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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KM Value
KM Value on EC 1.14.13.9 - kynurenine 3-monooxygenase
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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
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steady-state kinetics and ligand perturbation of flavin fluorescence, overview
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additional information
additional information
evaluation of the proton inventory resulting from medium effects or specific transition states, first-order rate constants are fit to variations of the Kresge (Gross-Butler) equation, kinetic isotope effects, oxidative half-reaction in the presence of ring perdeutero-L-Kyn, stopped-flow spectrophotometric measurements, kinetics, overview. The decay of the C4a-hydroperoxyflavin results in the regeneration of the oxidized flavin. The final step of the oxidative half-reaction is then the release of 3-hydroxy-L-kynurenine from the active site which is observed as a perturbation of the oxidized absorption spectrum
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additional information
additional information
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evaluation of the proton inventory resulting from medium effects or specific transition states, first-order rate constants are fit to variations of the Kresge (Gross-Butler) equation, kinetic isotope effects, oxidative half-reaction in the presence of ring perdeutero-L-Kyn, stopped-flow spectrophotometric measurements, kinetics, overview. The decay of the C4a-hydroperoxyflavin results in the regeneration of the oxidized flavin. The final step of the oxidative half-reaction is then the release of 3-hydroxy-L-kynurenine from the active site which is observed as a perturbation of the oxidized absorption spectrum
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