Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase and Organism(s) Aedes aegypti and UniProt Accession Q95VY4

for references in articles please use BRENDA:EC2.6.1.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.7 kynurenine-oxoglutarate transaminase
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aedes aegypti
UNIPROT: Q95VY4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminotransferase, kynurenine
-
-
-
-
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
-
-
-
-
kynurenine transaminase (cyclizing)
-
-
-
-
L-kynurenine aminotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-38-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine + 2-oxobutanoate
pyruvate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-cysteine + 2-oxobutanoate
? + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
Q95VY4
25% of activity with pyruvate
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Q95VY4
31% of activity with pyruvate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
Q95VY4
90% of activity with pyruvate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Q95VY4
best amino acceptor
-
?
L-leucine + 2-oxobutanoate
alpha-ketoleucine + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-serine + 2-oxobutanoate
3-hydroxy-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
Q95VY4
optima at pH 8.5 and 10.0
8.5
Q95VY4
optima at pH 8.5 and 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
Q95VY4
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Q95VY4
deduced amino acid sequence contains a mitochondrial leader sequence
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
Q95VY4
2 * 48000, truncated recombinant enzyme, SDS-PAGE
dimer
-
crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
truncated recombinant enzyme, DEAE-Sepharose, native PAGE
Q95VY4
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of full length enzyme and truncated version lacking the mitochondrial leader sequence in Sf9 insect cells
Q95VY4
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team