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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

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

     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

Engineering

Engineering on EC 1.14.13.9 - kynurenine 3-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E366Q
2% of the enzyme activity compared with that of the wild-type enzyme
M367A
2% of the enzyme activity compared with that of the wild-type enzyme
M367L
13% of the enzyme activity compared with that of the wild-type enzyme
N363A
28% of the enzyme activity compared with that of the wild-type enzyme
N363D
no activity detected
N465A
about 80% of the enzyme activity compared with that of the wild-type enzyme
R85A
no activity detected
R85K
1% of the enzyme activity compared with that of the wild-type enzyme
Y398A
1% of the enzyme activity compared with that of the wild-type enzyme
Y398F
1% of the enzyme activity compared with that of the wild-type enzyme
Y99A
no activity detected
Y99F
7% of the enzyme activity compared with that of the wild-type enzyme
E366A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
Y194A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
Y99A
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
E372A
about 15% of the enzyme activity compared with that of the wild-type enzyme
E372Q
about 5% of the enzyme activity compared with that of the wild-type enzyme
M373A
no activity detected
M373L
about 60% of the enzyme activity compared with that of the wild-type enzyme
N369A
about 65% of the enzyme activity compared with that of the wild-type enzyme
N369D
no activity detected
Q424A
mutation does not greatly affect enzyme activity. Ro 61-8048 shows no inhibition to the pfKMO mutant enzyme
R84A
no activity detected
Y404A
no activity detected
Y404F
about 40% of the enzyme activity compared with that of the wild-type enzyme
Y98A
no activity detected
Y98F
about 1% of the enzyme activity compared with that of the wild-type enzyme
D184A
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
Q187A
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
R380A
site-directed mutagenesis, the mutation has no effect on kynurenine hydroxylation, suggesting that residue R380 does not play a major role in substrate recognition
Y185P
site-directed mutagenesis, the mutation weakens the beta-sheet dimer interface of the enzyme
additional information