We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
The taxonomic range for the selected organisms is: Aedes aegypti The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aspartate aminotransferase, mitochondrial aspartate aminotransferase, kat ii, kat i, kynurenine aminotransferase ii, aadat, kat-i, kat-ii, kynurenine aminotransferase i, kynurenine-oxoglutarate transaminase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aminotransferase, kynurenine
-
-
-
-
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
-
-
-
-
kynurenine transaminase (cyclizing)
-
-
-
-
L-kynurenine aminotransferase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
amino group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-kynurenine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-alanine + 2-oxobutanoate
pyruvate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
Q95VY4
-
-
-
?
L-cysteine + 2-oxobutanoate
? + 2-aminobutanoate
Q95VY4
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
Q95VY4
25% of activity with pyruvate
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Q95VY4
31% of activity with pyruvate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
Q95VY4
90% of activity with pyruvate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
Q95VY4
best amino acceptor
-
?
L-leucine + 2-oxobutanoate
alpha-ketoleucine + 2-aminobutanoate
Q95VY4
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-serine + 2-oxobutanoate
3-hydroxy-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxal 5'-phosphate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
92.7
2-aminobutanoate
Q95VY4
pH 8.5, 45°C
246
L-alanine
Q95VY4
pH 8.5, 45°C
6.1
L-asparagine
Q95VY4
pH 8.5, 45°C
1.3
L-cysteine
Q95VY4
pH 8.5, 45°C
3.8
L-glutamine
Q95VY4
pH 8.5, 45°C
1.5
L-histidine
Q95VY4
pH 8.5, 45°C
4.3
L-kynurenine
Q95VY4
pH 8.5, 45°C
34.5
L-leucine
Q95VY4
pH 8.5, 45°C
1.4
L-methionine
Q95VY4
pH 8.5, 45°C
3.5
L-phenylalanine
Q95VY4
pH 8.5, 45°C
32.7
L-serine
Q95VY4
pH 8.5, 45°C
12.9
L-tryptophan
Q95VY4
pH 8.5, 45°C
0.9
L-tyrosine
Q95VY4
pH 8.5, 45°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
317
2-aminobutanoate
Q95VY4
pH 8.5, 45°C
1540
L-alanine
Q95VY4
pH 8.5, 45°C
230
L-asparagine
Q95VY4
pH 8.5, 45°C
206
L-cysteine
Q95VY4
pH 8.5, 45°C
561
L-glutamine
Q95VY4
pH 8.5, 45°C
168
L-histidine
Q95VY4
pH 8.5, 45°C
172
L-kynurenine
Q95VY4
pH 8.5, 45°C
758
L-leucine
Q95VY4
pH 8.5, 45°C
163
L-methionine
Q95VY4
pH 8.5, 45°C
283
L-phenylalanine
Q95VY4
pH 8.5, 45°C
345
L-serine
Q95VY4
pH 8.5, 45°C
283
L-tryptophan
Q95VY4
pH 8.5, 45°C
139
L-tyrosine
Q95VY4
pH 8.5, 45°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10
Q95VY4
optima at pH 8.5 and 10.0
8.5
Q95VY4
optima at pH 8.5 and 10.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
60
Q95VY4
recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Q95VY4
deduced amino acid sequence contains a mitochondrial leader sequence
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KAT_AEDAE
477
0
53506
Swiss-Prot
Mitochondrion (Reliability: 3 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
48000
Q95VY4
2 * 48000, truncated recombinant enzyme, SDS-PAGE
53000
Q95VY4
x * 53000, SDS-PAGE
53490
Q95VY4
x * 53490, deduced from nucleotide sequence
97000
Q95VY4
truncated recombinant enzyme, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
Q95VY4
2 * 48000, truncated recombinant enzyme, SDS-PAGE
dimer
-
crystallization data
?
Q95VY4
x * 53000, SDS-PAGE
?
Q95VY4
x * 53490, deduced from nucleotide sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
truncated recombinant enzyme, DEAE-Sepharose, native PAGE
Q95VY4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression of full length enzyme and truncated version lacking the mitochondrial leader sequence in Sf9 insect cells
Q95VY4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fang, J.; Han, Q.; Li, J.
Isolation, characterization, and functional expression of kynurenine aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1)
Insect Biochem. Mol. Biol.
32
943-950
2002
Aedes aegypti (Q95VY4)
brenda
Han, Q.; Gao, Y.G.; Robinson, H.; Ding, H.; Wilson, S.; Li, J.
Crystal structures of Aedes aegypti kynurenine aminotransferase
FEBS J.
272
2198-2206
2005
Aedes aegypti
brenda
Han, Q.; Li, J.
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
FEBS Lett.
577
381-385
2004
Aedes aegypti (Q95VY4)
brenda
Han, Q.; Gao, Y.G.; Robinson, H.; Li, J.
Structural insight into the mechanism of substrate specificity of Aedes kynurenine aminotransferase
Biochemistry
47
1622-1630
2008
Aedes aegypti, Homo sapiens
brenda
Transporter Classification Database (TCDB):
9.A.70.1.1