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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Cloned
Cloned on EC 1.14.13.9 - kynurenine 3-monooxygenase
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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 BC1G_07455, DNA and amino acid sequence determination and analysis of wild-type and enzyme mutant gene, phylogenetic analysis and tree, recombinant expression of eGFP-tagged wild-type enzyme in Botrytis cinerea mutant strain BCG183 protoplasts, quantitative real-time PCR enzyme expression analysis
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gene cinnabar, quantitative enzyme expression analysis, gene cinnabar genetically interacts with the Parkinson's disease associated genes Pink1 and parkin, as well as the mitochondrial fission gene Drp1, implicating KMO in mitochondrial dynamics and mitophagy, mechanisms which govern the maintenance of a healthy mitochondrial network. Overexpression of human KMO in HEK-293T cells. Cinnabar genetically interacts with Pink1 and parkin in a mechanism independent of KP metabolism, 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 kmo, KMO is an interferon-dependent gene, quantitative RT-PCR enzyme expression analysis
gene kmo, quantitative reverse transcription-PCR enzyme expression analysis
gene kmo, quantitative RT-PCR enzyme expression analysis
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
sequence comparisons, recombinant expression of GST-tagged full-length KMO (1-478) from baculovirus vector containing a thrombin cleavage site inserted between GST and the N-terminus of KMO, and a TEV site followed by a FLAG tag at the C-terminus with the Bac-to-Bac Baculovirus system in Spodoptera frugiperda (Sf9) cells. Recombinant enzyme expression in HEK-293 cells