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

Reaction

L-kynurenine
+
NADPH
+
H+
+
O2
=
3-hydroxy-L-kynurenine
+
NADP+
+
H2O

Synonyms

Bna4, cinnabar, EC 1.14.1.2, EC 1.99.1.5, K3H, KMO, KYN-OHase, kynurenine 3-hydroxylase, kynurenine hydroxylase, kynurenine monooxygenase, L-kynurenine 3-monooxygenase, L-kynurenine,NADPH2:oxygen oxidoreductase (3-hydroxylating), L-kynurenine-3-hydroxylase, More, oxygenase, kynurenine 3-mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.9 kynurenine 3-monooxygenase

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.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 enzyme–L-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
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