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Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase and Organism(s) Homo sapiens and UniProt Accession Q8N5Z0

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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.
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This record set is specific for:
Homo sapiens
UNIPROT: Q8N5Z0
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
KAT I
isoform
KAT II
KAT-II
isoform
kynurenine aminotransferase
-
kynurenine aminotransferase 2
-
kynurenine aminotransferase II
-
kynurenine/alpha-aminoadipate aminotransferase
-
aminotransferase, kynurenine
-
-
-
-
KAT I
KAT II
KAT III
KAT IV
KAT-I
KAT-II
-
isoform
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
kynurenine aminotransferase I
kynurenine aminotransferase II
-
-
kynurenine aminotransferase III
-
kynurenine aminotransferase-1
-
kynurenine aminotransferase-I
kynurenine transaminase (cyclizing)
-
-
-
-
L-kynurenine aminotransferase
-
-
-
-
type II 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
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoadipate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxocaproate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxovalerate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 3-methyl-2-oxobutanoate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 4-methyl-2-oxopentanoate
?
show the reaction diagram
-
-
-
?
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
glyoxylate shows a relatively low affinity for KAT II
-
-
?
L-kynurenine + hydroxyphenylpyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + indo-3-pyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + mercaptopyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + oxaloacetate
?
show the reaction diagram
-
-
-
?
L-kynurenine + phenylpyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + pyruvate
?
show the reaction diagram
-
-
-
?
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxoisocaproate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-leucine
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
-
-
-
-
?
L-kynurenine + mercaptopyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine
show the reaction diagram
-
-
-
-
?
L-kynurenine + oxaloacetate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminosuccinate
show the reaction diagram
-
-
-
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-kynurenine + pyruvate
4-(2-aminophenyl)-2,4-dioxobutanoic acid + L-alanine
show the reaction diagram
-
-
-
-
ir
L-kynurenine + pyruvate
4-(2-aminophenyl)2,4-dioxobutanoate + L-alanine
show the reaction diagram
-
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
L-leucine + 2-oxobutanoate
2-oxoisocaproate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-3-phenylpropanoic acid
-
(2S)-2-(5,6-dichloro-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)-3-phenylpropanoic acid
reversible inhibitor
(2S)-2-amino-4-[4-(ethylsulfonyl)phenyl]-4-oxobutanoic acid
reversible inhibitor
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
(3S)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
-
(5Z)-5-[3-(4-oxo-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-7-yl)benzylidene]-1,3-thiazolidine-2,4-dione
reversible inhibitor
-
(6R)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(S)-(-)-9-(4-aminopiperazin-1-yl)-8-fluoro-3-methyl-6-oxo-2,3-dihydro-6H-1-oxa-3a-azaphenalene-5-carboxylic acid
BFF-122
3,5-difluoro-N-[5-(1-phenylcyclopropyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
3,5-difluoro-N-{5-[(2R)-2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3,5-difluoro-N-{5-[(2S)-2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3,5-difluoro-N-{5-[2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3-hydroxykynurenine
less than 35% inhibition at 5 mM
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)benzenesulfonamide
reversible inhibitor
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethylbenzenesulfonamide
reversible inhibitor
4-chloro-N-(pyrrolidin-3-yl)-2-(trifluoromethyl)benzenesulfonamide
-
aminoadipate
less than 35% inhibition at 5 mM
BFF-122
BFF-816
carbenoxolone
highly selective and competitive inhibitor for isoform KAT2
estradiol disulfate
Estrone sulfate
weak inhibitor
glycyrrhetinic acid
highly selective and competitive inhibitor for isoform KAT2
glycyrrhizic acid
highly selective and competitive inhibitor for isoform KAT2
L-2-aminoadipate
-
L-asparagine
less than 35% inhibition at 5 mM
L-cysteine
less than 35% inhibition at 5 mM
L-glutamate
less than 35% inhibition at 5 mM
L-histidine
less than 35% inhibition at 5 mM
L-lysine
less than 35% inhibition at 5 mM
L-phenylalanine
less than 35% inhibition at 5 mM
N-(3-chloro-4-methylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
N-benzyl-1-[6-methyl-5-(oxan-4-yl)-7-oxo-6,7-dihydro[1,3]thiazolo[5,4-d]pyrimidin-2-yl]-D-prolinamide
reversible inhibitor
N-[5-(cyclopentylmethyl)-1,3,4-oxadiazol-2-yl]benzenesulfonamide
-
NS-1502
reversible inhibitor
PF-04859989
S-4-(ethylsulfonyl)benzoyl-L-alanine
(R)-2-amino-4-(4-(ethylsulfonyl)phenyl)-4-oxobutanoic acid
-
71% inhibition at 1 mM, 63% inhibition at 0.1 mM, poor substrate that undergo slow transamination, KM-value 4.5 mM, Kcat-value 0.15 1/sec, pH 7.5, 25°C
3-(2-carboxyethyl)-5-chloro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
-
3-hydroxykynurenine
-
5 mM decreases KAT II activity
3-indolepropionic acid
5-(2-(3-chlorophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-(2-(4-bromophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-(2-(4-chlorophenyl) hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-bromo-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
-
-
6-ethoxy-5-(2-(4-iodophenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-5-(2-(4-methoxyphenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-5-(2-(4-nitrophenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-6-oxo-5-(2-p-tolylhydrazono)hexanoic acid
-
-
aminoadipate
-
5 mM decreases KAT II activity
Aminooxyacetate
-
aminooxyphenylpropionic acid
-
BFF-122
irreversible inhibitor
BFF-816
reversible inhibitor
cysteine
-
-
cysteine sulfinate
-
poor substrate that undergoes slow transamination, KM-value 12.3 mM, pH 7.5, 25°C
DL-indole-3-lactic acid
estradiol disulfate
strong reversible inhibitor
glutamine
indole-3-acetic acid
-
Indole-3-propionic acid
-
-
Indole-3-pyruvate
-
5 mM, complete inhibition
indole-3-pyruvic acid
-
L- glutamate
-
5 mM decreases KAT II activity
L-asparagine
-
5 mM decreases KAT II activity
L-aspartate
-
specific inhibitor of KAT IV
L-cysteine
L-glutamine
-
inhibition of KAT I activity at 2 mM
L-histidine
-
5 mM decreases KAT II activity
L-lysine
-
5 mM decreases KAT II activity
L-phenylalanine
L-tryptophan
NS-1502
reversible inhibitor
PF-04859989
irreversible inhibitor
S-4-(ethylsulfonyl)benzoyl-L-alanine
reversible inhibitor
trans-3-indolacrylic acid
-
Tris amine
-
the commonly used buffer for KAT I assays greatly inhibits KAT I around neutral pH conditions, but shows no inhibition at basic pH condition
tryptophan
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tryptophan
-
2 mM, 84% increase in activity of heart KAT at pH 8.0
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
2-oxo-4-methylthiobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
20.9
2-oxoadipate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
12.7
2-oxobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.5
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.2
2-oxoglutarate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.4
2-oxovalerate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
12.9 - 14.2
3-methyl-2-oxobutanoate
3.3
4-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
18
glyoxylate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.5
hydroxyphenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.4
indo-3-pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.68 - 4.7
L-kynurenine
2.8
Mercaptopyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
16.8
oxaloacetate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.8
phenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
9.7
pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
21.3
2-aminobutanoate
-
pH 7.5, 45°C
3
2-oxobutanoate
-
pH 7.5, 45°C
0.62 - 1.2
2-oxoglutarate
1
2-oxoisocaproate
-
pH 7.5, 45°C
1.5
glyoxylate
-
pH 7.5, 45°C
23.1
L-asparagine
-
pH 7.5, 45°C
0.7
L-cysteine
-
pH 7.5, 45°C
2.8
L-glutamine
-
pH 7.5, 45°C
5.4
L-histidine
-
pH 7.5, 45°C
0.96 - 27
L-kynurenine
7.6
L-leucine
-
pH 7.5, 45°C
6.4
L-methionine
-
pH 7.5, 45°C
1.7
L-phenylalanine
-
pH 7.5, 45°C
1.2
L-tryptophan
-
pH 7.5, 45°C
3.2
L-tyrosine
-
pH 7.5, 45°C
2.5
Mercaptopyruvate
-
pH 7.5, 45°C
4.2
oxaloacetate
-
pH 7.5, 45°C
0.8
phenylpyruvate
-
pH 7.5, 45°C
1.15 - 12.1
pyruvate
additional information
additional information
-
isoform KAT I, vitreous body, 0.57 pM/g wet tissue/hour, retina, 3.42, isoform KAT II, vitreous body, 2.56 pM/g wet tissue/hour, retina 10.75
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.27
2-oxo-4-methylthiobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
4.84
2-oxoadipate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.49
2-oxobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
4.83
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
7.67
2-oxoglutarate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
2.66
2-oxovalerate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.92
3-methyl-2-oxobutanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.92
3-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
2.51
4-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.64
glyoxylate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.39
hydroxyphenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.49
indo-3-pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
4.6 - 9.76
L-kynurenine
3.59
Mercaptopyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.065
oxaloacetate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
4.73
phenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.36
pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
38.3
2-aminobutanoate
-
pH 7.5, 45°C
234
2-oxobutanoate
-
pH 7.5, 45°C
296
2-oxoisocaproate
-
pH 7.5, 45°C
263
glyoxylate
-
pH 7.5, 45°C
14.4
L-asparagine
-
pH 7.5, 45°C
9.6
L-cysteine
-
pH 7.5, 45°C
440
L-glutamine
-
pH 7.5, 45°C
143
L-histidine
-
pH 7.5, 45°C
1.8 - 201
L-kynurenine
339
L-leucine
-
pH 7.5, 45°C
215
L-methionine
-
pH 7.5, 45°C
91
L-phenylalanine
-
pH 7.5, 45°C
43.1
L-tryptophan
-
pH 7.5, 45°C
91
L-tyrosine
-
pH 7.5, 45°C
234
Mercaptopyruvate
-
pH 7.5, 45°C
143
oxaloacetate
-
pH 7.5, 45°C
110
phenylpyruvate
-
pH 7.5, 45°C
29
pyruvate
-
pH 7.5, 45°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.75
2-oxo-4-methylthiobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.23
2-oxoadipate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.27
2-oxobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.13
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
6.24
2-oxoglutarate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.78
2-oxovalerate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.45
3-hydroxy-DL-kynurenine
pH and temperature not specified in the publication
0.07
3-methyl-2-oxobutanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.065
3-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.76
4-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.2
glyoxylate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.27
hydroxyphenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.08
indo-3-pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
2.1 - 6.8
L-kynurenine
1.23
Mercaptopyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.09
oxaloacetate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
2.62
phenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.04
pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.713
L-kynurenine
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
cysteine sulfinate
-
17.2 mM dissociation constant for dissociation of the inhibitor from the enzyme substrate complex, pH 7.5, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.315
(2R)-2-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-3-phenylpropanoic acid
Homo sapiens
at pH 7.4 and 37°C
0.000015 - 0.00003
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
0.000004 - 0.000005
(3S)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
0.0045
(6R)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.1
(6R)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0024
(6R)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.044
(6R)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0749
(6S)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0155
(6S)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0965
(6S)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.097
(6S)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00091
(S)-(-)-9-(4-aminopiperazin-1-yl)-8-fluoro-3-methyl-6-oxo-2,3-dihydro-6H-1-oxa-3a-azaphenalene-5-carboxylic acid
Homo sapiens
0.0015 mM or the two enantiomers, pH 8.0, 37°C
0.0738
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)benzenesulfonamide
Homo sapiens
at pH 7.4 and 37°C
0.1128
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethylbenzenesulfonamide
Homo sapiens
at pH 7.4 and 37°C
0.0039
carbenoxolone
Homo sapiens
isoform KAT2, at pH 9.5 and 37°C
0.0263
estradiol disulfate
0.00696
glycyrrhetinic acid
Homo sapiens
isoform KAT2, at pH 9.5 and 37°C
0.00451
glycyrrhizic acid
Homo sapiens
isoform KAT2, at pH 9.5 and 37°C
0.00081
N-(3-chloro-4-methylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.008
N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.293
3-(2-carboxyethyl)-5-chloro-1H-indole-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.666
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
5-(2-(3-chlorophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.021
5-(2-(4-bromophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
5-(2-(4-chlorophenyl) hydrazono)-6-ethoxy-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.271
5-bromo-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.034
6-ethoxy-5-(2-(4-iodophenyl)hydrazono)-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.043
6-ethoxy-5-(2-(4-methoxyphenyl)hydrazono)-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.179
6-ethoxy-5-(2-(4-nitrophenyl)hydrazono)-6-oxohexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.033
6-ethoxy-6-oxo-5-(2-p-tolylhydrazono)hexanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0131
Aminooxyacetate
Homo sapiens
at pH 8.0 and 45°C
0.0057
aminooxyphenylpropionic acid
Homo sapiens
at pH 8.0 and 45°C
0.002
cysteine sulfinate
Homo sapiens
-
pH 7.5, 25°C
0.2915
estradiol disulfate
Homo sapiens
isoform KAT-I, at pH 7.4 and 37°C
0.14
Indole-3-propionic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
3
L-phenylalanine
Homo sapiens
at pH 8.0 and 45°C
1
L-tryptophan
Homo sapiens
at pH 8.0 and 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.65
with 3-hydroxy-DL-kynurenine as substrate, pH and temperature not specified in the publication
0.85
with L-kynurenine as substrate, pH and temperature not specified in the publication
3.9
with L-kynurenine as substrate, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
KAT II
7 - 8
-
KAT II from brain
7.4 - 10
-
KAT I
8 - 9
8.8
-
total placental KAT activity
9.5 - 10
-
optimal pH range of human brain and placenta KAT I
9.6 - 10
-
KAT I from brain, sharp optimum
9.8
-
placental KAT I activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
KAT II activity is significantly lower in plasma of patients with Parkinson's disease when compared with normal individuals
Manually annotated by BRENDA team
KAT II may be involved in mechanisms of retinal ageing and neurodegeneration leading to formation of corpora amylacea
Manually annotated by BRENDA team
increase in KAT II activity in plasma of patients with Parkinson's disease when compared with normal individuals
Manually annotated by BRENDA team
KAT II is expressed in retinal ganglion cells
Manually annotated by BRENDA team
the enzyme is generally more expressed in oxidative muscle fibers
Manually annotated by BRENDA team
KAT I activity is significantly lower in plasma of patients with Parkinson's disease when compared with normal individuals
Manually annotated by BRENDA team
no difference in mRNA levels for KAT-1 when schizophrenic individuals are compared with normal individuals
Manually annotated by BRENDA team
in some parts, only faint expression of isoform KAT II, and occasionally no staining. No association of staining variability for KAT II and localization of Corpora amylacea
Manually annotated by BRENDA team
KAT I may be involved in mechanisms of retinal ageing and neurodegeneration leading to formation of corpora amylacea
Manually annotated by BRENDA team
no difference in KAT I activity between normal individuals and patients with Parkinson's disease
Manually annotated by BRENDA team
-
vitreous body and retina
Manually annotated by BRENDA team
no difference in mRNA levels for KAT-1 when schizophrenic individuals are compared with normal individuals
Manually annotated by BRENDA team
the enzyme is generally more expressed in oxidative muscle fibers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
KAT-II is the enzymatic isoform that mainly accounts for the synthesis of cerebral kynurenic acid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AADAT_HUMAN
425
0
47352
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
x * 46000, SDS-PAGE, x * 47875, calculated
47875
-
x * 46000, SDS-PAGE, x * 47875, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length pyridoxal phosphate-form, to 1.83 A resolution. The electron density of the active site reveals an aldimine linkage between pyridoxal phosphate and Lys263
KAT II complex with 2-oxoglutarate, hanging drop vapor diffusion method
native enzyme, diffraction to 2.16 A resolution, in complex with kynurenine, diffraction to 1.95 A. Enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes and shows a unique folding of its first 65 N-terminal residues
to 1.83 A resolution, space group P43212, with unit cell parameters a = b = 102.46 A, c = 86.24 A, alpha = beta= gamma = 90°
5’-pyridoxal phosphate and pyridoxamine form and in complex with competing substrate L-phenylalanine
Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
in complex with 3-indolepropionic acid or DL-indole-3-lactic acid, hanging drop vapor diffusion method, using 22% (w/v) PEG 4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5
in complex with pyridoxal 5'-phosphate and aminooxyacetate, hanging drop vapor diffusion method, using 200 mM sodium acetate, 29% (w/v) PEG4000 in 100 mM Tris, pH 7.3
native enzyme and selenomethionine derivative, diffraction to 2.3 A and 2.4 A resolution, respectively. Structure reveals an antiparallel strand-loopstrand motif that forms an unprecedented intersubunit beta-sheet in the functional KAT II dimer. The N-terminal regions of KAT II and aspartate aminotransferase appear to have converged to highly similar although 2fold symmetry-related conformations, which fulfill the same functional role. Structural comparison of isoforms KAT I and KAT II reveals a larger and more aliphatic character to the active site of KAT II due to the absence of the aromatic cage involved in ligand binding in KAT I
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y142F
-
active site mutation
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, isolated KAT II, no noticeable decrease in specific activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and gel filtration
ammonium sulfate precipitation, phenyl Sepharose column chromatography, DEAE Sepharose column chromatography, Blue Sepharose column chromatography, and Superdex 200 gel filtration
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta 2 cells
expression in Escherichia coli
expression in Sf9 cell
maltose-binding protein fusion protein expressed in Escherichia coli BL21(DE3)
expressed in Sf9 insect cells
expression in Escherichia coli
-
expression of KAT I in Cos-1 cells
-
His-tagged protein expressed in Sf21 cells, hydrophobic interaction chromatography, gel filtration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
isoform KAT2 is a therapeutic target for the management of schizophrenia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baran, H.; Cairns, N.; Lubec, B.; Lubec, G.
Increased kynurenic acid levels and decreased brain kynurenine aminotransferase I in patients with Down syndrome
Life Sci.
58
1891-1899
1996
Homo sapiens
Manually annotated by BRENDA team
Baran, H.; Amann, G.; Lubec, B.; Lubec, G.
Kynurenic acid and kynurenine aminotransferase in heart
Pediatr. Res.
41
404-410
1997
Homo sapiens
Manually annotated by BRENDA team
Milart, P.; Urbanska, E.M.; Turski, W.A.; Paszkowski, T.; Sikorski, R.
Kynurenine aminotransferase I activity in human placenta
Placenta
22
259-261
2001
Homo sapiens
Manually annotated by BRENDA team
Mosca, M.; Croci, C.; Mostardini, M.; Breton, J.; Malyszko, J.; Avanzi, N.; Toma, S.; Benatti, L.; Gatti, S.
Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs
Biochim. Biophys. Acta
1628
1-10
2003
Homo sapiens, Rattus norvegicus (Q08415)
Manually annotated by BRENDA team
Han, Q.; Li, J.
pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I
Eur. J. Biochem.
271
4804-4814
2004
Homo sapiens
Manually annotated by BRENDA team
Rossi, F.; Han, Q.; Li, J.; Rizzi, M.
Crystal structure of human kynurenine aminotransferase I
J. Biol. Chem.
279
50214-50220
2004
Homo sapiens (Q16773), Homo sapiens
Manually annotated by BRENDA team
Zarnowski, T.; Rejdak, R.; Zagorski, Z.; Juenemann, A.G.; Zrenner, E.; Kocki, T.; Urbanska, E.M.; Turski, W.A.
Content of kynurenic acid and activity of kynurenine aminotransferases in mammalian eyes
Ophthalmic Res.
36
124-128
2004
Bos taurus, Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Kapoor, R.; Lim, K.S.; Cheng, A.; Garrick, T.; Kapoor, V.
Preliminary evidence for a link between schizophrenia and NMDA-glycine site receptor ligand metabolic enzymes, d-amino acid oxidase (DAAO) and kynurenine aminotransferase-1 (KAT-1)
Brain Res.
1106
205-210
2006
Homo sapiens (Q16773)
Manually annotated by BRENDA team
Rejdak, R.; Rummelt, C.; Zrenner, E.; Grieb, P.; Zarnowski, T.; Okuno, E.; Schlotzer-Schrehardt, U.; Naumann, G.O.; Kruse, F.; Junemann, A.G.
Immunohistochemical identification of kynurenine aminotransferases in corpora amylacea in the human retina and optic nerve
Folia Neuropathol.
45
66-71
2007
Homo sapiens, Homo sapiens (Q16773), Homo sapiens (Q8N5Z0)
Manually annotated by BRENDA team
Yu, P.; Li, Z.; Zhang, L.; Tagle, D.A.; Cai, T.
Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family
Gene
365
111-118
2006
Rattus norvegicus (Q58FK9), Homo sapiens (Q6YP21), Homo sapiens, Mus musculus (Q71RI9), Mus musculus
Manually annotated by BRENDA team
Hartai, Z.; Klivenyi, P.; Janaky, T.; Penke, B.; Dux, L.; Vecsei, L.
Kynurenine metabolism in plasma and in red blood cells in Parkinsons disease
J. Neurol. Sci.
239
31-35
2005
Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
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
Rossi, F.; Garavaglia, S.; Montalbano, V.; Walsh, M.A.; Rizzi, M.
Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia
J. Biol. Chem.
283
3559-3566
2008
Homo sapiens
Manually annotated by BRENDA team
Han, Q.; Robinson, H.; Li, J.
Crystal structure of human kynurenine aminotransferase II
J. Biol. Chem.
283
3567-3573
2008
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Bellocchi, D.; Macchiarulo, A.; Carotti, A.; Pellicciari, R.
Quantum mechanics/molecular mechanics (QM/MM) modeling of the irreversible transamination of L-kynurenine to kynurenic acid: the round dance of kynurenine aminotransferase II
Biochim. Biophys. Acta
1794
1802-1812
2009
Homo sapiens
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.A.; Robinson, H.; Li, J.
Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
Biosci. Rep.
28
205-215
2008
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.A.; Li, J.
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
Cell. Mol. Life Sci.
67
353-368
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Rossi, F.; Schwarcz, R.; Rizzi, M.
Curiosity to kill the KAT (kynurenine aminotransferase): structural insights into brain kynurenic acid synthesis
Curr. Opin. Struct. Biol.
18
748-755
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
J. Med. Chem.
52
2786-2793
2009
Homo sapiens (Q16773), Homo sapiens
Manually annotated by BRENDA team
Wong, J.; Ray, W.J.; Kornilova, A.Y.
Development of a microplate fluorescence assay for kynurenine aminotransferase
Anal. Biochem.
409
183-188
2011
Homo sapiens
Manually annotated by BRENDA team
Akladios, F.N.; Nadvi, N.A.; Park, J.; Hanrahan, J.R.; Kapoor, V.; Gorrell, M.D.; Church, W.B.
Design and synthesis of novel inhibitors of human kynurenine aminotransferase-I
Bioorg. Med. Chem. Lett.
22
1579-1581
2012
Homo sapiens
Manually annotated by BRENDA team
Casazza, V.; Rossi, F.; Rizzi, M.
Biochemical and structural investigations on kynurenine aminotransferase II: an example of conformation-driven species-specific inhibition?
Curr. Top. Med. Chem.
11
148-157
2011
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Passera, E.; Campanini, B.; Rossi, F.; Casazza, V.; Rizzi, M.; Pellicciari, R.; Mozzarelli, A.
Human kynurenine aminotransferase II--reactivity with substrates and inhibitors
FEBS J.
278
1882-1900
2011
Homo sapiens
Manually annotated by BRENDA team
Rossi, F.; Valentina, C.; Garavaglia, S.; Sathyasaikumar, K.V.; Schwarcz, R.; Kojima, S.; Okuwaki, K.; Ono, S.; Kajii, Y.; Rizzi, M.
Crystal structure-based selective targeting of the pyridoxal 5-phosphate dependent enzyme kynurenine aminotransferase II for cognitive enhancement
J. Med. Chem.
53
5684-5689
2010
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Lu, H.; Kopcho, L.; Ghosh, K.; Witmer, M.; Parker, M.; Gupta, S.; Paul, M.; Krishnamurthy, P.; Laksmaiah, B.; Xie, D.; Tredup, J.; Zhang, L.; Abell, L.M.
Development of a RapidFire mass spectrometry assay and a fluorescence assay for the discovery of kynurenine aminotransferase II inhibitors to treat central nervous system disorders
Anal. Biochem.
501
56-65
2016
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Nematollahi, A.; Sun, G.; Harrop, S.J.; Hanrahan, J.R.; Church, W.B.
Structure of the PLP-form of the human kynurenine aminotransferase II in a novel spacegroup at 1.83 A resolution
Int. J. Mol. Sci.
17
446
2016
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Pinto, J.T.; Krasnikov, B.F.; Alcutt, S.; Jones, M.E.; Dorai, T.; Villar, M.T.; Artigues, A.; Li, J.; Cooper, A.J.
Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate beta-lyase activity and can transaminate L-selenomethionine
J. Biol. Chem.
289
30950-30961
2014
Homo sapiens (Q6YP21), Homo sapiens
Manually annotated by BRENDA team
Sun, G.; Nematollahi, A.; Nadvi, N.A.; Kwan, A.H.; Jeffries, C.M.; Church, W.B.
Expression, purification and crystallization of human kynurenine aminotransferase 2 exploiting a highly optimized codon set
Protein Expr. Purif.
121
41-45
2016
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Kalliokoski, T.; Rummakko, P.; Rantanen, M.; Blaesse, M.; Augustin, M.; Ummenthala, G.R.; Choudhary, S.; Venaelaeinen, J.
Discovery of sulfonamides and 9-oxo-2,8-diazaspiro[5,5]undecane-2-carboxamides as human kynurenine aminotransferase 2 (KAT2) inhibitors
Bioorg. Med. Chem. Lett.
30
127060
2020
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Wyckelsma, V.L.; Lindkvist, W.; Venckunas, T.; Brazaitis, M.; Kamandulis, S.; Paeaesuke, M.; Ereline, J.; Westerblad, H.; Andersson, D.C.
Kynurenine aminotransferase isoforms display fiber-type specific expression in young and old human skeletal muscle
Exp. Gerontol.
134
110880
2020
Homo sapiens, Homo sapiens (Q6YP21), Homo sapiens (Q8N5Z0)
Manually annotated by BRENDA team
Rossi, F.; Miggiano, R.; Ferraris, D.M.; Rizzi, M.
The synthesis of kynurenic acid in mammals an updated kynurenine aminotransferase structural KATalogue
Front. Mol. Biosci.
6
7-7
2019
Mus musculus (P05202), Mus musculus (Q71RI9), Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Jayawickrama, G.; Nematollahi, A.; Sun, G.; Church, W.
Improvement of kynurenine aminotransferase-II inhibitors guided by mimicking sulfate esters
PLoS ONE
13
e0196404
2018
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Nadvi, N.A.; Salam, N.K.; Park, J.; Akladios, F.N.; Kapoor, V.; Collyer, C.A.; Gorrell, M.D.; Church, W.B.
High resolution crystal structures of human kynurenine aminotransferase-I bound to PLP cofactor, and in complex with aminooxyacetate
Protein Sci.
26
727-736
2017
Homo sapiens (Q16773), Homo sapiens
Manually annotated by BRENDA team
Jayawickrama, G.S.; Nematollahi, A.; Sun, G.; Gorrell, M.D.; Church, W.B.
Inhibition of human kynurenine aminotransferase isozymes by estrogen and its derivatives
Sci. Rep.
7
17559
2017
Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Yoshida, Y.; Fujigaki, H.; Kato, K.; Yamazaki, K.; Fujigaki, S.; Kunisawa, K.; Yamamoto, Y.; Mouri, A.; Oda, A.; Nabeshima, T.; Saito, K.
Selective and competitive inhibition of kynurenine aminotransferase 2 by glycyrrhizic acid and its analogues
Sci. Rep.
9
10243
2019
Homo sapiens (Q8N5Z0)
Manually annotated by BRENDA team