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Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase and Organism(s) Mus musculus and UniProt Accession P05202

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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:
Mus musculus
UNIPROT: P05202
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The taxonomic range for the selected organisms is: Mus musculus
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
aspartate aminotransferase
-
glutamic-oxaloacetic transaminase 2
-
KAT IV
isoform
kynurenine aminotransferase
-
kynurenine aminotransferase IV
-
kynurenine aminotransferase-IV
-
mitochondrial aspartate aminotransferase
-
aminoadipate aminotransferase
-
aminotransferase, kynurenine
-
-
-
-
cysteine conjugate beta-lyase 1
-
cysteine conjugate beta-lyase 2
-
glutamine transaminase K
-
KAT I
-
also called GTK or CCBL1
KAT II
-
also called AADAT
KAT III
KAT IV
-
also called mitochondrial ASAT or GOT2
KAT3
-
-
KAT3/GTL/CCBL2
-
-
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
kynurenine aminotransferase 3
-
-
kynurenine aminotransferase I
-
kynurenine aminotransferase II
-
kynurenine aminotransferase III
-
kynurenine transaminase (cyclizing)
-
-
-
-
L-kynurenine aminotransferase
-
-
-
-
additional information
-
see also EC 2.6.1.64 and EC 4.4.1.13
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
kynurenic acid + L-methionine
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxocaproic acid
kynurenic acid + 2-aminohexanoate
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxovalerate
kynurenic acid + 2-aminopentanoate
show the reaction diagram
-
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + hydroxyphenylpyruvate
kynurenic acid + L-tyrosine
show the reaction diagram
-
-
-
?
L-kynurenine + indole-3-pyruvate
kynurenic acid + L-tryptophan
show the reaction diagram
-
-
-
?
L-kynurenine + mercaptopyruvate
kynurenic acid + ?
show the reaction diagram
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + phenylpyruvate
kynurenic acid + L-phenylalanine
show the reaction diagram
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
?
2-aminobutyrate + glyoxylate
?
show the reaction diagram
-
-
-
?
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
?
3-hydroxykynurenine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-asparagine + glyoxylate
?
show the reaction diagram
KAT II has high transamination activity toward L-asparagine
-
-
?
L-cysteine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-glutamine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-histidine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxobutyrate
?
show the reaction diagram
-
high activity
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxocaproate
?
show the reaction diagram
-
high activity, 2-oxocaproate is the best cosubstrate
-
-
?
L-kynurenine + 2-oxocaproic acid
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
show the reaction diagram
-
very low activity with 2-oxogltarate
-
-
?
L-kynurenine + 2-oxoglutarate
?
show the reaction diagram
poor cosubstrate for KAT III
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxoisocaproic acid
4-(2-aminophenyl)-2,4-dioxobutanoate + L-leucine
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoleucine
?
show the reaction diagram
-
moderate activity
-
-
?
L-kynurenine + 2-oxomethylthiobutyric acid
?
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxovalerate
?
show the reaction diagram
L-kynurenine + 2-oxovaline
?
show the reaction diagram
-
low activity
-
-
?
L-kynurenine + glyoxylate
?
show the reaction diagram
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
show the reaction diagram
L-kynurenine + hydroxyphenylpyruvate
?
show the reaction diagram
-
moderate activity
-
-
?
L-kynurenine + indol-3-pyruvate
?
show the reaction diagram
-
moderate activity
-
-
?
L-kynurenine + indol-3-ylpyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + mercaptopyruvate
?
show the reaction diagram
L-kynurenine + oxaloacetate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-aspartate
show the reaction diagram
-
moderate activity
-
-
?
L-kynurenine + oxaloacetate
?
show the reaction diagram
-
-
-
?
L-kynurenine + p-hydroxyphenylpyruvate
?
show the reaction diagram
-
-
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
show the reaction diagram
-
high activity
-
-
?
L-kynurenine + phenylpyruvate
?
show the reaction diagram
L-kynurenine + pyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-alanine
show the reaction diagram
-
moderate activity
-
-
?
L-kynurenine + pyruvate
?
show the reaction diagram
poor cosubstrate for KAT III
-
-
?
L-lysine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-methionine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-phenylalanine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
?
show the reaction diagram
-
-
-
?
L-tryptophan + glyoxylate
?
show the reaction diagram
-
-
-
?
L-tyrosine + glyoxylate
?
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
irreversible inhibitor
(5S)-5-amino-7-hydroxy-2-phenyl-2,4,5,7-tetrahydro-6H-pyrazolo[3,4-b]pyridin-6-one
irreversible inhibitor
3-hydroxykynurenine
-
Indole-3-propionic acid
-
L-cysteine
-
L-glutamine
-
L-histidine
-
L-leucine
-
L-methionine
L-tryptophan
-
KAT I is greatly and specifically inhibited by 5 mM L-tryptophan
methionine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.7
2-oxo-4-methylthiobutyrate
pH 7.5, 38°C
42.2
2-oxobutyrate
pH 7.5, 38°C
10.4
2-oxocaproic acid
pH 7.5, 38°C
2.4
2-oxoglutarate
pH 7.5, 38°C
10.9
2-oxovalerate
pH 7.5, 38°C
4.2
glyoxylate
pH 7.5, 38°C
1.6
hydroxyphenylpyruvate
pH 7.5, 38°C
3.6
Indole-3-pyruvate
pH 7.5, 38°C
3.2
Mercaptopyruvate
pH 7.5, 38°C
0.9
oxaloacetate
pH 7.5, 38°C
0.7
phenylpyruvate
pH 7.5, 38°C
8.3
pyruvate
pH 7.5, 38°C
1
2-oxobutyrate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.5
2-oxocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
8.1
2-oxoglutarate
in 100 mM boric acid buffer, pH 9.0, at 45°C
5.3
2-oxoisocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.2
2-oxovalerate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.4
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.4
glyoxylate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1
hydroxyphenylpyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.5
indo-3-pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
6.2
L-alanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.4
L-asparagine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.7
L-cysteine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.7
L-glutamine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.7
L-histidine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.5
L-kynurenine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.9
L-methionine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.1
L-phenylalanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
3
L-serine
in 100 mM boric acid buffer, pH 9.0, at 45°C
7.1
L-tryptophan
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.7
L-tyrosine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.4
Mercaptopyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
4.9
oxaloacetate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.6
phenylpyruvate
10.6
pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
2-oxo-4-methylthiobutyrate
pH 7.5, 38°C
0.69
2-oxobutyrate
pH 7.5, 38°C
0.41
2-oxocaproic acid
pH 7.5, 38°C
0.53
2-oxoglutarate
pH 7.5, 38°C
0.13
2-oxovalerate
pH 7.5, 38°C
0.19
glyoxylate
pH 7.5, 38°C
0.41
hydroxyphenylpyruvate
pH 7.5, 38°C
0.49
Indole-3-pyruvate
pH 7.5, 38°C
0.44
Mercaptopyruvate
pH 7.5, 38°C
0.32
oxaloacetate
pH 7.5, 38°C
0.63
phenylpyruvate
pH 7.5, 38°C
0.37
pyruvate
pH 7.5, 38°C
2.93
2-oxobutyrate
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.59
2-oxocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.37
2-oxoglutarate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.74
2-oxoisocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.7
2-oxovalerate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.02
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.71
glyoxylate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.48
hydroxyphenylpyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.03
indo-3-pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.53
L-alanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.93
L-asparagine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.3
L-cysteine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.27
L-glutamine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2
L-histidine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.3
L-kynurenine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.43
L-methionine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.7
L-phenylalanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.17
L-serine
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.57
L-tryptophan
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.03
L-tyrosine
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.28
Mercaptopyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.68
oxaloacetate
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.53 - 3.17
phenylpyruvate
1.87
pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2-oxo-4-methylthiobutyrate
pH 7.5, 38°C
0.02
2-oxobutyrate
pH 7.5, 38°C
0.04
2-oxocaproic acid
pH 7.5, 38°C
0.22
2-oxoglutarate
pH 7.5, 38°C
0.01
2-oxovalerate
pH 7.5, 38°C
0.05
glyoxylate
pH 7.5, 38°C
0.26
hydroxyphenylpyruvate
pH 7.5, 38°C
0.13
Indole-3-pyruvate
pH 7.5, 38°C
0.14
Mercaptopyruvate
pH 7.5, 38°C
0.35
oxaloacetate
pH 7.5, 38°C
0.96
phenylpyruvate
pH 7.5, 38°C
0.05
pyruvate
pH 7.5, 38°C
2.93
2-oxobutyrate
in 100 mM boric acid buffer, pH 9.0, at 45°C
5.18
2-oxocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.045
2-oxoglutarate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.14
2-oxoisocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.25
2-oxovalerate
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.54
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
6.78
glyoxylate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.48
hydroxyphenylpyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.07
indo-3-pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.25
L-alanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.095
L-asparagine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.86
L-cysteine
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.24
L-glutamine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.86
L-histidine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.53
L-kynurenine
2.7
L-methionine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.45
L-phenylalanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.72
L-serine
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.5
L-tryptophan
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.38
L-tyrosine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.37
Mercaptopyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.75
oxaloacetate
in 100 mM boric acid buffer, pH 9.0, at 45°C
4.22 - 5.28
phenylpyruvate
0.18
pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3
with L-kynurenine as substrate, pH and temperature not specified in the publication
0.45
with 3-hydroxy-DL-kynurenine as substrate, pH and temperature not specified in the publication
0.5
with 3-hydroxy-DL-kynurenine as substrate, pH and temperature not specified in the publication
2.5
with L-kynurenine as substrate, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
KAT IV
7.5
-
assay at
8
-
KAT IV
9 - 10
-
KAT III
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
tissue localizations of KAT3/GTL/CCBL2, real-time RT-PCR enzyme expression analysis in tissues of female and male animals, overview. The enzyme is present in both liver and kidney of the mouse, but is much more abundant in the kidney than in the liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
kynurenine aminotransferase 3 (KAT3, EC 2.6.1.7) catalyzes the transamination of kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2, EC 4.4.1.13) and glutamine transaminase L (GTL, EC 2.6.1.64)
physiological function
-
kynurenine aminotransferase 3 (KAT3) catalyzes the transamination of kynurenine to kynurenic acid
additional information
-
the enzyme is a key enzyme for studying the nephrotoxic mechanism of some xenobiotics and the formation of chemopreventive compounds in the mouse kidney
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AATM_MOUSE
430
0
47411
Swiss-Prot
Mitochondrion (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, PEG 4000,
in complex with L-kynurenine and L-glutamine, hanging drop vapor diffusion method, using 21% (w/v) polyethylene glycol 400, 10% glycerol, 150 mM CaCl2, and 100 mM HEPES, pH 7.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing do not alter the activity
freezing and thawing do not alter the activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, ion exchange chromatography (Q-Sepharose), gel filtration
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
DEAE Sepharose column chromatography, hydroxyapatite column chromatography, Mono-Q column chromatography, and gel filtration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity purification, two different steps of anion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chitin-binding domain fusion proteinfusionexpressed in Escherichia coli
tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli
expressed in Sf9 insect cells
recombinant His-tagged enzyme expression in Escherichia coli, enzyme expression analysis by realtime RT-PCR
-
tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the enzyme is a key enzyme for studying the nephrotoxic mechanism of some xenobiotics and the formation of chemopreventive compounds in the mouse kidney
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Biochemical and structural properties of mouse kynurenine aminotransferase III
Mol. Cell. Biol.
29
784-793
2009
Mus musculus (Q71RI9), Mus musculus
Manually annotated by BRENDA team
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
Biosci. Rep.
31
323-332
2011
Mus musculus (P05202), Mus musculus
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.; Li, J.
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases
BMC Biochem.
11
0019
2010
Mus musculus (P05202), Mus musculus (Q71RI9), Mus musculus (Q8BTY1), Mus musculus (Q9WVM8), Mus musculus
Manually annotated by BRENDA team
Yang, C.; Zhang, L.; Han, Q.; Liao, C.; Lan, J.; Ding, H.; Zhou, H.; Diao, X.; Li, J.
Kynurenine aminotransferase 3/glutamine transaminase L/cysteine conjugate beta-lyase 2 is a major glutamine transaminase in the mouse kidney
Biochem. Biophys. Rep.
8
234-241
2016
Mus musculus
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