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Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase
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2.6.1.7 kynurenine-oxoglutarate transaminaseIUBMB 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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- 2.6.1.7
-
alt
- bilirubin
- cholesterol
- creatinine
- necrosis
- albumin
- triglyceride
- urea
- fibrosis
-
hepatotoxicity
- dismutase
- hepatocytes
- malondialdehyde
- cirrhosis
-
hepatoprotective
- platelet
- gsh
- sod
-
enrol
- wistar
-
gamma-glutamyl
- hemoglobin
- bile
- lipoprotein
- catalase
-
nonalcoholic
- ischemia
-
portal
-
c-reactive
- nafld
- gamma-glutamyltransferase
-
tetrachloride
- hematological
- steatosis
- ccl4
-
reperfusion
- transpeptidase
- prothrombin
- transaminases
-
jaundice
-
ccl4-induced
-
hematocrit
-
phosphokinase
- globulin
- steatohepatitis
-
corpuscular
-
admission
-
glutamyl
-
tetrachloride-induced
- silymarin
- analysis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
aspartate aminotransferase, mitochondrial aspartate aminotransferase, kat ii, kat i, kynurenine aminotransferase ii, aadat, kat-i, kat-ii, kynurenine aminotransferase i, kynurenine-oxoglutarate transaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
KAT
KAT I
KAT II
KAT III
KAT IV
KAT-I
kynurenine aminotransferase
kynurenine aminotransferase I
kynurenine aminotransferase II
kynurenine aminotransferase III
kynurenine aminotransferase-I
PhKAT
type II kynurenine aminotransferase
additional information
additional information
-
brain KAT I is identical with glutamine transferase K
additional information
-
enzyme from mitochondria may be identical with EC 2.6.1.39
additional information
-
identical to kidney soluble cysteine conjugate beta-lyase, EC 2.6.1.64, also referred to as glutamine transaminase K, EC 2.6.1.15, K stands for kidney
additional information
-
enzyme from mitochondria may be identical with EC 2.6.1.39
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
mechanism
Hansenula schneggii
-
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
transamination of the amino acid to a transient keto acid intermediate which spontaneously undergoes ring closure
-
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9030-38-0
-
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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-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 + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
-
-
-
?
L-kynurenine + phenylpyruvate
phenylalanine + L-glutamate + H2O
43% of activity with 2-oxoglutarate
-
?
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
-
-
?
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
-
?
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
-
-
?
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
-
-
?
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
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
-
-
?
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-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
kynurenic acid + L-glutamate
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
highest activity with aspartate and glutamate as substrate, but also active with other amino acids
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
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
-
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
-
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
2-oxobutyrate is also a co-substrate
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine
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
kynurenic acid + L-aspartate + H2O
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 + pyruvate
kynurenic acid + L-alanine + H2O
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
-
-
?
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
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
-
-
?
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
-
-
?
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
?
-
-
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
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
the purified recombinant KAT shows dose-dependent inhibition effect on the growth of equine babesial parasite, Babesia caballi, in in vitro culture
-
-
?
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
-
inducible enzyme of tryptophan catabolism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes, crystallization data
pyridoxal 5'-phosphate
a highly conserved pyridoxal 5'-phosphate binding site (Gly-Ser-Ala-Gly-Lys-Thr-Phe-Ser) is located between Gly-219 and Ser-226
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
not activated by chloride salts of Mg2+, Mn2+, Na+, K+ or NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3S)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
-
(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
(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
(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
3-Methyl-2-benzothiazolone hydrazone hydrochloride
Hansenula schneggii
-
0.1 mM, complete inhibition, reversible by pyridoxal phosphate
amino-2,3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid
-
inhibitory in whole cells
cysteine sulfinate
-
poor substrate that undergoes slow transamination, KM-value 12.3 mM, pH 7.5, 25°C
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
L-Cycloserine
Hansenula schneggii
-
0.1 mM, 88% inhibition, reversible by pyridoxal phosphate
L-cysteate
-
5.38 mM, 50% inhibition of brain KAT I, 1.55 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-Penicillamine
Hansenula schneggii
-
0.1 mM, 62% inhibition, reversible by pyridoxal phosphate
phenylhydrazine
Hansenula schneggii
-
0.1 mM, 81% inhibition, reversible by pyridoxal phosphate
quinolinic acid
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
Quisqualic acid
-
1 mM, isoform KAT I, 81% residual activity, isoform KAT II, 1% residual activity
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
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
-
i.e. PF-04859989, selective inhibitor
2-oxoglutarate
-
inhibited by high concentrations, allosterically regulated
3-hydroxykynurenine
-
0.6 mM, 54% inhibition of KAT I, 88% inhibition of KAT II
glutamine
-
strong inhibition of KAT I, phenylpyruvate, 2-oxo-4-methiolbutyrate or 2-oxo-isocaproate protect
L-aspartate
-
0.72 mM, 50% inhibition of brain KAT I, 0.073 mM, 50% inhibition of brain KAT II
L-cysteine
-
5 mM decreases KAT II activity; inhibition of human KAT I activity at 2 mM
L-glutamate
-
1.3 mM, 50% inhibition of brain KAT I, 0.79 mM, 50% inhibition of brain KAT II
L-phenylalanine
-
5 mM decreases KAT II activity; inhibition of KAT I activity at 2 mM
L-tryptophan
-
1 mM, isoform KAT I, 3% residual activity, isoform KAT II, 129% activity
additional information
-
KAT II is not inhibited by glutamine, tryptophan and phenylalanine
-
additional information
-
(S)-(4)-(ethylsulfonyl)benzoylalanine shows no inhibition (inhibitor of the rat enzyme)
-
additional information
-
KAT III is not inhibited by 5 mM tryptophan; KAT I is not inhibited by 5 mM L-methionine
-
additional information
indol-3ylpyruvate shows no noticeable inhibition of KAT III
-
additional information
-
indol-3ylpyruvate shows no noticeable inhibition of KAT III
-
additional information
-
not inhibited by L-3-hydroxykynurenine at higher concentrations
-
additional information
-
not inhibited by aspartate, tyrosine, phenylalanine
-
additional information
-
not inhibited by EGTA; not inhibited by quinolinate
-
additional information
-
not inhibited by 2-aminoadipate; not inhibited by oxaloacetic acid, 3-methylglutaric acid
-
additional information
-
not inhibited by antibodies against 2-aminoadipate transaminase
-
additional information
-
not inhibited by glycerol, DTT, up to 10%, tryptophan, 3-hydroxyanthranilate, picolinate, NAD+, NADH, NADP+, NADPH, serotonin, tryptamine, 5-hydroxytryptophan, indole-3-acetate, organic acids of tricarboxylic acid cycle, glyoxylate, pyruvate, glutamine, Mg2+, Ca2+, Mn2+, monovalent cations; not inhibited by quinolinate
-
additional information
-
brain KAT I is not inhibited by quiqualate, 4-carboxy-3-hydroxyphenylglycine, L-2-amino-4-phosphonobutyric acid, L-serine-O-phosphate, and trans-pyrrolidine-2,4-dicarboxylate
-
additional information
-
brain KAT I is not inhibited by L-cysteine sulfinate and L-homocysteine sulfinate
-
additional information
-
no influence on kynurenic acid synthesis: K+, 4-aminopyridine, N-methyl-D-aspartate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2062
3-hydroxykynurenine
in 200 mM phosphate buffer, pH 7.5, at 37°C
3.3
4-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.4
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
5.6
L-glutamate
pH 8.0, 37°C, alpha-aminoadipate aminotransferase activity
0.00438
2-oxo-4-methylthiobutyrate
in 200 mM phosphate buffer, pH 7.5, at 37°C
2.4
2-oxo-4-methylthiobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.000217
2-oxobutyrate
in 200 mM phosphate buffer, pH 7.5, at 37°C
12.7
2-oxobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.045
2-oxoglutarate
pH 8.0, 37°C, recombinant enzyme, cosubstrate L-kyrunenine
1.2
2-oxoglutarate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.2
2-oxoglutarate
-
pH not specified in the publication, temperature not specified in the publication
12.9
3-methyl-2-oxobutanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
14.2
3-methyl-2-oxobutanoate
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
0.083
L-kynurenine
-
pH 8.0, 37°C, recombinant enzyme, cosubstrate 2-oxoglutarate
0.1116
L-kynurenine
in 200 mM phosphate buffer, pH 7.5, at 37°C
0.68
L-kynurenine
mass spectrometry assay, pH 7.5, temperature not specified in the publication
2.8
Mercaptopyruvate
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
additional information
additional information
-
isoform KAT I, vitreous body, 0.25 pM/g wet tissue/hour, retina, 1.65, isoform KAT II, vitreous body, 0.25 pM/g wet tissue/hour, retina 2.37
-
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
-
additional information
additional information
-
isoform KAT I, vitreous body, 0.82 pM/g wet tissue/hour, retina, 0.39, isoform KAT II, vitreous body, 1.05 pM/g wet tissue/hour, retina 1.88
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.83
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
65.12
3-hydroxykynurenine
in 200 mM phosphate buffer, pH 7.5, 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
1.02
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.16
2-oxo-4-methylthiobutyrate
in 200 mM phosphate buffer, pH 7.5, at 37°C
4.27
2-oxo-4-methylthiobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0018
2-oxobutyrate
in 200 mM phosphate buffer, pH 7.5, at 37°C
3.49
2-oxobutyrate
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
0.39
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
L-kynurenine
mass spectrometry assay, pH 7.5, temperature not specified in the publication
55.5
L-kynurenine
in 200 mM phosphate buffer, pH 7.5, at 37°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.13
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
315
3-hydroxykynurenine
in 200 mM phosphate buffer, pH7.5, at 37°C
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
36.8
alpha-keto-gamma-methylthiobutyrate
in 200 mM phosphate buffer, pH7.5, at 37°C
2.54
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.75
2-oxo-4-methylthiobutyrate
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
8.2
2-oxobutyrate
in 200 mM phosphate buffer, pH7.5, 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
0.27
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
6.8
L-kynurenine
mass spectrometry assay, pH 7.5, temperature not specified in the publication
1.23
Mercaptopyruvate
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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