1.14.13.9: kynurenine 3-monooxygenase
This is an abbreviated version!
For detailed information about kynurenine 3-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.9
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1.14.13.9
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mercury
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hg
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kynurenic
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3-hydroxykynurenine
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quinolinic
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2,3-dioxygenase
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kynureninase
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indoleamine
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cronbach
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huntington
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bartlett
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paint
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3-hydroxyanthranilic
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quin
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neuroactive
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ochre
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realgar
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psychometric
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calcite
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methylmercury
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xanthurenic
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eigenvalue
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vermilion
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hematite
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test-retest
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excitotoxins
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ommochrome
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artwork
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geochemical
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indoleamine-2,3-dioxygenase
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archaeological
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varimax
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roman
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mineralogical
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slovenia
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micro-raman
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molecular biology
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medicine
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analysis
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pharmacology
- 1.14.13.9
- mercury
- hg
-
kynurenic
- 3-hydroxykynurenine
-
quinolinic
-
2,3-dioxygenase
- kynureninase
- indoleamine
-
cronbach
- huntington
-
bartlett
-
paint
-
3-hydroxyanthranilic
-
quin
-
neuroactive
-
ochre
-
realgar
-
psychometric
-
calcite
- methylmercury
-
xanthurenic
-
eigenvalue
-
vermilion
-
hematite
-
test-retest
-
excitotoxins
-
ommochrome
-
artwork
-
geochemical
- indoleamine-2,3-dioxygenase
-
archaeological
-
varimax
-
roman
-
mineralogical
-
slovenia
-
micro-raman
- molecular biology
- medicine
- analysis
- pharmacology
Reaction
Synonyms
BcKMO, Bna4, cinnabar, EC 1.14.1.2, EC 1.99.1.5, FAD dependent kynurenine 3-monooxygenase, flavin adenine dinucleotide dependent kynurenine 3-monooxygenase, hKMO, Hs-KMO, K3H, KMO, KYN-OHase, kynurenine 3-hydroxylase, kynurenine 3-monooxygenase, kynurenine hydroxylase, kynurenine monooxygenase, kynurenine-3-monooxygenase, L-kynurenine 3-monooxygenase, L-kynurenine,NADPH2:oxygen oxidoreductase (3-hydroxylating), L-kynurenine-3-hydroxylase, More, NADPH-dependent flavin monooxygenase, oxygenase, kynurenine 3-mono-, pfKMO, Rat-KMO, scKMO
ECTree
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Engineering
Engineering on EC 1.14.13.9 - kynurenine 3-monooxygenase
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E366Q
2% of the enzyme activity compared with that of the wild-type enzyme
M367A
2% of the enzyme activity compared with that of the wild-type enzyme
M367L
13% of the enzyme activity compared with that of the wild-type enzyme
N363A
28% of the enzyme activity compared with that of the wild-type enzyme
N465A
about 80% of the enzyme activity compared with that of the wild-type enzyme
R85K
1% of the enzyme activity compared with that of the wild-type enzyme
Y398A
1% of the enzyme activity compared with that of the wild-type enzyme
Y398F
1% of the enzyme activity compared with that of the wild-type enzyme
Y99F
7% of the enzyme activity compared with that of the wild-type enzyme
E366A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
Y194A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
Y99A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
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
D184A
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
Q187A
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
R380A
site-directed mutagenesis, the mutation has no effect on kynurenine hydroxylation, suggesting that residue R380 does not play a major role in substrate recognition
Y185P
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
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
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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
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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
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additional information
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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
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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
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additional information
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pathogenic mutant BCG183 is obtained by screening the T-DNA insertion library of Botrytis cinerea. Semiquantitative RT-PCR is used to determine the expression levels of the T-DNA insert gene and confirm the presence of the mutant gene in the mutant BCG183. The pathogenicity-related gene BcKMO, which encodes kynurenine 3-monooxygenase (KMO), is isolated and identified via thermal asymmetric interlaced PCR, bioinformatics analyses, and KMO activity measurement. The mutant BCG183 grows slowly, does not produce conidia and sclerotia, has slender hyphae, and presents enhanced pathogenicity. The phenotype and pathogenicity of the BcKMO complementing mutant (BCG183/BcKMO) are similar to those of the wild-type strain. The wild-type and BCG183/BcKMO colonies are taupe-colored and produce large amounts of sclerotia, while mutant the BCG183 colonies are gray and do not produce sclerotia. The BCG183 mycelia are white and slender with shorter transverse septa, when compared with wild-type and BCG183/BcKMO mycelia. The BCG183 mutant do not produce conidia, whereas the wild-type and BCG183/BcKMO strains do. The BCG183 mutant exhibits remarkably higher sensitivity to NaCl and KCl, when compared with the wild-type. Also, the sensitivity of the mutant BCG183 to fluconazole, Congo Red, menadione, and H2O2 is significantly weaker, when compared with that of the wild-type and BCG183/BcKMO strains. The BCG183 mutant sensitivity to SQ22536 and U0126, inhibitors of the cAMP and MAPK signaling pathways, is significantly weaker, when compared with that of wild-type and BCG183/BcKMO strains. The cAMP content in the mutant BCG183 is significantly lower, when compared with that in wild-type and BCG183/BcKMO strains
additional information
Botrytis cinerea BC22
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pathogenic mutant BCG183 is obtained by screening the T-DNA insertion library of Botrytis cinerea. Semiquantitative RT-PCR is used to determine the expression levels of the T-DNA insert gene and confirm the presence of the mutant gene in the mutant BCG183. The pathogenicity-related gene BcKMO, which encodes kynurenine 3-monooxygenase (KMO), is isolated and identified via thermal asymmetric interlaced PCR, bioinformatics analyses, and KMO activity measurement. The mutant BCG183 grows slowly, does not produce conidia and sclerotia, has slender hyphae, and presents enhanced pathogenicity. The phenotype and pathogenicity of the BcKMO complementing mutant (BCG183/BcKMO) are similar to those of the wild-type strain. The wild-type and BCG183/BcKMO colonies are taupe-colored and produce large amounts of sclerotia, while mutant the BCG183 colonies are gray and do not produce sclerotia. The BCG183 mycelia are white and slender with shorter transverse septa, when compared with wild-type and BCG183/BcKMO mycelia. The BCG183 mutant do not produce conidia, whereas the wild-type and BCG183/BcKMO strains do. The BCG183 mutant exhibits remarkably higher sensitivity to NaCl and KCl, when compared with the wild-type. Also, the sensitivity of the mutant BCG183 to fluconazole, Congo Red, menadione, and H2O2 is significantly weaker, when compared with that of the wild-type and BCG183/BcKMO strains. The BCG183 mutant sensitivity to SQ22536 and U0126, inhibitors of the cAMP and MAPK signaling pathways, is significantly weaker, when compared with that of wild-type and BCG183/BcKMO strains. The cAMP content in the mutant BCG183 is significantly lower, when compared with that in wild-type and BCG183/BcKMO strains
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additional information
cinnabar null cn3 line analysis, the aspect ratio and Feret's diameter are increased in cn3 flies compared to Canton S control flies, reflecting mitochondrial elongation arising from KMO deficiency. Mitochondrial respiratory capacity and locomotor activity are decreased in cn flies, independent from 3-hydroxy-L-kynurenine (3-HK) synthesis. Gene cinnabar silencing with about 80% knockdown resulting in an elongation of the mitochondrial network compared with cells treated with the control dsRNAi construct, phenotype overview. Drp1 upregulation reverses climbing phenotype of cn-deficient flies
additional information
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cinnabar null cn3 line analysis, the aspect ratio and Feret's diameter are increased in cn3 flies compared to Canton S control flies, reflecting mitochondrial elongation arising from KMO deficiency. Mitochondrial respiratory capacity and locomotor activity are decreased in cn flies, independent from 3-hydroxy-L-kynurenine (3-HK) synthesis. Gene cinnabar silencing with about 80% knockdown resulting in an elongation of the mitochondrial network compared with cells treated with the control dsRNAi construct, phenotype overview. Drp1 upregulation reverses climbing phenotype of cn-deficient flies
additional information
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cinnabar null cn3 line analysis, the aspect ratio and Feret's diameter are increased in cn3 flies compared to Canton S control flies, reflecting mitochondrial elongation arising from KMO deficiency. Mitochondrial respiratory capacity and locomotor activity are decreased in cn flies, independent from 3-hydroxy-L-kynurenine (3-HK) synthesis. Gene cinnabar silencing with about 80% knockdown resulting in an elongation of the mitochondrial network compared with cells treated with the control dsRNAi construct, phenotype overview. Drp1 upregulation reverses climbing phenotype of cn-deficient flies
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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
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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
generation of a C-terminal domain truncated human KMO whose membrane targeting sequence in its C-terminal domain is suggested to be an essential part of its catalysis
additional information
analysis of kynurenine pathway (KP) metabolism in the brain after depleting microglial cells pharmacologically with the colony stimulating factor 1 receptor inhibitor PLX5622. Young adult mice are fed PLX5622 for 21 days and are euthanized either on the next day or after receiving normal chow for an additional21 days. Expression of microglial marker genes is dramatically reduced on day 22 but has fully recovered by day 43. In both groups, PLX5622 treatment fails to affect Kmo expression, KMO activity or tissue levels of 3-HK and KYNA in the brain. In a parallel experiment, PLX5622 treatment also does not reduce KMO activity, 3-HK and KYNA in the brain of R6/2 mice (a model of HD with activated microglia). With freshly isolated mouse cells ex vivo, KMO is found only in microglia and neurons but not in astrocytes. Neurons contain a large proportion of functional KMO in the adult mouse brain under both physiological and pathological conditions
additional information
generation of enzyme knockout mutant mice, which are engineered on a C57BL/6 background to lack KMO activity by insertion of a polyA transcription stop motif before exon 5 of the Kmo gene (Kmotm1a(KOMP)Wtsi). Kmonull mice are unable to form 3-hydroxykynurenine. Kmonull mice are protected against AKI after renal ischemia-reperfusion injury (IRI). KMO deletion inhibits neutrophil infiltration in the kidney following IRI. Mutant mouse phenotype, detailed overview
additional information
the KMO expression is effectively inhibited using small interfering RNA (siRNA) and short hairpin RNA (shRNA), respectively. HSV-1 replication is significantly enhanced in KMO-knockdown cells compared to wild-type cells. Overexpression of catalytically inactive KMO catalytic residues mutants has no significant inhibition effect on HSV-1 infection
additional information
Mus musculus C57BL/6N x C57BL/6J
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generation of enzyme knockout mutant mice, which are engineered on a C57BL/6 background to lack KMO activity by insertion of a polyA transcription stop motif before exon 5 of the Kmo gene (Kmotm1a(KOMP)Wtsi). Kmonull mice are unable to form 3-hydroxykynurenine. Kmonull mice are protected against AKI after renal ischemia-reperfusion injury (IRI). KMO deletion inhibits neutrophil infiltration in the kidney following IRI. Mutant mouse phenotype, detailed overview
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additional information
generation of a C-terminal domain truncated human KMO whose membrane targeting sequence in its C-terminal domain is suggested to be an essential part of its catalysis
additional information
generation of a C-terminal domain truncated human KMO whose membrane targeting sequence in its C-terminal domain is suggested to be an essential part of its catalysis
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
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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
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construction of mutants lacking functional enzyme via RNA interference, RNAi, the gene is unlinked to known eye-color mutants