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Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase and Organism(s) Rattus norvegicus and UniProt Accession Q64602

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     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:
Rattus norvegicus
UNIPROT: Q64602
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
kynurenine aminotransferases II
-
aminotransferase, kynurenine
-
-
-
-
KAT I
KAT II
KAT III
-
also called CCBL2
KAT IV
-
also called mitochondrial ASAT or GOT2
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
-
-
-
-
kynurenine aminotransferase I
-
-
kynurenine aminotransferase II
-
-
kynurenine aminotransferase III
-
kynurenine aminotransferase-I
-
kynurenine aminotransferases I
-
kynurenine pyruvate aminotransferase
-
i.e. KAT-I
kynurenine transaminase (cyclizing)
-
-
-
-
kynurenine-2-oxoglutarate aminotransferase
-
i.e. KAT-II
L-kynurenine aminotransferase
-
-
-
-
type II kynurenine aminotransferase
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
show the reaction diagram
transamination of the amino acid to a transient keto acid intermediate which spontaneously undergoes ring closure
-
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-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
91% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
28% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
enzyme has both kynurenine aminotransferase and alpha-aminoadipate aminotransferase activity
-
?
L-kynurenine + 4-methyl-2-oxovalerate
kynurenic acid + 2,4-dimethylvalerate + H2O
show the reaction diagram
5.9% of activity with 2-oxoglutarate
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
show the reaction diagram
43% of activity with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
3% of activity with 2-oxoglutarate
-
?
3,5-diiodo-L-tyrosine + 2-oxoglutarate
3-(2,5-diiodo-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
slightly better than L-kynurenine
-
?
L-2-aminoheptane-1,7-dioate + 2-oxoglutarate
2-oxoheptane-1,7-dioate + L-glutamate
show the reaction diagram
-
at 39.7% of the activity with 2-aminohexane-1,6-dioate
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
L-4-chloro-kynurenine + 2-oxoglutarate
L-7-chloro-kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-5-chloro-kynurenine + 2-oxoglutarate
L-6-chloro-kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
show the reaction diagram
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
show the reaction diagram
-
poor substrate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
show the reaction diagram
-
12% the rate of L-kynurenine
-
?
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
-
at about 30% the rate of L-kynurenine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
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
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
inducible enzyme of tryptophan catabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
approx. 4fold increase in activity at pH 6.4
additional information
-
not activated by chloride salts of Mg2+, Mn2+, Na+, K+ or NH4+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
-
i.e. PF-04859989, selective inhibitor
(S)-(4)-(ethylsulfonyl)benzoylalanine
-
no inhibition of the human enzyme
(S)-4-ethylsulfonylbenzoylalanine
-
specific inhibitor of KAT II
(S)-9-(4-aminopiperazine-1-yl)-8-fluoro-3-methyl-6-oxo-2,3,5,6-tetrahydro-4H-1-oxa-3a-azaphenalene-5-carboxylic acid
-
BFF 122, KAT II activity is totally blocked at 0.01 mM, 43% inhibition of KAT II at 0.001 mM, 26% inhibition of KAT I at 1 mM
2-Aminoadipate
-
-
2-oxoadipate
-
-
2-oxoglutarate
-
substrate inhibition
3-hydroxykynurenine
4-carboxy-3-hydroxyphenylglycine
-
inhibition of brain KAT II
4-chloromercuribenzoate
-
-
adipate
alpha-aminoadipate
-
strong inhibition of KAT II
amino-2,3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid
-
inhibitory in whole cells
aminooxyacetic acid
-
inhibitory in whole cells
anthranilate
-
weak inhibition
azelaic acid
-
-
Decanoic acid
-
-
Dicarboxylic acids
-
C-2 to C-10
Diethylglutaric acid
-
-
dimethylglutaric acid
-
-
EGTA
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
glutamate
-
weak inhibition
glutamine
hydroxylamine
-
complete inhibition
Isonicotinic acid hydrazide
-
anti-tuberculosis drug, enzyme is inhibited in animals fed with a diet containing isonicotinic acid hydrazide and by injection of the drug
KCN
-
complete inhibition
Kynurenate
-
weak inhibition
L-2-amino-4-phosphonobutyric acid
-
inhibition of brain KAT II
L-4-chlorokynurenine
-
-
L-5-chlorokynurenine
-
-
L-aspartate
-
0.72 mM, 50% inhibition of brain KAT I, 0.073 mM, 50% inhibition of brain KAT II
L-cysteate
-
5.38 mM, 50% inhibition of brain KAT I, 1.55 mM, 50% inhibition of brain KAT II
L-cysteine
L-cysteine sulfinate
-
0.002 mM, 50% inhibition of brain KAT II
L-glutamate
-
1.3 mM, 50% inhibition of brain KAT I, 0.79 mM, 50% inhibition of brain KAT II
L-Homocysteate
-
5.0 mM, 50% inhibition of brain KAT I, 2.1 mM, 50% inhibition of brain KAT II
L-Homocysteine sulfinate
-
1.59 mM, 50% inhibition of brain KAT II
L-kynurenine
-
substrate inhibition above 6 mM
L-leucine
-
inhibitory in whole cells
L-phenylalanine
-
strong inhibition of KAT I
L-serine-O-phosphate
-
inhibition of brain KAT II
L-tryptophan
N-omega-nitro-L-arginine
-
-
nicotinate
-
weak inhibition
phosphate
-
-
pimelate
-
-
quinolinic acid
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
quisqualate
S-dichlorovinyl-L-cysteine
Sulfate or phosphate esters of steroids
-
-
-
trans-pyrrolidine-2,4-dicarboxylate
-
inhibition of brain KAT II
xanthurenate
-
weak inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
2-oxoglutarate
pH 8.0, 37°C, recombinant enzyme, cosubstrate L-kyrunenine
1.36
L-3-hydroxykynurenine
pH 8.0, 37°C, recombinant enzyme
5.6
L-glutamate
pH 8.0, 37°C, alpha-aminoadipate aminotransferase activity
0.95
L-kynurenine
pH 8.0, 37°C, recombinant enzyme
0.01
2-oxoadipate
-
-
0.013 - 1
2-oxoglutarate
2 - 6.3
L-3-hydroxykynurenine
0.083 - 5
L-kynurenine
0.00085
pyridoxal 5'-phosphate
-
pH 6.5, 37°C
0.053 - 1.63
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
-
L-kynurenine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
KAT II
9 - 9.5
-
KAT I
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.8
-
maximal activity at pH 6.5, approx. half-maximal activity at pH 8.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
neuronal culture prepared from cortices of 18-day-old fetuses
Manually annotated by BRENDA team
astrocytes in the substantia nigra express KAT-I under normal conditions. The amount of this enzyme increases after administration of 6-hydroxydopamine
Manually annotated by BRENDA team
microglial cells become KAT-I immunoreactive only after treatment with 6-hydroxydopamine
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
oligodendrocyte cell line
Manually annotated by BRENDA team
-
KAT I, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
pars compacta. Neurons and glial cells. Treatment with 6-hydroxydopamine produces loss of the majority of nigral neurons. KAT-I diminished considerably in the remaining neurons. Astrocytes in the substantia nigra express KAT-I under normal conditions, the amount of this enzyme increases after administration of 6-hydroxydopamine. Microglial cells become KAT-I immunoreactive only after treatment with 6-hydroxydopamine
Manually annotated by BRENDA team
-
KAT I, low activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
KAT I of astroglial cells is associated with ribosomes of the endoplasmic reticulum
Manually annotated by BRENDA team
-
10% of liver total activity at pH 6.5
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
acute administration of the KAT II inhibitor (3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one is associated with a short-onset, time-dependent decrease in firing rate and burst activity of dopamine neurons, both parameters reaching a 50% reduction within 45 min. (3S)-3-Amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one reduces the number of spontaneously active dopamine cells. Pretreatment with D-cycloserine or [3-[[(3,4-dichlorophenyl)methyl]amino]propyl](diethoxy-methyl) phosphinic acid (CGP-52432) prevents the inhibitory action of (3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one. Pretreatment with methyllycaconitine does not change the response, whereas picrotoxin partially prevents the inhibitory effects of (3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AADAT_RAT
425
0
47784
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
2 * 45000, SDS-PAGE
90000 - 100000
gel filtration
100000
-
isoenzyme 2, sucrose density gradient centrifugation
44000
-
2 * 44000, SDS-PAGE
45000
-
2 * 45000, SDS-PAGE in the absence of 2-mercaptoethanol
45500
-
2 * 45500, SDS-PAGE in the presence of 2-mercaptoethanol
47000
-
2 * 47000, SDS-PAGE
49500
-
2 * 49500, SDS-PAGE
85000
90000 - 100000
-
gel filtration
91000
-
gel filtration
additional information
-
amino acid composition
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 45000, SDS-PAGE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E61G
40-60% of wild-type activity, Km for L-kynurenine and pyruvate is reduced, missense mutation found in spontaneously hypertensive rats
E64G
-
the naturally occurring mutation in rat KAT I results in dramatically impaired kynurenic acid synthesis and in an associated spontaneously hypertensive phenotype
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
75 min, inactivation, t1/2: 30 min
636622
5
-
and below, inactivation even in the presence of pyridoxal phosphate
636608
6.5 - 7.5
-
most stable
636608
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
phosphate buffer, pH 6.3, inactivation within a few min, pyridoxal phosphate restores activity, only slow inactivation at pH 7.4, 2-oxoglutarate protects
40
-
and above, 5 min, decreasing activity
50
-
in 20% glycerol, 0.1 mM DTT, 2 mM pyridoxal phosphate, 25 mM imidazole-HCl buffer, pH 7, 30 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alcohol fractionation inactivates
-
ammonium sulfate fractionation inactivates
-
dialysis against phosphate buffer inactivates, 2-oxoglutarate protects to some extent
-
dialysis of the apoenzyme against Tris-HCl or imidazole-HCl buffer inactivates
-
freeze-thawing inactivates
-
slightly acidic buffer solutions inactivate, pyridoxal phosphate or pyridoxamine phosphate restores activity, 2-oxoglutarate protects
-
stable in phosphate buffer supplemented with pyridoxal phosphate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 10 mM phosphate buffer, pH 7, 50% glycerol, at least 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sepharose, phenyl-Sepharose, Mono Q, Mono P
acid precipitation, ammonium sulfate, DEAE-cellulose, hydroxylapatite
-
DEAE-cellulose, heat treatment, hydroxyapatite, CM-Sephadex C-25, Sephadex G-100
-
DEAE-Sepharose, ammonium sulfate, Sephadex G-25, partial purification of KAT I and KAT II
-
DEAE-Sepharose, phenyl-Sepharose, Superose 12, Mono Q
-
partial purification
-
partial purification of kynurenine apotransaminase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transient expression in HEK-293 cells
transient expression in HEK-293 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alberati-Giani, D.; Malherbe, P.; Khler, C.; Lang, G.; Kiefer, V.; Lahm, H.W.; Cesura, A.M.
Cloning and characterization of a soluble kynurenine aminotransferase from rat brain: identity with kidney cysteine conjugate beta-lyase
J. Neurochem.
64
1448-1455
1995
Rattus norvegicus
Manually annotated by BRENDA team
Cesura, A.M.; Alberati-Giani, D.; Buchli, R.; Broger, C.; Kohler, C.; Vilbois, F.; Lahm, H.W.; Heitz, M.P.; Malherbe, P.
Molecular characterization of kynurenine pathway enzymes: 3-Hydroxyanthranilic-acid dioxygenase and kynurenine aminotransferase
Adv. Exp. Med. Biol.
398
477-483
1996
Rattus norvegicus
Manually annotated by BRENDA team
Mason, M.
Kynurenine transaminase of rat kidney: a study of coenzyme dissociation
J. Biol. Chem.
227
61-68
1957
Rattus norvegicus
Manually annotated by BRENDA team
Tobes, M.C.
Kynurenine-oxoglutarate aminotransferase from rat kidney
Methods Enzymol.
142
217-224
1987
Rattus norvegicus
Manually annotated by BRENDA team
De Antoni, A.; Costa, C.; Allegri, G.
Studies on the kynurenine adminotransferase activity in rat liver and kidney
Hoppe-Seyler's Z. Physiol. Chem.
357
1707-1712
1976
Rattus norvegicus
Manually annotated by BRENDA team
Noguchi, T.; Minatogawa, Y.; Okuno, E.; Nakatani, M.; Morimoto, M.; Kido, R.
Purification and characterization of kynurenine-2-oxoglutarate aminotransferase from the liver, brain and small intestine of rats
Biochem. J.
151
399-406
1975
Rattus norvegicus, Rattus norvegicus Donryu
Manually annotated by BRENDA team
Nakatani, M.; Morimoto, M.; Noguchi, T.; Kido, R.
Subcellular distribution and properties of kynurenine transaminase in rat liver
Biochem. J.
143
303-310
1974
Rattus norvegicus, Rattus norvegicus Donryu
Manually annotated by BRENDA team
Mason, M.
Effects of calcium ions and quinolinic acid on rat kidney mitochondrial kynurenine aminotransferase
Biochem. Biophys. Res. Commun.
60
64-69
1974
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Kido, R.; Noguchi, T.
Subcellular distribution and properties of rat liver kynurenine transaminase
Acta Vitaminol. Enzymol.
29
307-309
1975
Rattus norvegicus
Manually annotated by BRENDA team
Hartline, R.A.
Kynurenine aminotransferase from kidney supernatant
Methods Enzymol.
113
664-672
1985
Rattus norvegicus
Manually annotated by BRENDA team
Mawal, M.R.; Mukhopadhyay, A.; Deshmukh, D.R.
Purification and properties of kynurenine aminotransferase from rat kidney
Biochem. J.
279
595-599
1991
Rattus norvegicus
-
Manually annotated by BRENDA team
Mawal, M.R.; Deshmukh, D.R.
alpha-Aminoadipate and kynurenine aminotransferase activities from rat kidney. Evidence for separate identity
J. Biol. Chem.
266
2573-2575
1991
Rattus norvegicus
Manually annotated by BRENDA team
Takeuchi, F.; Otsuka, H.; Shibata, Y.
Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase
Biochim. Biophys. Acta
743
323-330
1983
Rattus norvegicus
Manually annotated by BRENDA team
Buchli, R.; Alberati-Giani, D.; Malherbe, P.; Kohler, C.; Broger, C.; Cesura, A.M.
Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney
J. Biol. Chem.
270
29330-29335
1995
Rattus norvegicus (Q64602)
Manually annotated by BRENDA team
Malherbe, P.; Alberati-Giani, D.; Koehler, C.; Cesura, A.M.
Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain
FEBS Lett.
367
141-144
1995
Rattus norvegicus (Q08415)
Manually annotated by BRENDA team
Varasi, M.; Della Torre, A.; Heidempergher, F.; Pevarello, P.; Speciale, C.; Guidetti, P.; Wells, D.R.; Schwarcz, R.
Derivatives of kynurenine as inhibitors of rat brain kynurenine aminotransferase
Eur. J. Med. Chem.
31
11-21
1996
Rattus norvegicus
-
Manually annotated by BRENDA team
Shibata, K.; Marugami, M.; Kondo, T.
In vivo inhibition of kynurenine aminotransferase activity by isonicotinic acid hydrazide in rats
Biosci. Biotechnol. Biochem.
60
874-876
1996
Rattus norvegicus
Manually annotated by BRENDA team
Okuno, E.; Nishikawa, T.; Nakamura, M.
Kynurenine aminotransferases in the rat. Localization and characterization
Adv. Exp. Med. Biol.
398
455-464
1996
Rattus norvegicus
Manually annotated by BRENDA team
Guidetti, P.; Okuno, E.; Schwarcz, R.
Characterization of rat brain kynurenine aminotransferases I and II
J. Neurosci. Res.
50
457-465
1997
Rattus norvegicus
Manually annotated by BRENDA team
Knyihar-Csillik, E.; Okuno, E.; Vecsei, L.
Effects of in vivo sodium azide administration on the immunohistochemical localization of kynurenine aminotransferase in the rat brain
Neuroscience
94
269-277
1999
Rattus norvegicus
Manually annotated by BRENDA team
Battaglia, G.; Rassoulpour, A.; Wu, H.Q.; Hodgkins, P.S.; Kiss, C.; Nicoletti, F.; Schwarcz, R.
Some metabotropic glutamate receptor ligands reduce kynurenate synthesis in rats by intracellular inhibition of kynurenine aminotransferase II
J. Neurochem.
75
2051-2060
2000
Rattus norvegicus
Manually annotated by BRENDA team
Kwok, J.B.J.; Kapoor, R.; Gotoda, T.; Iwamoto, Y.; Iizuka, Y.; Yamada, N.; Isaacs, K.E.; Kushwaha, V.V.; Church, W.B.; Schofield, P.R.; Kapoor, V.
A Missense Mutation in Kynurenine Aminotransferase-1 in Spontaneously Hypertensive Rats
J. Biol. Chem.
277
35779-35782
2002
Rattus norvegicus (Q08415)
Manually annotated by BRENDA team
Csillik, A.; Knyihar, E.; Okuno, E.; Krisztin-Peva, B.; Csillik, B.; Vecsei, L.
Effect of 3-nitropropionic acid on kynurenine aminotransferase in the rat brain
Exp. Neurol.
177
233-241
2002
Rattus norvegicus
Manually annotated by BRENDA team
Kocki, T.; Luchowski, P.; Luchowska, E.; Wielosz, M.; Turski, W.A.; Urbanska, E.M.
L-cysteine sulphinate, endogenous sulphur-containing amino acid, inhibits rat brain kynurenic acid production via selective interference with kynurenine aminotransferase II
Neurosci. Lett.
346
97-100
2003
Rattus norvegicus
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
Wejksza, K.; Rzeski, W.; Okuno, E.; Kandefer-Szerszen, M.; Albrecht, J.; Turski, W.A.
Demonstration of kynurenine aminotransferases I and II and characterization of kynurenic acid synthesis in oligodendrocyte cell line (OLN-93)
Neurochem. Res.
30
963-968
2005
Rattus norvegicus
Manually annotated by BRENDA team
Knyihar-Csillik, E.; Chadaide, Z.; Mihaly, A.; Krisztin-Peva, B.; Fenyo, R.; Vecsei, L.
Effect of 6-hydroxydopamine treatment on kynurenine aminotransferase-I (KAT-I) immunoreactivity of neurons and glial cells in the rat substantia nigra
Acta Neuropathol.
112
127-137
2006
Rattus norvegicus (Q08415)
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
Rzeski, W.; Kocki, T.; Dybel, A.; Wejksza, K.; Zdzisinska, B.; Kandefer-Szerszen, M.; Turski, W.A.; Okuno, E.; Albrecht, J.
Demonstration of kynurenine aminotransferases I and II and characterization of kynurenic acid synthesis in cultured cerebral cortical neurons
J. Neurosci. Res.
80
677-682
2005
Rattus norvegicus (Q08415), Rattus norvegicus (Q64602)
Manually annotated by BRENDA team
Rozsa, E.; Robotka, H.; Nagy, D.; Farkas, T.; Sas, K.; Vecsei, L.; Toldi, J.
The pentylenetetrazole-induced activity in the hippocampus can be inhibited by the conversion of L-kynurenine to kynurenic acid: an in vitro study
Brain Res. Bull.
76
474-479
2008
Rattus norvegicus
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
Fukushima, T.; Sone, Y.; Mitsuhashi, S.; Tomiya, M.; Toyooka, T.
Alteration of kynurenic acid concentration in rat plasma following optically pure kynurenine administration: a comparative study between enantiomers
Chirality
21
468-472
2009
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
Amori, L.; Guidetti, P.; Pellicciari, R.; Kajii, Y.; Schwarcz, R.
On the relationship between the two branches of the kynurenine pathway in the rat brain in vivo
J. Neurochem.
109
316-325
2009
Rattus norvegicus
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
Linderholm, K.R.; Alm, M.T.; Larsson, M.K.; Olsson, S.K.; Goiny, M.; Hajos, M.; Erhardt, S.; Engberg, G.
Inhibition of kynurenine aminotransferase II reduces activity of midbrain dopamine neurons
Neuropharmacology
102
42-47
2016
Rattus norvegicus
Manually annotated by BRENDA team