2.6.1.7: kynurenine-oxoglutarate transaminase
This is an abbreviated version!
For detailed information about kynurenine-oxoglutarate transaminase, go to the full flat file.
Word Map on EC 2.6.1.7
-
2.6.1.7
-
alt
-
bilirubin
-
creatinine
-
cholesterol
-
albumin
-
necrosis
-
triglyceride
-
fibrosis
-
hepatotoxicity
-
platelet
-
hepatocytes
-
dismutase
-
malondialdehyde
-
hepatoprotective
-
tnf
-
lipoprotein
-
hemoglobin
-
sod
-
bile
-
catalase
-
cirrhosis
-
gamma-glutamyl
-
wistar
-
gg
-
ccl4
-
nafld
-
reperfusion
-
admission
-
gamma-glutamyltransferase
-
hematological
-
nonalcoholic
-
c-reactive
-
uric
-
portal
-
tetrachloride
-
transpeptidase
-
steatosis
-
steatohepatitis
-
ccl4-induced
-
globulin
-
phosphokinase
-
prothrombin
-
hematocrit
-
transaminases
-
jaundice
-
glutamyl
-
analysis
-
tetrachloride-induced
-
silymarin
-
medicine
-
child-pugh
-
corpuscular
- 2.6.1.7
-
alt
- bilirubin
- creatinine
- cholesterol
- albumin
- necrosis
- triglyceride
- fibrosis
-
hepatotoxicity
- platelet
- hepatocytes
- dismutase
- malondialdehyde
-
hepatoprotective
- tnf
- lipoprotein
- hemoglobin
- sod
- bile
- catalase
- cirrhosis
-
gamma-glutamyl
- wistar
- gg
- ccl4
- nafld
-
reperfusion
-
admission
- gamma-glutamyltransferase
- hematological
-
nonalcoholic
-
c-reactive
-
uric
-
portal
-
tetrachloride
- transpeptidase
- steatosis
- steatohepatitis
-
ccl4-induced
- globulin
-
phosphokinase
- prothrombin
-
hematocrit
- transaminases
-
jaundice
-
glutamyl
- analysis
-
tetrachloride-induced
- silymarin
- medicine
-
child-pugh
-
corpuscular
Reaction
Synonyms
AadAT, aminoadipate aminotransferase, aminotransferase, kynurenine, aspartate aminotransferase, Bna3, CCBL2, cysteine conjugate beta-lyase 1, cysteine conjugate beta-lyase 2, glutamic-oxaloacetic transaminase 2, glutamine transaminase K, KAT, KAT I, KAT II, KAT III, KAT IV, KAT-1, KAT-I, KAT-II, KAT2, KAT3, KAT3/GTL/CCBL2, KYAT3, kynurenine 2-oxoglutarate transaminase, kynurenine aminotransferase, kynurenine aminotransferase 2, kynurenine aminotransferase 3, kynurenine aminotransferase I, kynurenine aminotransferase II, kynurenine aminotransferase III, kynurenine aminotransferase IV, kynurenine aminotransferase-1, kynurenine aminotransferase-I, kynurenine aminotransferase-IV, kynurenine aminotransferases I, kynurenine aminotransferases II, kynurenine pyruvate aminotransferase, kynurenine transaminase (cyclizing), kynurenine-2-oxoglutarate aminotransferase, kynurenine/alpha-aminoadipate aminotransferase, L-kynurenine aminotransferase, mitochondrial aspartate aminotransferase, More, PhKAT, phKAT-II, type II kynurenine aminotransferase
ECTree
2.6.1.7 kynurenine-oxoglutarate transaminaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,5-diiodo-L-tyrosine + 2-oxoglutarate
3-(2,5-diiodo-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
slightly better than L-kynurenine
-
?
L-2-aminoheptane-1,7-dioate + 2-oxoglutarate
2-oxoheptane-1,7-dioate + L-glutamate
-
at 39.7% of the activity with 2-aminohexane-1,6-dioate
-
?
L-2-aminohexane-1,6-dioate + 2-oxoglutarate
2-oxohexane-1,6-dioate + L-glutamate
Hansenula schneggii
-
at about 60% the rate of L-kynurenine
-
?
L-4-chloro-kynurenine + 2-oxoglutarate
L-7-chloro-kynurenic acid + L-glutamate
-
-
-
?
L-5-chloro-kynurenine + 2-oxoglutarate
L-6-chloro-kynurenic acid + L-glutamate
-
-
-
?
L-asparagine + glyoxylate
?
KAT II has high transamination activity toward L-asparagine
-
-
?
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenic acid + L-methionine
-
-
-
?
L-kynurenine + 2-oxocaproic acid
kynurenic acid + 2-aminohexanoate
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
-
very low activity with 2-oxogltarate
-
-
?
L-kynurenine + 2-oxohexanoate
kynurenic acid + L-norleucine + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisocaproate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-leucine
-
-
-
-
?
L-kynurenine + 2-oxoisocaproic acid
4-(2-aminophenyl)-2,4-dioxobutanoate + L-leucine
-
-
-
?
L-kynurenine + 2-oxoisopentanoate
kynurenic acid + 2-aminoisopentanoate + H2O
-
poor substrate
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
kynurenic acid + L-isoleucine + H2O
-
poor substrate
-
?
L-kynurenine + 4-methyl-2-oxovalerate
kynurenic acid + 2,4-dimethylvalerate + H2O
5.9% of activity with 2-oxoglutarate
-
?
L-kynurenine + mercaptopyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine
-
-
-
-
?
L-kynurenine + oxaloacetate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminosuccinate
-
-
-
-
?
L-kynurenine + oxaloacetate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-aspartate
-
moderate activity
-
-
?
L-kynurenine + pyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-alanine
-
moderate activity
-
-
?
L-kynurenine + pyruvate
4-(2-aminophenyl)-2,4-dioxobutanoic acid + L-alanine
-
-
-
-
ir
L-kynurenine + pyruvate
4-(2-aminophenyl)2,4-dioxobutanoate + L-alanine
-
-
-
-
?
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
at about 30% the rate of L-kynurenine
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxobutanoate
3-hydroxy-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-vinylglycine
2-oxobutyrate + NH3
Hansenula schneggii
-
deamination at 1% the rate of kynurenine, suicide substrate
-
?
L-vinylglycine + 1-propanethiol
S-n-propylhomocysteine
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
-
?
L-vinylglycine + 2-oxobutyrate
2-aminobutyrate + 2-oxo-3-butenoate
Hansenula schneggii
-
-
-
?
L-vinylglycine + ethanethiol
ethionine
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
i.e. S-ethylhomocysteine
?
L-vinylglycine + methanethiol
methionine
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
-
?
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
-
-
-
?
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
Hansenula schneggii
-
at about 45% the rate of L-kynurenine
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
ir
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
no activity with D-isomer
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
KAT I, no good substrate
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
Q95VY4
-
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
-
-
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
-
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
-
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenate + L-methionine
-
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenate + L-methionine
-
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
Q95VY4
25% of activity with pyruvate
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
91% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
Hansenula schneggii
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
28% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxocaproate
?
-
high activity, 2-oxocaproate is the best cosubstrate
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
-
-
-
ir
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenate + L-glutamate + H2O
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Q95VY4
31% of activity with pyruvate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
broad specificity
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
best substrates
via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
initial reaction in quinaldine pathway of kynurenine catabolism
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Hansenula schneggii
-
inducible enzyme of tryptophan catabolism
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
KAT I shows far higher activity with 2-oxoisohexanoate than with 2-oxoglutarate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
highest activity with aspartate and glutamate as substrate, but also active with other amino acids
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
no activity with D-kynureinine
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
broad specificity
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
best substrates
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
soluble kidney/brain kynurenine aminotransferase has both amino transferase and cysteine conjugate beta-lyase, i.e., glutamine transaminase K activities
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
KAT II shows equal activity with 2-oxoglutarate and pyruvate, KAT I shows lower activity with 2-oxoglutarate than with pyruvate, ratio of KAT I to KAT II in normal brain is approx. 1/4
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
enzyme has both kynurenine aminotransferase and alpha-aminoadipate aminotransferase activity
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
enzyme has both kynurenine aminotransferase and glutamine transaminase K activity
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
isoenzyme 2, no activity with L-tyrosine, L-phenylalanine, L-tryptophan, 5-hydroxy-L-tryptophan and L-aspartate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
inducible enzyme of tryptophan catabolism
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
isoenzyme 2, no activity with L-tyrosine, L-phenylalanine, L-tryptophan, 5-hydroxy-L-tryptophan and L-aspartate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
Saccharomyces fragilis
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
-
KAT I shows far higher activity with 2-oxoisohexanoate than with 2-oxoglutarate
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
-
heart KAT, low activity
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxopentanoate
kynurenic acid + L-norvaline + H2O
Hansenula schneggii
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxopentanoate
kynurenic acid + L-norvaline + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 3-indole-2-oxopropanoate
kynurenic acid + L-tryptophan + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 3-indole-2-oxopropanoate
kynurenic acid + L-tryptophan + H2O
-
-
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
Hansenula schneggii
-
-
-
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
-
-
-
?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
kynurenic acid + L-methionine + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
kynurenic acid + L-methionine + H2O
Hansenula schneggii
-
-
-
?
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
-
-
-
-
?
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
glyoxylate shows a relatively low affinity for KAT II
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
2-oxobutyrate is also a co-substrate
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
alpha-ketobutyrate is also a co-substrate
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
-
poor substrate
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
-
poor substrate
-
?
L-kynurenine + oxaloacetate
kynurenate + L-aspartate + H2O
-
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
Q95VY4
90% of activity with pyruvate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
-
-
-
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
-
high activity
-
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
43% of activity with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
Q95VY4
best amino acceptor
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
placental KAT I, higher activity than with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
best substrate of heart KAT
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
KAT I shows far higher activity with 2-oxoisohexanoate and pyruvate than with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
3% of activity with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
100fold higher maximal velocity than with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
less effective than 2-oxoglutarate
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Hansenula schneggii
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
Hansenula schneggii
-
at about 85% the rate of L-kynurenine
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
-
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
Hansenula schneggii
-
at about 36% the rate of L-kynurenine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
-
12% the rate of L-kynurenine
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
Hansenula schneggii
-
at about 60% the rate of L-kynurenine
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
poor substrate
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
-
16% the rate of L-kynurenine
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
?
additional information
?
-
the purified recombinant KAT shows dose-dependent inhibition effect on the growth of equine babesial parasite, Babesia caballi, in in vitro culture
-
-
?
additional information
?
-
no activity towards L-tryptophan and pyruvic acid
-
-
?
additional information
?
-
-
very bad substrate: L-glycine, L-alanine, L-arginine, L-serine, L-lysine, no substrate: l-threonine, L-isoleucine, L-aspartate, L-glutamate, L-valine, L-aminoadipate
-
-
?
additional information
?
-
2-oxoglutarate, 2-oxocaproate, phenylpyruvate, and 2-oxo-4-methylthiobutyrate are highly efficient as amino-group acceptors for KAT II
-
-
?
additional information
?
-
-
2-oxoglutarate, 2-oxocaproate, phenylpyruvate, and 2-oxo-4-methylthiobutyrate are highly efficient as amino-group acceptors for KAT II
-
-
?
additional information
?
-
3-indolepropionic acid and DL-indole-3-lactic acid are no substrates of kynurenine aminotransferase I
-
-
?
additional information
?
-
-
3-indolepropionic acid and DL-indole-3-lactic acid are no substrates of kynurenine aminotransferase I
-
-
?
additional information
?
-
-
KAT I is most active with large neutral/aromatic/sulfur-containing amino acids, including L-glutamine, L-phenylalanine, L-leucine, L-kynurenine, L-tryptophan, L-methionine, L-tyrosine, L-histidine, L-cysteine, aminobutyrate, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, and S-(1,2-dichlorovinyl)-L-cysteine. The enzyme has detectable activity with Se-methylselenocysteine, 5-S-cysteinyldopamine, 5-S-cysteinyl-DOPA, L-asparagine, glycine, L-alanine, L-arginine, L-serine, and L-lysine. KAT I can use many 2-oxo acids as its amino group acceptors: 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, 2-oxo-4-methylthiobutyrate, mercaptopyruvate, indol-3-ylpyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate. All of them demonstrate the capacity to act as amino group acceptors, but 2-oxoglutarate, 2-oxoiosleucine, indo-3-pyruvate, 2-oxoadipate, and 2-oxovaline have very low activity. Although the activity of KAT I using oxaloacetate, phenylpyruvate, or pyruvate as an amino group acceptor is detectable, the specific activity with these three 2-oxo acids is so low that they are unlikely to be physiological co-substrates for human KAT I
-
-
?
additional information
?
-
-
KAT II is efficient in catalyzing the transamination of aminoadipate, L-kynurenine, L-methionine, and L-glutamate, and is less efficient in catalyzing L-tyrosine, L-phenylalanine, L-tryptophan, L-leucine, 3-hydroxykynurenine, L-glutamine, L-alanine, and aminobutyrate. KAT II is efficient in catalyzing the transamination of 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, and 2-oxo-4-methylthiobutyrate, and less efficient in catalyzing mercaptopyruvate, indol-3-ylpyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate (in order of decreasing catalytic efficiency)
-
-
?
additional information
?
-
-
KAT III shows activity towards L-phenylalanine, L-kynurenine, L-tryptophan, 3-hydroxykynurenine, L-tyrosine, and L-histidine, L-methionine and L-cysteine, L-glutamine, L-asparagine, L-serine, L-alanine, aminobutyrate, and L-lysine. Glyoxylate, 2-oxocaproic acid, phenylpyruvate, 2-oxobutyrate, 2-oxo-4-methylthiobutyrate, 2-oxovalerate, indol-3-ylpyruvate, p-hydroxyphenylpyruvate, mercaptopyruvate, and oxaloacetate are good amino group acceptors for KAT III and pyruvate, phenylpyruvate, while 2-oxoglutarate are poor co-substrates for the enzyme
-
-
?
additional information
?
-
-
KAT IV shows high transamination activity towards L-glutamate, L-aspartate, L-phenylalanine, L-tyrosine, and L-cysteine, and detectable activity towards L-tryptophan, 3-hydroxykynurenine, L-methionine, L-kynurenine, and L-asparagine. It can use 2-oxoglutarate, phenylpyruvate, 2-oxo-4-methylthiobutyrate, indol-3-ylpyruvate, hydroxyphenylpyruvate, mercaptopyruvate, 2-oxocaproic acid, oxaloacetate, 2-oxobutyrate, pyruvate, and glyoxylate as amino group acceptors. It also shows detectable activity towards other co-substrates, including 2-oxovalerate, 2-oxoleucine, 2-oxoadipate, 2-oxovaline, and 2-oxoisoleucine
-
-
?
additional information
?
-
human KAT III/CCBL2 possesses cysteine S-conjugate beta-lyase activity, EC 4.4.1.13. KAtT III and glutamine transaminase L are identical enzymes
-
-
?
additional information
?
-
-
human KAT III/CCBL2 possesses cysteine S-conjugate beta-lyase activity, EC 4.4.1.13. KAtT III and glutamine transaminase L are identical enzymes
-
-
?
additional information
?
-
-
KAT I is most active with large neutral/aromatic/sulfur-containing amino acids, including L-glutamine, L-phenylalanine, L-leucine, L-kynurenine, L-tryptophan, L-methionine, L-tyrosine, L-histidine, L-cysteine, aminobutyrate, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, and S-(1,2-dichlorovinyl)-L-cysteine. The enzyme has detectable activity with Se-methylselenocysteine, 5-S-cysteinyldopamine, 5-S-cysteinyl-DOPA, L-asparagine, glycine, L-alanine, L-arginine, L-serine, and L-lysine. KAT I can use many 2-oxo acids as its amino group acceptors: 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, 2-oxo-4-methylthiobutyrate, mercaptopyruvate, indo-3-pyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate. All of them demonstrate the capacity to act as amino group acceptors, but 2-oxoglutarate, 2-oxoiosleucine, indol-3-ylpyruvate, 2-oxoadipate, and 2-oxovaline have very low activity. Although the activity of KAT I using oxaloacetate, phenylpyruvate, or pyruvate as an amino group acceptor is detectable, the specific activity with these three 2-oxo acids is so low that they are unlikely to be physiological co-substrates for human KAT I
-
-
?
additional information
?
-
-
KAT II is efficient in catalyzing the transamination of aminoadipate, L-kynurenine, L-methionine, and L-glutamate, and is less efficient in catalyzing L-tyrosine, L-phenylalanine, L-tryptophan, L-leucine, 3-hydroxykynurenine, L-glutamine, L-alanine, and aminobutyrate. KAT II is efficient in catalyzing the transamination of 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, and alpha-oxo-gamma-methiol-butyric acid, and less efficient in catalyzing mercaptopyruvate, indol-3-ylpyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate (in order of decreasing catalytic efficiency)
-
-
?
additional information
?
-
KAT III does not use L-valine, L-proline, L-threonine, L-leucine, L-isoleucine, L-glutamate, L-aspartate, L-arginine, and aminoadipate as substrates
-
-
?
additional information
?
-
-
KAT III does not use L-valine, L-proline, L-threonine, L-leucine, L-isoleucine, L-glutamate, L-aspartate, L-arginine, and aminoadipate as substrates
-
-
?
additional information
?
-
-
KAT III shows activity towards L-phenylalanine, L-kynurenine, L-tryptophan, 3-hydroxykynurenine, L-tyrosine, and L-histidine, L-methionine and L-cysteine, L-glutamine, L-asparagine, L-serine, L-alanine, aminobutyrate, and L-lysine. Glyoxylate, 2-oxocaproic acid, phenylpyruvate, 2-oxobutyrate, alpha-oxo-gamma-methiol-butyric acid, 2-oxovalerate, indo-3-pyruvate, p-hydroxyphenylpyruvate, mercaptopyruvate, and oxaloacetate are good amino group acceptors for KAT III and pyruvate, phenylpyruvate, while 2-oxoglutarate are poor co-substrates for the enzyme
-
-
?
additional information
?
-
-
KAT IV shows high transamination activity towards L-glutamate, L-aspartate, L-phenylalanine, L-tyrosine, and L-cysteine, and detectable activity towards L-tryptophan, 3-hydroxykynurenine, L-methionine, L-kynurenine, and L-asparagine. It can use 2-oxoglutarate, phenylpyruvate, 2-oxo-4-methylthiobutyrate, indol-3-ylpyruvate, hydroxyphenylpyruvate, mercaptopyruvate, 2-oxocaproic acid, oxaloacetate, 2-oxobutyrate, pyruvate, and glyoxylate as amino group acceptors. It also shows detectable activity towards other co-substrates, including 2-oxovalerate, 2-oxoleucine, 2-oxoadipate, 2-oxovaline, and 2-oxoisoleucine
-
-
?
additional information
?
-
-
cosubstrate specificity, overview. No or poor activity with 2-oxoadipate and 2-oxoisoleucine. Recombinant mouse KAT3/GTL selectively metabolizes selenomethionine to 2-oxo-gamma-methylselenobutyrate, KAT3/GTLis more efficient in transamination of both than is KAT1/GTK
-
-
-
additional information
?
-
-
KAT I is most active with large neutral/aromatic/sulfur-containing amino acids, including L-glutamine, L-phenylalanine, L-leucine, L-kynurenine, L-tryptophan, L-methionine, L-tyrosine, L-histidine, L-cysteine, aminobutyrate, S-(1,1,2,2-tetrafluoroethyl)-L-cysteine, and S-(1,2-dichlorovinyl)-L-cysteine. The enzyme has detectable activity with Se-methylselenocysteine, 5-S-cysteinyldopamine, 5-S-cysteinyl-DOPA, L-asparagine, glycine, L-alanine, L-arginine, L-serine, and L-lysine. KAT I can use many 2-oxo acids as its amino group acceptors: 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, 2-oxo-4-methylthiobutyrate, mercaptopyruvate, indol-3-ylpyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate. All of them demonstrate the capacity to act as amino group acceptors, but 2-oxoglutarate, 2-oxoisoleucine, indol-3-ylpyruvate, 2-oxoadipate, and 2-oxovaline have very low activity. Although the activity of KAT I using oxaloacetate, phenylpyruvate, or pyruvate as an amino group acceptor is detectable, the specific activity with these three 2-oxo acids is so low that they are unlikely to be physiological co-substrates for human KAT I
-
-
?
additional information
?
-
-
KAT II is efficient in catalyzing the transamination of aminoadipate, L-kynurenine, L-methionine, and L-glutamate, and is less efficient in catalyzing L-tyrosine, L-phenylalanine, L-tryptophan, L-leucine, 3-hydroxykynurenine, L-glutamine, L-alanine, and aminobutyrate. KAT II is efficient in catalyzing the transamination of 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate, and 2-oxo-4-methylthiobutyrate, and less efficient in catalyzing mercaptopyruvate, indol-3-ylpyruvate, 2-oxovalerate, 2-oxoleucine, 2-oxobutyrate, p-hydroxyphenylpyruvate, 2-oxoadipate, glyoxylate, oxaloacetate, 2-oxovaline, 2-oxoisoleucine, and pyruvate (in order of decreasing catalytic efficiency)
-
-
?
additional information
?
-
-
KAT III shows activity towards L-phenylalanine, L-kynurenine, L-tryptophan, 3-hydroxykynurenine, L-tyrosine, and L-histidine, L-methionine and L-cysteine, L-glutamine, L-asparagine, L-serine, L-alanine, aminobutyrate, and L-lysine. Glyoxylate, 2-oxocaproic acid, phenylpyruvate, 2-oxobutyrate, 2-oxo-4-methylthiobutyrate, 2-oxovalerate, indol-3-ylpyruvate, p-hydroxyphenylpyruvate, mercaptopyruvate, and oxaloacetate are good amino group acceptors for KAT III and pyruvate, phenylpyruvate, while 2-oxoglutarate are poor co-substrates for the enzyme
-
-
?
additional information
?
-
-
KAT IV shows high transamination activity towards L-glutamate, L-aspartate, L-phenylalanine, L-tyrosine, and L-cysteine, and detectable activity towards L-tryptophan, 3-hydroxykynurenine, L-methionine, L-kynurenine, and L-asparagine. It can use 2-oxoglutarate, phenylpyruvate, 2-oxo-4-methylthiobutyrate, indol-3-ylpyruvate, hydroxyphenylpyruvate, mercaptopyruvate, 2-oxocaproic acid, oxaloacetate, 2-oxobutyrate, pyruvate, and glyoxylate as amino group acceptors. It also shows detectable activity towards other co-substrates, including 2-oxovalerate, 2-oxoleucine, 2-oxoadipate, 2-oxovaline, and 2-oxoisoleucine
-
-
?
