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
-
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
- 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
Advanced search results
Crystallization
Crystallization on EC 1.14.13.9 - kynurenine 3-monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
purified full-length structure of KMO in its membrane-embedded form, complexed with 2-(benzyloxy)-5-[5-(4-chloro-3-fluorophenyl)-4-methyl-1H-pyrazol-1-yl]benzoic acid and 4-chloro-2-([5-chloro-2-(5-methoxy-1,3-dihydro-2H-isoindol-2-yl)-1,3-thiazole-4-carbonyl](methyl)amino)-5-fluorobenzoic acid at 3.0 A resolution
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 enzymeL-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
purified full-length structure of KMO in its membrane-embedded form complexed with inhibitors 2-(benzyloxy)-5-[5-(4-chloro-3-fluorophenyl)-4-methyl-1H-pyrazol-1-yl]benzoic acid or 4-chloro-2-([5-chloro-2-(5-methoxy-1,3-dihydro-2H-isoindol-2-yl)-1,3-thiazole-4-carbonyl](methyl)amino)-5-fluorobenzoic acid, sitting drop vapour diffusion method, mixing of enzyme in lipidic cubic phase formed by mixing a 9:1 monoolein:cholesterol molten lipid mixture and inhibitors, with reservoir solution containing 0.04 M Tris-Cl, pH 7.0, 0.06 M Bis-Tris, pH 6.5, 0.3-0.51 M lithium sulfate, and 34-45% PEG 400 for 2-(benzyloxy)-5-[5-(4-chloro-3-fluorophenyl)-4-methyl-1H-pyrazol-1-yl]benzoic acid and containing 0.04-0.05 M sodium citrate, pH 6.5, or 0.04 M Bis-Tris pH 6.5, 0.05-0.06 M Tris-Cl, pH 7.0, 0.12-0.43 M lithium sulfate, and 34-46% PEG 400 for 4-chloro-2-([5-chloro-2-(5-methoxy-1,3-dihydro-2H-isoindol-2-yl)-1,3-thiazole-4-carbonyl](methyl)amino)-5-fluorobenzoic acid, in a 2:3 ratio at 17°C for 1-3 days, X-ray diffraction structure determination and analysis at 3.0 A resolution
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