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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Localization
Localization on EC 1.14.13.9 - kynurenine 3-monooxygenase
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enzyme is hydrophobis and contains 2 transmembrane segments
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enzyme is hydrophobis and contains 2 transmembrane segments
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specifically, KMO is localised to the outer membrane of mitochondria where it associates with the lipid membrane using C-terminal transmembrane domains, which are also crucial for the catalytic activity of KMO
specifically, KMO is localised to the outer membrane of mitochondria where it associates with the lipid membrane using C-terminal transmembrane domains, which are also crucial for the catalytic activity of KMO
specifically, KMO is localised to the outer membrane of mitochondria where it associates with the lipid membrane using C-terminal transmembrane domains, which are also crucial for the catalytic activity of KMO
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
KMO is localized to the outer mitochondrial membrane in eukaryotic organisms
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KMO is localized to the outer mitochondrial membrane in eukaryotic organisms
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KMO has two transmembrane domains, KMO is actually a single-pass transmembrane protein, with the other transmembrane domain lying laterally along the membrane, where it forms part of the ligand-binding pocket. Membrane-bound structure, overview
KMO has two transmembrane domains, KMO is actually a single-pass transmembrane protein, with the other transmembrane domain lying laterally along the membrane, where it forms part of the ligand-binding pocket. Membrane-bound structure, overview
the C-terminal region functions as a mitochondrial targeting signal
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