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Literature summary for 1.14.13.9 extracted from

  • Han, Q.; Calvo, E.; Marinotti, O.; Fang, J.; Rizzi, M.; James, A.A.; Li, J.
    Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti (2003), Insect Mol. Biol., 12, 483-490.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene kh, DNA and amino acid sequence analysis of wild-type and mutant genes, expression in Spodoptera frugiperda Sf9 cells as His-tagged, soluble protein via the baculovirus infection system Aedes aegypti

Protein Variants

Protein Variants Comment Organism
additional information an inactive mutant lacks 162 nucleotides near the 3'-end of the mutant allele, the in-frame deletion results in loss of 54 amino acids leading to loss of enzyme activity and white eyes Aedes aegypti

Inhibitors

Inhibitors Comment Organism Structure
chloride mixed-type inhibition Aedes aegypti
pyridoxal 5'-phosphate noncompetitive Aedes aegypti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Aedes aegypti
0.82
-
NADPH recombinant enzyme, pH 7.5, 37°C Aedes aegypti
0.89
-
L-kynurenine recombinant enzyme, pH 7.5, 37°C Aedes aegypti
5.17
-
NADH recombinant enzyme, pH 7.5, 37°C Aedes aegypti

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme is hydrophobis and contains 2 transmembrane segments Aedes aegypti 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE Aedes aegypti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-kynurenine + NADPH + O2 Aedes aegypti enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?
L-kynurenine + NADPH + O2 Aedes aegypti Liverpool enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Aedes aegypti Q86PM2 yellow fever mosquito, black-eyed Liverpool strain
-
Aedes aegypti Liverpool Q86PM2 yellow fever mosquito, black-eyed Liverpool strain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from soluble fraction of Sf9 insect cells by nickel affinity chromatography Aedes aegypti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + NADH + H+ + O2
-
Aedes aegypti 3-hydroxy-L-kynurenine + NAD+ + H2O
-
?
L-kynurenine + NADH + H+ + O2
-
Aedes aegypti Liverpool 3-hydroxy-L-kynurenine + NAD+ + H2O
-
?
L-kynurenine + NADPH + O2
-
Aedes aegypti 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?
L-kynurenine + NADPH + O2 enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos Aedes aegypti 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?
L-kynurenine + NADPH + O2
-
Aedes aegypti Liverpool 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?
L-kynurenine + NADPH + O2 enzyme has a key role in L-tryptophan catabolism and in synthesis of ommochrome pigments in the eyes of the mosquitos Aedes aegypti Liverpool 3-hydroxy-L-kynurenine + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
? x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE Aedes aegypti

Synonyms

Synonyms Comment Organism
KMO
-
Aedes aegypti
kynurenine hydroxylase
-
Aedes aegypti
kynurenine monooxygenase
-
Aedes aegypti
More the enzyme is a member of the glutathione reductase structural family Aedes aegypti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Aedes aegypti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.85
-
NADH recombinant enzyme, pH 7.5, 37°C Aedes aegypti
1.88
-
L-kynurenine recombinant enzyme, pH 7.5, 37°C Aedes aegypti
2.03
-
NADPH recombinant enzyme, pH 7.5, 37°C Aedes aegypti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Aedes aegypti

Cofactor

Cofactor Comment Organism Structure
FAD consensus domain sequence, probably FAD-containing Aedes aegypti
NADH low activity, ineffective cofactor Aedes aegypti
NADPH highly preferred cofactor with respect to NADH Aedes aegypti

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.17
-
pyridoxal 5'-phosphate recombinant enzyme, with respect to NADPH, pH 7.5, 37°C Aedes aegypti
0.27
-
pyridoxal 5'-phosphate recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C Aedes aegypti
11.2
-
chloride recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C Aedes aegypti
24.5
-
chloride recombinant enzyme, with respect to NADPH, pH 7.5, 37°C Aedes aegypti