinesias
Effect of non-dopaminergic drug treatment on Levodopa induced dyskinesias in MPTP monkeys: Common implication of striatal neuropeptides.
Dyskinesias
Effects of the kynurenine 3-hydroxylase inhibitor Ro 61-8048 after intrastriatal injections on the severity of dystonia in the dt sz mutant.
Dyskinesias
Implication of NMDA Receptors in the Antidyskinetic Activity of Cabergoline, CI-1041, and Ro 61-8048 in MPTP Monkeys with Levodopa-induced Dyskinesias.
Dyskinesias
Prolonged kynurenine 3-hydroxylase inhibition reduces development of levodopa-induced dyskinesias in parkinsonian monkeys.
Dyskinesias
The kynurenine 3-hydroxylase inhibitor Ro 61-8048 improves dystonia in a genetic model of paroxysmal dyskinesia.
Dystonia
Effects of the kynurenine 3-hydroxylase inhibitor Ro 61-8048 after intrastriatal injections on the severity of dystonia in the dt sz mutant.
Dystonia
The kynurenine 3-hydroxylase inhibitor Ro 61-8048 improves dystonia in a genetic model of paroxysmal dyskinesia.
Gastritis
Kynurenine 3-monooxygenase mediates inhibition of Th17 differentiation via catabolism of endogenous aryl hydrocarbon receptor ligands.
Glioma
Involvement of the kynurenine pathway in human glioma pathophysiology.
Hearing Loss
Ototoxicity induced by cinnabar (a naturally occurring HgS) in mice through oxidative stress and down-regulated Na(+)/K(+)-ATPase activities.
Huntington Disease
A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease.
Huntington Disease
Bacterial expression of human kynurenine 3-monooxygenase: solubility, activity, purification.
Huntington Disease
Development of a Rapid Fluorescence-Based High-Throughput Screening Assay to Identify Novel Kynurenine 3-Monooxygenase Inhibitor Scaffolds.
Huntington Disease
Development of a Series of Aryl Pyrimidine Kynurenine Monooxygenase Inhibitors as Potential Therapeutic Agents for the Treatment of Huntington's Disease.
Huntington Disease
Development of a Series of Kynurenine 3-Monooxygenase Inhibitors Leading to a Clinical Candidate for the Treatment of Acute Pancreatitis.
Huntington Disease
Development of LC/MS/MS, High-Throughput Enzymatic and Cellular Assays for the Characterization of Compounds That Inhibit Kynurenine Monooxygenase (KMO).
Huntington Disease
First molecular modeling report on novel arylpyrimidine kynurenine monooxygenase inhibitors through multi-QSAR analysis against Huntington's disease: A proposal to chemists!
Huntington Disease
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Huntington Disease
Targeting Kynurenine 3-Monooxygenase (KMO): Implications for Therapy in Huntington's Disease.
Huntington Disease
The novel KMO inhibitor CHDI-340246 leads to a restoration of electrophysiological alterations in mouse models of Huntington's disease.
Hyperalgesia
Upregulation of neuronal kynurenine 3-monooxygenase mediates depression-like behavior in a mouse model of neuropathic pain.
Hypersensitivity
Allergic reactions to tattoo pigment after laser treatment.
Hypersensitivity
[Analysis of adverse effects of cinnabar]
Hypotension
Vasorelaxing Action of the Kynurenine Metabolite, Xanthurenic Acid: The Missing Link in Endotoxin-Induced Hypotension?
Hypothyroidism
Presence of kynurenine hydroxylase in developing rat brain.
Infarction, Middle Cerebral Artery
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.
Infection
A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases.
Infection
Antiviral Effect of IDO in Mouse Fibroblast Cells During Influenza Virus Infection.
Infection
Central Nervous System Infection with Borna Disease Virus Causes Kynurenine Pathway Dysregulation and Neurotoxic Quinolinic Acid Production.
Ischemic Attack, Transient
Mechanism of delayed increases in kynurenine pathway metabolism in damaged brain regions following transient cerebral ischemia.
kynurenine 3-monooxygenase deficiency
Peripheral kynurenine-3-monooxygenase deficiency as a potential risk factor for metabolic syndrome in schizophrenia patients.
Leiomyomatosis
Germline deletions of EXO1 do not cause colorectal tumors and lesions which are null for EXO1 do not have microsatellite instability.
Mercury Poisoning
Chinese patent medicine as a potential source of mercury poisoning.
Mercury Poisoning
Chronic mercury exposure in Late Neolithic/Chalcolithic populations in Portugal from the cultural use of cinnabar.
Myocarditis
Absence of kynurenine 3-monooxygenase reduces mortality of acute viral myocarditis in mice.
Neoplasms
Fluoxetine prevents the development of depressive-like behavior in a mouse model of cancer related fatigue.
Neoplasms
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Neoplasms
Tryptophan PET Imaging of the Kynurenine Pathway in Patient-Derived Xenograft Models of Glioblastoma.
Neoplasms
Whole-exome sequencing combined with functional genomics reveals novel candidate driver cancer genes in endometrial cancer.
Nervous System Diseases
Biochemistry and structural studies of kynurenine 3-monooxygenase reveal allosteric inhibition by Ro 61-8048.
Nervous System Diseases
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.
Neuralgia
Pharmacological kynurenine 3-monooxygenase enzyme inhibition significantly reduces neuropathic pain in a rat model.
Neuralgia
Upregulation of neuronal kynurenine 3-monooxygenase mediates depression-like behavior in a mouse model of neuropathic pain.
Neurodegenerative Diseases
A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases.
Neurodegenerative Diseases
A magnetic bead-based ligand binding assay to facilitate human kynurenine 3-monooxygenase drug discovery.
Neurodegenerative Diseases
Challenges and Opportunities in the Discovery of New Therapeutics Targeting the Kynurenine Pathway.
Neurodegenerative Diseases
Development of a Rapid Fluorescence-Based High-Throughput Screening Assay to Identify Novel Kynurenine 3-Monooxygenase Inhibitor Scaffolds.
Neurodegenerative Diseases
Development of LC/MS/MS, High-Throughput Enzymatic and Cellular Assays for the Characterization of Compounds That Inhibit Kynurenine Monooxygenase (KMO).
Neurodegenerative Diseases
Dual Role of the Carboxyl-terminal Region of Pig Liver L-Kynurenine 3-Monooxygenase: Mitochondrial Targeting Signal and Enzymatic Activity.
Neurodegenerative Diseases
First molecular modeling report on novel arylpyrimidine kynurenine monooxygenase inhibitors through multi-QSAR analysis against Huntington's disease: A proposal to chemists!
Neurodegenerative Diseases
Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).
Neurodegenerative Diseases
Kynurenine Monooxygenase (KMO) Inhibitors for the Treatment of Acute Pancreatitis and Neurodegenerative Disorders.
Neurodegenerative Diseases
Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenase.
Neurodegenerative Diseases
Structural Basis for Inhibitor-Induced Hydrogen Peroxide Production by Kynurenine 3-Monooxygenase.
Neurodegenerative Diseases
Structural basis of kynurenine 3-monooxygenase inhibition.
Neurodegenerative Diseases
Substrate and inhibitor specificity of kynurenine monooxygenase from Cytophaga hutchinsonii.
Neurodegenerative Diseases
The kynurenine pathway modulates neurodegeneration in a Drosophila model of Huntington's disease.
Obesity
Erratum: The kynurenine pathway is activated in human obesity and shifted toward kynurenine monooxygenase activation.
Obesity
Peripheral kynurenine-3-monooxygenase deficiency as a potential risk factor for metabolic syndrome in schizophrenia patients.
Obesity
The kynurenine pathway is activated in human obesity and shifted toward kynurenine monooxygenase activation.
Oral Ulcer
[Detection of Cinnabars in Mongolian Medicines Using Raman Spectroscopy].
Pancreatitis
Development of a Series of Kynurenine 3-Monooxygenase Inhibitors Leading to a Clinical Candidate for the Treatment of Acute Pancreatitis.
Pancreatitis
Increased levels of 3-hydroxykynurenine parallel disease severity in human acute pancreatitis.
Pancreatitis
Kynurenine Monooxygenase (KMO) Inhibitors for the Treatment of Acute Pancreatitis and Neurodegenerative Disorders.
Pancreatitis
Pancreatitis: KMO inhibitor for multi-organ failure in experimental acute pancreatitis.
Pancreatitis
The discovery of potent and selective kynurenine 3-monooxygenase inhibitors for the treatment of acute pancreatitis.
Parkinson Disease
Effect of kynurenine 3-hydroxylase inhibition on the dyskinetic and antiparkinsonian responses to levodopa in Parkinsonian monkeys.
Parkinson Disease
Tryptophan-2,3-dioxygenase (TDO) inhibition ameliorates neurodegeneration by modulation of kynurenine pathway metabolites.
Pneumoconiosis
[On the problem of the combined effect of cinnabar and mercury vapor on the development of pneumoconiosis in experimental animals]
Proteinuria
Loss of Kynurenine 3-Mono-oxygenase Causes Proteinuria.
Sepsis
Is sepsis-induced apoptosis associated with macrophage dysfunction?
Sexually Transmitted Diseases
[Mercury--a major agent in the history of medicine and alchemy]
Stroke
Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400.
Stroke
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.
Trachoma
[Mercury--a major agent in the history of medicine and alchemy]
Virus Diseases
Absence of kynurenine 3-monooxygenase reduces mortality of acute viral myocarditis in mice.
Yellow Fever
Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti.
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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
Homo sapiens, Macaca mulatta, Meriones unguiculatus, 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, Mus musculus, Oryctolagus cuniculus, 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, Anopheles stephensi (Q8ISJ5)
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, Aedes aegypti (Q86PM2), 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
Homo sapiens, Saccharomyces cerevisiae
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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