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Enzyme Nomenclature
Information on EC 1.14.13.9 - kynurenine 3-monooxygenase
for references in articles please use BRENDA:EC1.14.13.9
Word Map on EC 1.14.13.9
- 1.14.13.9
- mercury
- hg
-
kynurenic
- 3-hydroxykynurenine
-
quinolinic
-
2,3-dioxygenase
- kynureninase
- indoleamine
- huntington
- 3-hydroxyanthranilate
-
paint
- methylmercury
-
quin
-
ochre
- jacobaeae
-
cronbach
-
realgar
-
vermilion
-
bartlett
-
slovenia
-
geochemical
- senecio
-
roman
-
excitotoxins
-
xanthurenic
-
micro-raman
-
archaeological
-
mineralogical
-
ommochrome
-
calcite
- medicine
- analysis
- pharmacology
- molecular biology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.14.13.9
-
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RECOMMENDED NAME
GeneOntology No.
kynurenine 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9029-61-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male, 4-month-old diabetic/hyperlipidemic New Zealand White rabbits
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
additional information
-
the C-terminal region of pig liver KMO plays a dual role. First, it is required for the enzymatic activity. Second, it functions as a mitochondrial targeting signal
drug target
-
contents of L-tryptophan and monoamines and their metabolites are measured in the serum and hippocampus of kynurenine 3-monooxygenase KO mice. It is investigated whether antidepressants improve the depressive-like behaviors in kynurenine 3-monooxygenase KO mice. KO mice show antidepressants-responsive depressive-like behaviors and monoaminergic dysfunctions via abnormality of kynurenine metabolism with good validities as model for major depressive disorder
drug target
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
drug target
-
kynurenine represents a branch point of the kynurenine pathway, being converted into the neurotoxin 3-hydroxykynurenine via kynurenine monooxygenase, neuroprotectant kynurenic acid, and anthranilic acid. As a result of this branch point, kynurenine monooxygenase is an attractive drug target for several neurodegenerative and/or neuroinflammatory diseases, especially Huntington's, Alzheimer's, and Parkinson's diseases
drug target
-
the enzyme is a potential therapeutic target for neurodegenerative and neurologic disorders
drug target
-
the enzyme is a clinical candidate for the treatment of acute pancreatitis
drug target
-
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington’s and Alzheimer’s. It is a target for acute pancreatitis multiple organ dysfunction syndrome
drug target
-
the enzyme is a therapeutic target in several disease states, including Huntington's disease
malfunction
-
contents of L-tryptophan and monoamines and their metabolites are measured in the serum and hippocampus of kynurenine 3-monooxygenase KO mice. It is investigated whether antidepressants improve the depressive-like behaviors in kynurenine 3-monooxygenase KO mice. A deficiency in kynurenine 3-monooxygenase appears to be implicated in antidepressant-responsive depression-like behaviors. In the kynurenine 3-monooxygenase KO mice, there are abnormal kynurenine pathway metabolites and monoamines. The abnormal monoamines in addition to the abnormal kynurenine pathway metabolites may play an important role in the pathophysiology of major depressive disorder
malfunction
-
adaptive—and possibly regulatory-changes in mice with a targeted deletion of kynurenine 3-monooxygenase (Kmo-/-) are investigated kynurenine 3-monooxygenase-deficient mice are characterized using six behavioral assays relevant for the study of schizophrenia. Elimination of kynurenine 3-monooxygenase in mice is associated with multiple gene and functional alterations that appear to duplicate aspects of the psychopathology of several neuropsychiatric disorder
malfunction
-
human polymorphism in the C-terminal region of the enzyme results in an Arg452Cys mutation, statistically linked to bipolar disorder and schizophrenia
malfunction
-
the white egg 1 (w-1) mutant, which is characterized by white eyes and white eggs, is deficient in Bombyx kynurenine 3-monooxygenase activity. To investigate whether the w-1 mutant phenotype is rescued by introducing the wild-type kynurenine 3-monooxygenase gene, transgenic silkworms with the wild-type Bombyx kynurenine 3-monooxygenase gene under the control of either the cytoplasmic actin gene promoter or the native kynurenine 3-monooxygenase gene promoter are constructed. The results indicate that the wild-type kynurenine 3-monooxygenase gene can be used as a marker gene for visually screening transgenic silkworms
metabolism
-
enzyme of the kynurenine pathway, which is the major catabolic route of tryptophan
metabolism
-
the enzyme is involved in kynurenine pathway. It catalyzes the decisive step in production of metabolites as quinolinic acid
metabolism
-
the enzyme is very important in kynurenine pathway because it catalyzes the decisive step in production of metabolites as quinolinic acid
metabolism
-
the enzyme is central to the kynurenine pathway of tryptophan metabolism
physiological function
-
the white egg 1 mutant, which is characterized by white eyes and white eggs, is deficient in Bombyx kynurenine 3-monooxygenase activity.Expression of the wild-type gene under control of either the cytoplasmic actin gene promoter (A3KMO) or the native KMO gene promoter (KKMO) leads to adults with brown eyes, and the eggs laid by the transgenic females are also brown. The A3KMO silkworm lines express the transcript in the mid-gut, fat bodies, and Malpighian tubules. The KKMO line expresses the transcript only in the fat bodies and Malpighian tubules. The intensity of eye and egg color in the transgenic lines is proportional to the KMO expression level
physiological function
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
physiological function
-
adaptive-and possibly regulatory-changes in mice with a targeted deletion of kynurenine 3-monooxygenase (Kmo-/-) are investigated kynurenine 3-monooxygenase-deficient mice are characterized using six behavioral assays relevant for the study of schizophrenia. Elimination of kynurenine 3-monooxygenase in mice is associated with multiple gene and functional alterations that appear to duplicate aspects of the psychopathology of several neuropsychiatric disorder
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-bromo-L-kynurenine + NADPH + H+ + O2
5-bromo-3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
5-chloro-L-kynurenine + NADPH + H+ + O2
5-chloro-3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the enzyme is involved in the kynurenine pathway of tryptophan metabolsim, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme activity depends on the reduction state of the enzyme
-
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme activity depends on the reduction state of the enzyme
-
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
-
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
L-kynurenine + NADH + H+ + O2
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
-
L-kynurenine + NADH + H+ + O2
3-hydroxy-L-kynurenine + NAD+ + H2O
-
-
-
-
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is involved in tryptophan catabolism
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
prolonged kynurenine 3-hydroxylase inhibition reduces development of levodopa-induced dyskinesias in Parkinsonian monkeys, enzyme regulation and involvement in Parkinson's disease, overview
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
the enzyme is not involved in regulation of 3-hydroxy-L-kynurenine level in vivo
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
function of the enzyme may change from a role in immunosuppression at the maternal-fetal interface in early pregnancy to one associated with regulation of fetoplacental blood flow or placental metabolism in late gestation
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
binding of L-kynurenine to the oxidized enzyme is relatively slow and involves at least two reversible steps
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
r
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
no reaction with D-isomer
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
enzyme is involved in L-tryptophan catabolism, pathway regulation in comparison to other species, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
no reaction with D-isomer
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
NADH is less effective
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
step in L-tryptophan catabolism, overview
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in injured brain regions following cerebral ischemia
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
increased activity in the spinal cord with experimental allergic encephalopathy
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
key enzyme in the kynurenine pathway of tryptophan degradation
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
rate limiting step in the pyridine nucleotide biosynthesis from tryptophan
-
-
?
o-hydroxybenzoyl-DL-alanine + NADPH + O2
? + NADP+
-
about 25% of the activity with L-kynurenine
-
-
?
o-hydroxybenzoyl-DL-alanine + NADPH + O2
? + NADP+
-
about 25% of the activity with L-kynurenine
-
-
?
additional information
?
-
enzyme is involved in eye pigmentation
-
-
-
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease by aggregation in nuclear and cytoplasmic inclusion bodies
-
-
-
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, newborn mice delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
-
-
additional information
?
-
-
catalyzes NADH- and NADPH-linked reductions of low molecular weight acceptors such as 2,6-dichlorophenolindophenol and ferricyanide
-
-
-
additional information
?
-
-
age affects the enzyme activities of tryptophan metabolism along the kynurenine pathway, one of the various tryptophan metabolic routes, kynurenine 3-monooxygenase activity progressively decreases with age in liver and kidney of newborn to mature rats, quantitative overview
-
-
-
additional information
?
-
-
the kynurenine pathway of tryptophan degradation contains three neuroactive metabolites: the neuroinhibitory agent kynurenic acid and, in a competing branch, the free radical generator 3-hydroxykynurenine and the excitotoxin quinolinic acid, rat pups delivered by UPF 648-treated mothers and immediately exposed to neonatal asphyxia show further enhanced brain kynurenic acid levels, overview
-
-
-
additional information
?
-
-
the enzyme is responsible for driving formation of neurotoxic and neuroprotective kynurenine metabolites, regulation mechanism, overview
-
-
-
additional information
?
-
-
the enzyme is a very potent suppressor of toxicity of a fragment of the protein huntingtin, Htt, which causes the neurodegenerative Huntington disease in humans by aggregation in nuclear and cytoplasmic inclusion bodies
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the enzyme is involved in the kynurenine pathway of tryptophan metabolsim, overview
-
-
?
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate
the product acts as apoptotic signal
-
ir
kynurenine + NADPH + O2
3-hydroxy-kynurenine + NADP+ + H2O
-
enzyme inhibition in immature rats shifts cerebral kynurenine pathway metabolism toward increased kynurenic acid formation, overview
-
-
?
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
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+
-
increased activity in the spinal cord with experimental allergic encephalopathy
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
key enzyme in the kynurenine pathway of tryptophan degradation
-
-
?
L-kynurenine + NADPH + O2
? + NADP+
-
rate limiting step in the pyridine nucleotide biosynthesis from tryptophan
-
-
?
additional information
?
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
dependent on, the Gly-X-Gly-X-X-Gly motif, residues 27-32, and the hydrophobic amino acid residues at positions 23, 25, 36, 39, 46, and 48 are indispensable for correct folding of the beta1-alpha-beta2-structure of the dinucleotide binding domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S,2S)-2-(3,4-dichlorobenzoyl)-cyclopropane-1-carboxylic acid
-
KMO inhibitor UPF 648, totally blocks KMO at 0.1 and 0.01 mM and is still highly active at 0.001 mM (81% inhibition). It reduces 3-hydroxykynurenine synthesis by 64% without affecting kynurenic acid formation. In neuron-depleted striata, UPF 648 decreases both 3-hydroxykynurenine and quinolinic acid production by 77% and 66%, respectively and also raises kynurenic acid synthesis by 27%. 0.1 mM UPF 648 blocks KMO in both lesioned and contralateral striatum, but does not interfere with KAT activity in either tissue
(R)-3-(5-chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
-
-
-
(R,S)-2-amino-oxo-4-(3',4'-dichlorophenyl)butanoic acid
-
FCE 28833, 50% inhibition at 0.2 microM, blocks not only the cerebral but also the peripheral enzyme
(S)-3-(5-Chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
-
-
-
(S)-9-(4-aminopiperazine-1-yl)-8-fluoro-3-methyl-6-oxo-2,3,5,6-tetrahydro-4H-1-oxa-3a-azaphenalene-5-carboxylic acid
-
does not affect KMO activity significantly, 1 mM inhibits by 17%
3-(5,6-dichloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
-
-
-
3-(5-chloro-6-cyclopropoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
-
-
3-(5-chloro-6-ethoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
-
-
3-(5-chloro-6-ethyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
-
-
3-(5-chloro-6-methoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
-
-
-
3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
-
-
-
3-[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-[(1R)-1-(1,3-oxazol-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(4-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(6-methylpyridazin-3-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(6-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[5-chloro-6-[(1R)-1-(pyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
-
-
-
3-[6-(benzyloxy)-5-chloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
-
-
-
3-[6-chloro-3-oxo-7-[(1R)-1-(pyridin-2-yl)ethoxy]-3,4-dihydro-2H-1,4-benzoxazin-4-yl]propanoic acid
-
-
-
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indazol-1-yl]propanoic acid
-
-
-
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indol-1-yl]-propanoic acid
-
-
-
4-amino-N-[4-[2-fluoro-5-(trifluoromethyl)phenyl]thiazol-2-yl]benzenesulfonamide
-
50% inhibition at 19nM
7-chloro-3-methyl-1H-pyrrolo[3,2-c]quinoline-4-carboxylic acid
-
relatively potent and selective inhibitor
benzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
Cl-
-
70% inhibition with 0.1 M NaCl or KCl, competitive with respect to NADPH and non-competitive with respect to L-kynurenine
m-nitrobenzoylalanine
-
KMO inhibitor that mimics the substrate structure, and also stimulates reduction of the flavin by NADPH
(m-nitrobenzoyl)-alanine
-
mNBA, leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
(m-nitrobenzoyl)-alanine
-
mNBA, leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
(m-nitrobenzoyl)-alanine
-
various pyrrolo[3,2-c]quinoline derivates cause enzyme inhibition
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
Ro-61-8048, 50% inhibition at 37 nM
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
leads to an increase of L-kynurenine and kynurenic acid concentrations in the brain cortex after application in vivo
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
inhibition after oral or intraperitoneal administration
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
i.e. Ro 61-8048, high-affinity low molecular inhibitor
Ro 61-8048
-
noncompetitive. Theinhibitor is bound in the tunnel at the interface where the N- and C-terminal domains associate
UPF 648
UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine
additional information
-
kynurenines substituted with a halogen at the 5-position are excellent substrates, with values of kcat and kcat/Km comparable to or higher than kynurenine. Kynurenines substituted in the 3-position are competitive inhibitors, with KI values lower than the Km for kynurenine. Bromination also enhances inhibition. A pharmacophore model of kynurenine monooxygenase is developed, and predicted that 3,4-dichlorohippuric acid would be an inhibitor
-
additional information
kynurenines substituted with a halogen at the 5-position are excellent substrates, with values of kcat and kcat/Km comparable to or higher than kynurenine. Kynurenines substituted in the 3-position are competitive inhibitors, with KI values lower than the Km for kynurenine. Bromination also enhances inhibition. A pharmacophore model of kynurenine monooxygenase is developed, and predicted that 3,4-dichlorohippuric acid would be an inhibitor
-
additional information
-
inhibition by various 2-amino-4-aryl-4-oxobut-2-enoic acids and esters at 10 micromolar; inhibition by various 4-aryl-2-hyroxy-4-oxobut-2-enoic acids and esters at 10 micromolar
-
additional information
-
the molecular mechanism of action of three classes of inhibitors with differentiated binding modes and kinetics is reported. Two inhibitor classes trap the catalytic flavin in a tilting conformation. This correlates with picomolar affinities, increased residence times and an absence of the peroxide production
-
additional information
-
the specific enzyme activity is not affected by cloricromene in vitro and in vivo in liver and kidney
-
additional information
-
targeted inhibition of KMO is a viable strategy for achieving local elevation of kynurenate concentrations
-
additional information
-
development and optimization of a series of inhibitors
-
additional information
-
the molecular mechanism of action of three classes of inhibitors with differentiated binding modes and kinetics is reported. Two inhibitor classes trap the catalytic flavin in a tilting conformation. This correlates with picomolar affinities, increased residence times and an absence of the peroxide production
-
additional information
-
inhibition by N-(4-phenylthiazol-2-yl)benzenesulfonamides with various modifications
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
a systemic inflammatory challenge stimulates KMO expression in brain, increased enzyme expression is observed in rat brain 24 h post lipopolysaccharide treatment, without any change in kynurenine aminotransferase II expression
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
5-bromo-L-kynurenine
pH and temperature not specified in the publication
0.002
5-chloro-L-kynurenine
pH and temperature not specified in the publication
0.067
L-kynurenine
pH and temperature not specified in the publication
0.153
L-kynurenine
-
pH 7, 37°C, full length 12His-tagged enzyme, FLAG tag removed during affinity purification
0.0087
NADPH
-
pH 7, 37°C, full length 12His-tagged enzyme, FLAG tag removed during affinity purification
additional information
additional information
-
steady-state kinetics and ligand perturbation of flavin fluorescence, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
5-bromo-L-kynurenine
pH and temperature not specified in the publication
0.8
5-chloro-L-kynurenine
pH and temperature not specified in the publication
2
L-kynurenine
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
133.3
5-bromo-L-kynurenine
pH and temperature not specified in the publication
400
5-chloro-L-kynurenine
pH and temperature not specified in the publication
29.9
L-kynurenine
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000095
(R,S)-2-amino-oxo-4-(3'-4'-dichlorophenyl)butanoic acid
-
competitive inhibitor
0.034
3,4-dichlorohippuric acid
pH and temperature not specified in the publication
-
0.0000048
3,4-dimethoxy-N-[4-(3-nitrophenyl)thiazol-2-yl]benzenesulfonamide
-
competitive inhibitor
1
3,4-dimethoxyhippuric acid
pH and temperature not specified in the publication
-
0.0015
3,5-dibromo-L-kynurenine
pH and temperature not specified in the publication
0.0138
3-chloro-DL-kynurenine
pH and temperature not specified in the publication
0.0086
3-methyl-DL-kynurenine
pH and temperature not specified in the publication
0.011
5-bromo-3-chloro-DL-kynurenine
pH and temperature not specified in the publication
0.0102
5-bromo-3-methyl-DL-kynurenine
pH and temperature not specified in the publication
-
0.0135
Ro 61-8048
-
pH and temperature not specified in the publication
11.2
chloride
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
0.17
pyridoxal 5'-phosphate
recombinant enzyme, with respect to NADPH, pH 7.5, 37°C
0.27
pyridoxal 5'-phosphate
recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
(6-chloro-1H-indazol-1-yl)acetic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000025
(R)-3-(5-chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00025
(S)-3-(5-Chloro-2-oxo-6-(1-(pyridin-2-yl)ethoxy)benzo[d]oxazol-3(2H)-yl)propanoate
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0025
2-amino-3-(6-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0063
3-(1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000063
3-(5,6-dichloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000063
3-(5,6-dichloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000025
3-(5-chloro-1,2-benzoxazol-3-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.001
3-(5-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.000013
3-(5-chloro-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0001
3-(5-chloro-6-cyano-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000032
3-(5-chloro-6-cyclopropoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000005
3-(5-chloro-6-ethoxy-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.000005
3-(5-chloro-6-ethoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00001
3-(5-chloro-6-ethyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.00001
3-(5-chloro-6-ethyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000013
3-(5-chloro-6-methoxy-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.000013
3-(5-chloro-6-methoxy-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000013
3-(5-chloro-6-methyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000126
3-(5-chloro-6-methyl-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl)propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000063
3-(5-chloro-7-methyl-2-oxo-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.00063
3-(5-cyano-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.001
3-(5-methoxy-2-methylidene-1,3-benzoxazol-3(2H)-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000398
3-(6-bromo-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0005
3-(6-chloro-1H-benzotriazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0006
3-(6-chloro-1H-indazol-1-yl)-2-hydroxypropanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0025
3-(6-chloro-1H-indazol-1-yl)-2-methylpropanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.005
3-(6-chloro-1H-indazol-1-yl)butanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.00005
3-(6-chloro-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.00013
3-(6-chloro-1H-indol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.002
3-(6-chloro-3-methyl-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.000079
3-(6-chloro-3-oxo-3,4-dihydro-2H-1-benzopyran-4-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0032
3-(6-methyl-1H-indazol-1-yl)propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.005
3-[2-methylidene-5-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0001
3-[5-chloro-2-oxo-6-(propan-2-yl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-2-oxo-6-(pyridin-2-ylmethoxy)-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000398
3-[5-chloro-2-oxo-6-(trifluoromethyl)-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000013
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridazin-3-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000002
3-[5-chloro-2-oxo-6-[(1R)-1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzothiazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000005
3-[5-chloro-2-oxo-6-[(1R)-1-(pyrimidin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000079
3-[5-chloro-2-oxo-6-[(propan-2-yl)oxy]-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-2-oxo-6-[1-(pyridin-2-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000794
3-[5-chloro-2-oxo-6-[2-(pyrrolidin-1-yl)ethoxy]-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000032
3-[5-chloro-6-(2-methoxyethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000013
3-[5-chloro-6-(2-methylpropyl)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000025
3-[5-chloro-6-(cyclobutylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00001
3-[5-chloro-6-(cyclopropylmethoxy)-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000032
3-[5-chloro-6-(cyclopropyloxy)-2-oxo-1,3-benzoxazol-3(2H)-yl]propanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000032
3-[5-chloro-6-[(1R)-1-(1,3-oxazol-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00000398
3-[5-chloro-6-[(1R)-1-(4-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000032
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00000316
3-[5-chloro-6-[(1R)-1-(5-chloropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000032
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000025
3-[5-chloro-6-[(1R)-1-(5-fluoropyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.0000032
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00000316
3-[5-chloro-6-[(1R)-1-(5-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000002
3-[5-chloro-6-[(1R)-1-(6-methylpyridazin-3-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000005
3-[5-chloro-6-[(1R)-1-(6-methylpyridin-2-yl)ethoxy]-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid, 3-[5-chloro-6-[(1R)-1-(pyridin-2-yl)ethoxy]-1,2-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000025
3-[6-(benzyloxy)-5-chloro-2-oxo-2,3-dihydro-1,3-benzoxazol-3-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000005
3-[6-chloro-3-oxo-7-[(1R)-1-(pyridin-2-yl)ethoxy]-3,4-dihydro-2H-1,4-benzoxazin-4-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.00000316
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indazol-1-yl]propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.000005
3-[6-chloro-5-[(1R)-1-(pyridin-2-yl)ethoxy]-1H-indol-1-yl]-propanoic acid
Pseudomonas fluorescens;
-
pH and temperature not specified in the publication
-
0.003
4-(6-chloro-1H-indazol-1-yl)butanoic acid
Homo sapiens;
-
pH and temperature not specified in the publication
0.0000007
GSK366
Pseudomonas fluorescens;
-
pH 7.5, temperature not specified in the publication
0.00006
GSK428
Pseudomonas fluorescens;
-
pH 7.5, temperature not specified in the publication
0.000003
GSK775
Pseudomonas fluorescens;
-
pH 7.5, temperature not specified in the publication
0.0000043
GSK891
Pseudomonas fluorescens;
-
pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
0.0025
additional information
additional information
-
specific activities of apoenzyme and holoenzyme with different electron acceptors
additional information
-
specific activity in organs of rats with experimental allergic encephalopathy
additional information
-
enzyme activity at different temperatures in different strains
additional information
-
enzyme activity with different cofactors and under anaerobic conditions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in first and second trimester of the placenta, within the fetal villus
-
especially in stromal and glandular epithelium in the first trimester decidua
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
additional information
-
-
additional information
-
constitutive expression of the enzyme in all developmental stages from egg via larva and pupa to adult mosquito
additional information
constitutive expression of the enzyme in all developmental stages from egg via larva and pupa to adult mosquito
additional information
-
enzyme expression analysis in untreated and in brain after induction of inflammation, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme is hydrophobis and contains 2 transmembrane segments
-
enzyme is hydrophobis and contains 2 transmembrane segments
-
-
the C terminus of the enzyme contains a putative outer mitochondrial membrane-targeting sequence and this portion of the molecule is required enzyme function
-
the C terminus of the enzyme contains a putative outer mitochondrial membrane-targeting sequence and this portion of the molecule is required enzyme function
-
the C-terminal region functions as a mitochondrial targeting signal
-
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas fluorescens;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P38169
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
55760
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
?
-
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE
-
additional information
-
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are obtained by hanging-drop vapor diffusion at 20°C. Crystal structures of the complex of the full-length enzyme with the substrate L-kynurenine and in complex with L-kynurenine and Ro 61-8048 at a resolution of 1.85 and 2.34 A, respectively. The crystals of the enzyme-L-kynurenine complex belong to the space group P2(1) with 1 enzyme molecule in the asymmetric unit. The crystal structure of the enzyme–L-kynurenine-Ro61-8048 complex belongs to the space group P2(1)2(1)2(1) with 1 pfKMO molecule in the asymmetric unit. The crystal structure of the SeMet enzyme derivative belongs to the space group P2(1) with 2 enzyme molecules in the asymmetric unit
-
crystal structure, in the free form and in complex with the tight-binding inhibitor UPF 648. UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
disulfide reductants like dithiothreitol or 2-mercaptoethanol stabilize the enzyme
-
enzyme is protected against inactivation in the solubilized state by the presence of DTT, Triton X-100, and FAD in 0.1 M Tris-acetate buffer at pH 8.1
-
purified recombinant enzyme is highly unstable, activity decreases directly after purification also at -80°C
solubilized enzyme is appreciably stabilized in 0.05 M Tris-acetate buffer, pH 8.1, 1 mM DTT, 0.2 M mannitol, 0.2% Triton X-100, 0.005 mM FAD
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
recombinant enzyme 8.8fold from Escherichia coli strain by ammonium sulfate fractionation and ion exchange chromatography to homogeneity
-
recombinant enzyme from Sf9 insect cells by solubilization with Triton X-100 and affinity chromatography
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AsK3H, DNA and amino acid sequence determination and analysis, functional expression in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, membrane associated
DNA and amino acid sequence determnination and analysis, sequence comparisons, expression of FLAG-tagged wild-type enzyme and of C-terminal truncation mutants in COS-7 cells. The FLAG tag directs the wild-type enzyme to mitochondria but also to the cytosol and the plasma mambrane, overview
-
gene kh, DNA and amino acid sequence analysis of wild-type and mutant genes, expression in Spodoptera frugiperda Sf9 cells as His-tagged, soluble protein via the baculovirus infection system
gene Tccn, homology-based cloning, DNA and amino acid sequence determination and analysis, gene structure analysis, the Tccn gene is located on linkage group 2
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N465A
-
about 80% of the enzyme activity compared with that of the wild-type enzyme
E372A
-
about 15% of the enzyme activity compared with that of the wild-type enzyme
E372Q
-
about 5% of the enzyme activity compared with that of the wild-type enzyme
M373L
-
about 60% of the enzyme activity compared with that of the wild-type enzyme
N369A
-
about 65% of the enzyme activity compared with that of the wild-type enzyme
Q424A
-
mutation does not greatly affect enzyme activity. Ro 61-8048 shows no inhibition to the pfKMO mutant enzyme
Y404F
-
about 40% of the enzyme activity compared with that of the wild-type enzyme
Y98F
-
about 1% of the enzyme activity compared with that of the wild-type enzyme
additional information
additional information
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
additional information
-
an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes
-
additional information
-
enzyme deficiency leads to the white eyes and white eggs w-1 phenotype in mutant silkworms, it can be partially rescued by expression of wild-type enzyme under control of either the cytoplasmic actin gene promoter, A3KMO, or the native KMO gene promoter, KKMO, phenotypes, overview
additional information
-
enzyme deficiency leads to the white eyes and white eggs w-1 phenotype in mutant silkworms, it can be partially rescued by expression of wild-type enzyme under control of either the cytoplasmic actin gene promoter, A3KMO, or the native KMO gene promoter, KKMO, phenotypes, overview
-
additional information
-
the enzyme is systematically truncated according to the sequence alignments and the predicted secondary structures. For the truncations 1-377, 1-379, and 1-394, which have 1 or 2 more predicted alpha-helices than that of the 1-372/374, no or weak protein expression is detected. Although for the truncation 1-430 that has the C-terminal hydrophobic tail removed, no enzymatic activities can be detected but the protein expression is normal. The results indicate that the C-terminal portion is important for both the folding and the enzymatic activity
additional information
-
construction of C-terminal truncation mutants KMODELTAC10, KMODELTAC20, KMODELTAC30, KMODELTAC50, and KMODELTAC70, that are all localized in the cytosol after recombinant expression in COS-7 cells, exept for KMODELTAC10. Two forms of C-terminal truncation, KMODELTAC10D and KMODELTAC20D retain almost full activity but KMODELTAC30D shows 1.6fold higher activity than the wild-type. The activities of KMODELTAC50 and KMODELTAC70 is highly reduced, overview. The quantity of expressed KMODELTA30D in COS-7 cellsis 1.3fold higher than the wild-type KMO
additional information
construction of mutants lacking functional enzyme via RNA interference, RNAi, the gene is unlinked to known eye-color mutants
additional information
-
construction of mutants lacking functional enzyme via RNA interference, RNAi, the gene is unlinked to known eye-color mutants
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
comprehensive panel of biochemical and cell-based assays that use liquid chromatography/tandem mass spectrometry to quantify unlabeled kynurenine and 3-hydroxykynurenine and application to measure kynurenine monooxygenase inhibition in cell and tissue extracts, as well as cellular assays
medicine
molecular biology
pharmacology
medicine
-
the enzyme is an attractive target for the treatment of ischemic stroke
medicine
-
T helper 17 cells preferentially express kynurenine 3-monooxygenase. Enzyme inhibition, either with a specific inhibitor or via siRNA-mediated silencing, markedly increases IL-17 productionin vitro, whereas IFN-gamma production by T helper 1 cells is unaffected. Inhibition of kynurenine 3-monooxygenase significantly exacerbates disease in a Th17-driven model of autoimmune gastritis
medicine
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
medicine
-
the enzyme is a potential therapeutic target for neurodegenerative and neurologic disorders
medicine
-
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington's and Alzheimer's. It is a target for acute pancreatitis multiple organ dysfunction syndrome
medicine
-
inhibition of the enzyme shows benefit in neurodegenerative diseases such as Huntington's and Alzheimer's. It is a target for acute pancreatitis multiple organ dysfunction syndrome (AP-MODS)
medicine
-
the enzyme is an attractive target for the treatment of ischemic stroke
-
molecular biology
development of a transformant selection system for Tribolium castaneum on the basis of mutant rescue
molecular biology
-
the wild-type enzyme gene can be used as a marker gene for visually screening transgenic silkworms; wild-type KMO gene can be used as a marker gene for visually screening transgenic silkworms
molecular biology
-
wild-type KMO gene can be used as a marker gene for visually screening transgenic silkworms
-
pharmacology
the enzyme is a potential drug target for treatment of neurodegenerative disorders such as Huntington's and Alzheimer's diseases
pharmacology
-
kynurenine represents a branch point of the kynurenine pathway, being converted into the neurotoxin 3-hydroxykynurenine via kynurenine monooxygenase, neuroprotectant kynurenic acid, and anthranilic acid. As a result of this branch point, kynurenine monooxygenase is an attractive drug target for several neurodegenerative and/or neuroinflammatory diseases, especially Huntington's, Alzheimer's, and Parkinson's diseases
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.9)
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