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2-aminobutyrate + glyoxylate
?
-
-
-
?
3,5-diiodo-L-tyrosine + 2-oxoglutarate
3-(2,5-diiodo-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
slightly better than L-kynurenine
-
?
3-hydroxy-DL-kynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate + H2O
3-hydroxykynurenine + glyoxylate
?
-
-
-
?
3-hydroxykynurenine + pyruvate
?
-
-
-
?
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-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
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-alanine + 2-oxobutanoate
pyruvate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-alanine + glyoxylate
?
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
L-asparagine + glyoxylate
?
KAT II has high transamination activity toward L-asparagine
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
L-cysteine + 2-oxobutanoate
? + 2-aminobutanoate
Q95VY4
-
-
-
?
L-cysteine + glyoxylate
?
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
L-glutamine + glyoxylate
?
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
-
-
?
L-histidine + glyoxylate
?
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenate + L-methionine
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenic acid + L-methionine
-
-
-
?
L-kynurenine + 2-oxoadipate
?
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
L-kynurenine + 2-oxobutyrate
?
L-kynurenine + 2-oxobutyrate
kynurenate + ?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
L-kynurenine + 2-oxocaproate
?
L-kynurenine + 2-oxocaproic acid
?
-
-
-
?
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-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate + H2O
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
L-kynurenine + 2-oxoglutarate
?
poor cosubstrate for KAT III
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenate + L-glutamate + H2O
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
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-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
L-kynurenine + 2-oxoisopentanoate
kynurenic acid + 2-aminoisopentanoate + H2O
-
poor substrate
-
?
L-kynurenine + 2-oxoleucine
?
-
moderate activity
-
-
?
L-kynurenine + 2-oxomethylthiobutyric acid
?
-
-
-
?
L-kynurenine + 2-oxopentanoate
kynurenic acid + L-norvaline + H2O
L-kynurenine + 2-oxovalerate
?
L-kynurenine + 2-oxovalerate
kynurenic acid + 2-aminopentanoate
-
-
-
?
L-kynurenine + 2-oxovaline
?
-
low activity
-
-
?
L-kynurenine + 3-indole-2-oxopropanoate
kynurenic acid + L-tryptophan + H2O
L-kynurenine + 3-methyl-2-oxobutanoate
?
-
-
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
?
-
-
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
kynurenic acid + L-isoleucine + H2O
-
poor substrate
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
L-kynurenine + 4-methyl-2-oxopentanoate
?
-
-
-
?
L-kynurenine + 4-methyl-2-oxovalerate
kynurenic acid + 2,4-dimethylvalerate + H2O
5.9% of activity with 2-oxoglutarate
-
?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
kynurenic acid + L-methionine + H2O
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
L-kynurenine + glyoxylate
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
L-kynurenine + hydroxyphenylpyruvate
?
L-kynurenine + hydroxyphenylpyruvate
kynurenic acid + L-tyrosine
-
-
-
?
L-kynurenine + indo-3-pyruvate
?
-
-
-
?
L-kynurenine + indol-3-pyruvate
?
-
moderate activity
-
-
?
L-kynurenine + indol-3-ylpyruvate
?
-
-
-
?
L-kynurenine + indole-3-pyruvate
kynurenic acid + L-tryptophan
-
-
-
?
L-kynurenine + mercaptopyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine
-
-
-
-
?
L-kynurenine + mercaptopyruvate
?
L-kynurenine + mercaptopyruvate
kynurenic acid + ?
-
-
-
?
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 + oxaloacetate
?
L-kynurenine + oxaloacetate
kynurenate + L-aspartate + H2O
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
L-kynurenine + p-hydroxyphenylpyruvate
?
-
-
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
L-kynurenine + phenylpyruvate
?
L-kynurenine + phenylpyruvate
kynurenic acid + L-phenylalanine
-
-
-
?
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-kynurenine + pyruvate
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
L-leucine + 2-oxobutanoate
2-oxoisocaproate + 2-aminobutanoate
-
-
-
-
?
L-leucine + 2-oxobutanoate
alpha-ketoleucine + 2-aminobutanoate
Q95VY4
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
L-lysine + glyoxylate
?
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
L-methionine + glyoxylate
?
-
-
-
?
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
at about 30% the rate of L-kynurenine
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
-
-
-
?
L-phenylalanine + glyoxylate
?
-
-
-
?
L-serine + 2-oxobutanoate
3-hydroxy-2-oxopropanoate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-serine + glyoxylate
?
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
L-tryptophan + glyoxylate
?
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
L-tyrosine + glyoxylate
?
-
-
-
?
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
-
?
additional information
?
-
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-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-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
Q95VY4
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
-
-
-
-
?
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
?
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
?
-
-
-
?
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
?
-
-
-
?
L-kynurenine + 2-oxobutyrate
?
-
high activity
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenate + ?
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenate + ?
-
-
-
-
?
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
-
-
-
?
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
?
-
-
-
?
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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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 + 2-oxovalerate
?
-
-
-
?
L-kynurenine + 2-oxovalerate
?
-
-
-
?
L-kynurenine + 2-oxovalerate
?
-
high activity
-
-
?
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
?
-
-
-
?
L-kynurenine + glyoxylate
?
-
high activity
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
-
-
-
?
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 + hydroxyphenylpyruvate
?
-
-
-
?
L-kynurenine + hydroxyphenylpyruvate
?
-
moderate activity
-
-
?
L-kynurenine + mercaptopyruvate
?
-
-
-
?
L-kynurenine + mercaptopyruvate
?
-
-
-
?
L-kynurenine + mercaptopyruvate
?
-
moderate activity
-
-
?
L-kynurenine + oxaloacetate
?
-
-
-
?
L-kynurenine + oxaloacetate
?
-
-
-
?
L-kynurenine + oxaloacetate
kynurenate + L-aspartate + H2O
-
-
-
-
?
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
-
-
-
?
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 + phenylpyruvate
?
-
-
-
?
L-kynurenine + phenylpyruvate
?
-
-
-
?
L-kynurenine + phenylpyruvate
?
poor cosubstrate for KAT III
-
-
?
L-kynurenine + pyruvate
?
-
-
-
?
L-kynurenine + pyruvate
?
poor cosubstrate for KAT III
-
-
?
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
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
-
-
?
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-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
-
-
-
-
?
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
?
-
-
does not use D-kynurenine as substrate
-
-
?
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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(2R)-2-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-3-phenylpropanoic acid
-
(2S)-2-(5,6-dichloro-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)-3-phenylpropanoic acid
reversible inhibitor
(2S)-2-amino-4-[4-(ethylsulfonyl)phenyl]-4-oxobutanoic acid
reversible inhibitor
(3R)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
irreversible inhibitor
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
(3S)-3-amino-6-benzyl-1-hydroxy-7-methoxy-3,4-dihydroquinolin-2(1H)-one
-
(5S)-5-amino-7-hydroxy-2-phenyl-2,4,5,7-tetrahydro-6H-pyrazolo[3,4-b]pyridin-6-one
irreversible inhibitor
(5Z)-5-[3-(4-oxo-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-7-yl)benzylidene]-1,3-thiazolidine-2,4-dione
reversible inhibitor
-
(6R)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6R)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-8-cyclopropyl-N-(3,5-dimethylphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-8-cyclopropyl-N-(4-methoxyphenyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-N-(3-chloro-4-fluorophenyl)-8-(cyclopropylmethyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(6S)-N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
(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)-(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
3,5-difluoro-N-[5-(1-phenylcyclopropyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
3,5-difluoro-N-{5-[(2R)-2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3,5-difluoro-N-{5-[(2S)-2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3,5-difluoro-N-{5-[2-(3-fluorophenyl)-3-methylbutyl]-1,3,4-thiadiazol-2-yl}benzenesulfonamide
-
3-(2-carboxyethyl)-5-chloro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
-
3-Methyl-2-benzothiazolone hydrazone hydrochloride
Hansenula schneggii
-
0.1 mM, complete inhibition, reversible by pyridoxal phosphate
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)benzenesulfonamide
reversible inhibitor
4-(5,6-dichloro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethylbenzenesulfonamide
reversible inhibitor
4-carboxy-3-hydroxyphenylglycine
-
inhibition of brain KAT II
4-chloro-N-(pyrrolidin-3-yl)-2-(trifluoromethyl)benzenesulfonamide
-
5-(2-(3-chlorophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-(2-(4-bromophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-(2-(4-chlorophenyl) hydrazono)-6-ethoxy-6-oxohexanoic acid
-
-
5-bromo-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
-
-
6-ethoxy-5-(2-(4-iodophenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-5-(2-(4-methoxyphenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-5-(2-(4-nitrophenyl)hydrazono)-6-oxohexanoic acid
-
-
6-ethoxy-6-oxo-5-(2-p-tolylhydrazono)hexanoic acid
-
-
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
aminooxyphenylpropionic acid
-
anthranilate
-
weak inhibition
carbenoxolone
highly selective and competitive inhibitor for isoform KAT2
cysteine sulfinate
-
poor substrate that undergoes slow transamination, KM-value 12.3 mM, pH 7.5, 25°C
dimethylglutaric acid
-
-
EGTA
-
strong inhibition at pH 6.8 and Ca2+ concentrations below 0.5 mM
Estrone sulfate
weak inhibitor
glycyrrhetinic acid
highly selective and competitive inhibitor for isoform KAT2
glycyrrhizic acid
highly selective and competitive inhibitor for isoform KAT2
Indole-3-pyruvate
-
5 mM, 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- glutamate
-
5 mM decreases KAT II activity
L-2-amino-4-phosphonobutyric acid
-
inhibition of brain KAT II
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-cysteine sulfinate
-
0.002 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-Penicillamine
Hansenula schneggii
-
0.1 mM, 62% inhibition, reversible by pyridoxal phosphate
L-serine-O-phosphate
-
inhibition of brain KAT II
N-(3-chloro-4-methylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
N-(3-ethylphenyl)-8-(3-methylbutyl)-9-oxo-2,8-diazaspiro[5.5]undecane-2-carboxamide
-
N-benzyl-1-[6-methyl-5-(oxan-4-yl)-7-oxo-6,7-dihydro[1,3]thiazolo[5,4-d]pyrimidin-2-yl]-D-prolinamide
reversible inhibitor
N-ethylmaleimide
Hansenula schneggii
-
-
N-omega-nitro-L-arginine
-
-
N-[5-(cyclopentylmethyl)-1,3,4-oxadiazol-2-yl]benzenesulfonamide
-
nicotinate
-
weak inhibition
NS-1502
reversible inhibitor; reversible inhibitor
phenylhydrazine
Hansenula schneggii
-
0.1 mM, 81% inhibition, reversible by pyridoxal phosphate
pyridoxal 5'-phosphate
-
at high concentrations
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
S-4-(ethylsulfonyl)benzoyl-L-alanine
S-dichlorovinyl-L-cysteine
Sulfate or phosphate esters of steroids
-
-
-
trans-3-indolacrylic acid
-
trans-pyrrolidine-2,4-dicarboxylate
-
inhibition of brain KAT II
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
xanthurenate
-
weak inhibition
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
-
(3S)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one
irreversible inhibitor
(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
2-oxoglutarate
-
substrate inhibition
3-hydroxykynurenine
less than 35% inhibition at 5 mM
3-hydroxykynurenine
-
5 mM decreases KAT II activity
3-hydroxykynurenine
-
2 mM, 50% inhibition of KAT I activity
3-hydroxykynurenine
-
0.6 mM, 54% inhibition of KAT I, 88% inhibition of KAT II
3-indolepropionic acid
-
specific inhibition of KAT I activity
4-chloromercuribenzoate
Hansenula schneggii
-
1 mM, 78% inhibition
4-chloromercuribenzoate
Hansenula schneggii
-
-
4-chloromercuribenzoate
-
-
adipate
Hansenula schneggii
-
10 mM, 39% inhibition
adipate
-
strong inhibition
aminoadipate
less than 35% inhibition at 5 mM
aminoadipate
-
5 mM decreases KAT II activity
BFF-122
irreversible inhibitor
BFF-122
irreversible inhibitor; irreversible inhibitor
BFF-816
reversible inhibitor; reversible inhibitor
cysteine
-
-
Dicarboxylic acids
Hansenula schneggii
-
-
Dicarboxylic acids
-
C-2 to C-10
DL-indole-3-lactic acid
-
specific inhibition of KAT I activity
DL-indole-3-lactic acid
-
estradiol disulfate
very strong inhibitor
estradiol disulfate
strong reversible inhibitor; strong reversible inhibitor
glutamate
-
glutamate
-
weak inhibition
glutamine
-
0.08 mM; inhibition of KAT I
glutamine
-
0.08 mM; 50% inhibition of placental KAT I
glutamine
-
strong inhibition of KAT I, phenylpyruvate, 2-oxo-4-methiolbutyrate or 2-oxo-isocaproate protect
glutamine
-
strong inhibition of KAT I
Hg2+
Hansenula schneggii
-
0.1 mM, 89% inhibition
Hg2+
Hansenula schneggii
-
-
hydroxylamine
Hansenula schneggii
-
0.1 mM, complete inhibition after 30 min
hydroxylamine
-
complete inhibition
Indole-3-propionic acid
-
-
Indole-3-propionic acid
-
iodoacetate
Hansenula schneggii
-
1 mM, 64% inhibition
iodoacetate
Hansenula schneggii
-
-
L-asparagine
less than 35% inhibition at 5 mM
L-asparagine
-
5 mM decreases KAT II activity
L-aspartate
-
specific inhibitor of KAT IV
L-aspartate
-
0.72 mM, 50% inhibition of brain KAT I, 0.073 mM, 50% inhibition of brain KAT II
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
L-cysteine
less than 35% inhibition at 5 mM
L-cysteine
-
5 mM decreases KAT II activity; inhibition of human KAT I activity at 2 mM
L-cysteine
-
inhibition of KAT I
L-cysteine
-
inhibitory in whole cells
L-glutamate
less than 35% inhibition at 5 mM
L-glutamate
-
1.3 mM, 50% inhibition of brain KAT I, 0.79 mM, 50% inhibition of brain KAT II
L-glutamine
-
inhibition of KAT I activity at 2 mM
L-histidine
less than 35% inhibition at 5 mM
L-histidine
-
5 mM decreases KAT II activity
L-kynurenine
-
inhibition above 5 mM
L-kynurenine
-
substrate inhibition above 6 mM
L-leucine
-
L-leucine
-
inhibitory in whole cells
L-lysine
less than 35% inhibition at 5 mM
L-lysine
-
5 mM decreases KAT II activity
L-methionine
-
specific inhibitor of KAT III
L-phenylalanine
-
inhibition of KAT I
L-phenylalanine
less than 35% inhibition at 5 mM
L-phenylalanine
-
5 mM decreases KAT II activity; inhibition of KAT I activity at 2 mM
L-phenylalanine
-
strong inhibition of KAT I
L-tryptophan
-
1 mM, isoform KAT I, 3% residual activity, isoform KAT II, 129% activity
L-tryptophan
-
inhibition of KAT I
L-tryptophan
-
specific inhibition of KAT I activity at 2 mM
L-tryptophan
-
KAT I is greatly and specifically inhibited by 5 mM L-tryptophan
L-tryptophan
-
strong inhibition of KAT I
L-tryptophan
-
inhibitory in whole cells
methionine
-
KAT III is greatly inhibited by 5 mM methionine
PF-04859989
irreversible inhibitor; irreversible inhibitor
pimelate
Hansenula schneggii
-
10 mM, 53% inhibition
quisqualate
-
0.52 mM, 50% inhibition of KAT II, 2 mM, 80% inhibition
quisqualate
-
inhibition of brain KAT II
S-4-(ethylsulfonyl)benzoyl-L-alanine
reversible inhibitor; reversible inhibitor
S-4-(ethylsulfonyl)benzoyl-L-alanine
-
S-dichlorovinyl-L-cysteine
-
strong inhibition of KAT I
S-dichlorovinyl-L-cysteine
-
2 mM, 90% inhibition of KAT I and KAT II
Tris
-
Tris buffer pH 7.5, low activity, pH 8.0, no activity
tryptophan
-
KAT I is greatly inhibited by 2 mM tryptophan
additional information
Hansenula schneggii
-
not inhibited by EDTA, 2,2'-dipyridyl
-
additional information
Hansenula schneggii
-
not inhibited by EDTA, 2,2'-dipyridyl
-
additional information
-
KAT II is not inhibited by glutamine, tryptophan and phenylalanine
-
additional information
not inhibited by glyoxylate
-
additional information
-
not inhibited by glyoxylate
-
additional information
-
KAT I is not inhibited by 2 mM methionine
-
additional information
glycerol is not a functional inhibitor of KAT I
-
additional information
-
glycerol is not a functional inhibitor of KAT I
-
additional information
-
(S)-(4)-(ethylsulfonyl)benzoylalanine shows no inhibition (inhibitor of the rat enzyme)
-
additional information
not inhibited by estradiol and estradiol 3-sulfate; not inhibited by estrone sulfate, estradiol and estradiol 3-sulfate
-
additional information
not inhibited by estradiol and estradiol 3-sulfate; not inhibited by estrone sulfate, estradiol and estradiol 3-sulfate
-
additional information
-
not inhibited by estradiol and estradiol 3-sulfate; not inhibited by estrone sulfate, estradiol and estradiol 3-sulfate
-
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
-
KAT I is not inhibited by quisqualate
-
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
-
additional information
-
KAT is not inhibited by UPF 648
-
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21.3 - 92.7
2-aminobutanoate
0.00241 - 5.7
2-oxo-4-methylthiobutyrate
3
2-oxobutanoate
-
pH 7.5, 45°C
0.000217 - 42.2
2-oxobutyrate
1.5
2-oxocaproate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.5 - 10.4
2-oxocaproic acid
0.013 - 8.1
2-oxoglutarate
5.3
2-oxoisocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.9
3-(2-aminobenzoyl)-L-alanine
Hansenula schneggii
-
pH 8.0, 37°C
0.2062
3-hydroxykynurenine
in 200 mM phosphate buffer, pH 7.5, at 37°C
12.9 - 14.2
3-methyl-2-oxobutanoate
3.3
4-methyl-2-oxopentanoate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.4
alpha-oxo-gamma-methiol-butyric acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
1 - 1.6
hydroxyphenylpyruvate
0.5 - 1.4
indo-3-pyruvate
3.6
Indole-3-pyruvate
pH 7.5, 38°C
1.36 - 6.3
L-3-hydroxykynurenine
5.6
L-glutamate
pH 8.0, 37°C, alpha-aminoadipate aminotransferase activity
1.1 - 3.5
L-phenylalanine
2.7
L-Vinylglycine
Hansenula schneggii
-
pH 8.0. 25°C
2.4 - 3.2
Mercaptopyruvate
0.00085 - 0.0013
pyridoxal 5'-phosphate
0.0032
pyridoxamine 5'-phosphate
Hansenula schneggii
-
pH 8.0, 37°C
additional information
additional information
-
21.3
2-aminobutanoate
-
pH 7.5, 45°C
92.7
2-aminobutanoate
Q95VY4
pH 8.5, 45°C
0.00241
2-oxo-4-methylthiobutyrate
-
0.1 mM L-kynurenine, pH 7.5, 25°C
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
5.7
2-oxo-4-methylthiobutyrate
pH 7.5, 38°C
0.01
2-oxoadipate
-
-
20.9
2-oxoadipate
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
0.00173
2-oxobutyrate
-
0.1 mM L-kynurenine, pH 7.5, 25°C
1
2-oxobutyrate
in 100 mM boric acid buffer, pH 9.0, at 45°C
12.7
2-oxobutyrate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
42.2
2-oxobutyrate
pH 7.5, 38°C
0.5
2-oxocaproic acid
in 100 mM boric acid buffer, pH 9.0, at 45°C
10.4
2-oxocaproic acid
pH 7.5, 38°C
0.013
2-oxoglutarate
-
cosubstrate hydroxykynurenine
0.02
2-oxoglutarate
-
cosubstrate L-kynurenine
0.024
2-oxoglutarate
-
pH 9.5, 37°C, KAT I
0.045
2-oxoglutarate
pH 8.0, 37°C, recombinant enzyme, cosubstrate L-kyrunenine
0.096
2-oxoglutarate
pH 8.0, 37°C, recombinant mitochondrial enzyme
0.62
2-oxoglutarate
-
pH 8.0, 37°C, heart KAT, at 5 mM L-kynurenine
0.7
2-oxoglutarate
-
pH 7.5, 37°C, cosubstrate L-kynurenine
0.879
2-oxoglutarate
-
pH 7.0, 37°C, KAT II
1
2-oxoglutarate
-
pH 6.5, 37°C
1.1
2-oxoglutarate
Hansenula schneggii
-
-
1.1
2-oxoglutarate
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate L-kynurenine
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
2.4
2-oxoglutarate
pH 7.5, 38°C
8.1
2-oxoglutarate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1
2-oxoisocaproate
Hansenula schneggii
-
-
1
2-oxoisocaproate
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate L-kynurenine
1
2-oxoisocaproate
-
pH 7.5, 45°C
1.2
2-oxovalerate
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.4
2-oxovalerate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
10.9
2-oxovalerate
pH 7.5, 38°C
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
1.2
beta-phenylpyruvate
Hansenula schneggii
-
-
1.2
beta-phenylpyruvate
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate L-kynurenine
0.4
glyoxylate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.5
glyoxylate
-
pH 7.5, 45°C
4.2
glyoxylate
pH 7.5, 38°C
18
glyoxylate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1
hydroxyphenylpyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.5
hydroxyphenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.6
hydroxyphenylpyruvate
pH 7.5, 38°C
0.5
indo-3-pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.4
indo-3-pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
1.36
L-3-hydroxykynurenine
pH 8.0, 37°C, recombinant enzyme
2
L-3-hydroxykynurenine
-
pH 6.5, 37°C
2.5
L-3-hydroxykynurenine
-
pH 7.2, 37°C, kidney mitochondria
5
L-3-hydroxykynurenine
-
pH 7.2, 37°C, liver supernatant
5.3
L-3-hydroxykynurenine
-
pH 7.2, 37°C, kidney supernatant
6.3
L-3-hydroxykynurenine
-
pH 7.2, 37°C, liver mitochondria
6.2
L-alanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
246
L-alanine
Q95VY4
pH 8.5, 45°C
1.4
L-asparagine
in 100 mM boric acid buffer, pH 9.0, at 45°C
6.1
L-asparagine
Q95VY4
pH 8.5, 45°C
23.1
L-asparagine
-
pH 7.5, 45°C
0.7
L-cysteine
-
pH 7.5, 45°C
0.7
L-cysteine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.3
L-cysteine
Q95VY4
pH 8.5, 45°C
0.7
L-glutamine
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.8
L-glutamine
-
pH 7.5, 45°C
3.8
L-glutamine
Q95VY4
pH 8.5, 45°C
0.7
L-histidine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.5
L-histidine
Q95VY4
pH 8.5, 45°C
5.4
L-histidine
-
pH 7.5, 45°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
0.2
L-kynurenine
E61G mutant KAT I from brain
0.25
L-kynurenine
-
pH 8.0. 30°C
0.68
L-kynurenine
mass spectrometry assay, pH 7.5, temperature not specified in the publication
0.95
L-kynurenine
pH 8.0, 37°C, recombinant enzyme
0.96
L-kynurenine
-
discontinuous assay, pH 7.5, 45°C
1.2
L-kynurenine
-
pH 8.0, 37°C, recombinant enzyme, cosubstrate pyruvate
1.4
L-kynurenine
-
pH 6.5, 37°C
1.4
L-kynurenine
recombinant brain KAT I
1.5
L-kynurenine
-
pH 7.5, 37°C
1.5
L-kynurenine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.6
L-kynurenine
-
pH 6.5, 37°C, enzyme from supernatant
1.7
L-kynurenine
-
pH 8.0, 37°C, cosubstrate pyruvate
2.09
L-kynurenine
-
continuous assay, pH 7.5, 45°C
2.2
L-kynurenine
Hansenula schneggii
-
-
2.5
L-kynurenine
-
pH 6.5, 37°C, mitochondrial enzyme
2.5
L-kynurenine
-
pH 7.2, 37°C, kidney supernatant
3
L-kynurenine
-
pH 7.2, 37°C, liver supernatant
3.4
L-kynurenine
-
pH 7.2, 37°C, kidney mitochondria
4.3
L-kynurenine
Q95VY4
pH 8.5, 45°C
4.7
L-kynurenine
-
pH 7.5, 45°C
4.7
L-kynurenine
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
5
L-kynurenine
-
pH 7.2, 37°C, liver mitochondria
20
L-kynurenine
-
pH 8.0, 37°C, heart KAT, cosubstrate 5 mM pyruvate
27
L-kynurenine
-
pH 8.0, 37°C, heart KAT, cosubstrate 5 mM 2-oxoglutarate
5
L-leucine
Hansenula schneggii
-
-
5
L-leucine
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate 2-oxoglutarate
7.6
L-leucine
-
pH 7.5, 45°C
34.5
L-leucine
Q95VY4
pH 8.5, 45°C
0.9
L-methionine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.4
L-methionine
Q95VY4
pH 8.5, 45°C
5
L-methionine
Hansenula schneggii
-
-
5
L-methionine
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate 2-oxoglutarate
6.4
L-methionine
-
pH 7.5, 45°C
1.1
L-phenylalanine
in 100 mM boric acid buffer, pH 9.0, at 45°C
1.7
L-phenylalanine
-
pH 7.5, 45°C
3.5
L-phenylalanine
Q95VY4
pH 8.5, 45°C
3
L-serine
in 100 mM boric acid buffer, pH 9.0, at 45°C
32.7
L-serine
Q95VY4
pH 8.5, 45°C
1.2
L-tryptophan
-
pH 7.5, 45°C
2.6
L-tryptophan
Hansenula schneggii
-
-
2.6
L-tryptophan
Hansenula schneggii
-
pH 8.0, 37°C, cosubstrate 2-oxoglutarate
7.1
L-tryptophan
in 100 mM boric acid buffer, pH 9.0, at 45°C
12.9
L-tryptophan
Q95VY4
pH 8.5, 45°C
0.9
L-tyrosine
Q95VY4
pH 8.5, 45°C
2.7
L-tyrosine
in 100 mM boric acid buffer, pH 9.0, at 45°C
3.2
L-tyrosine
-
pH 7.5, 45°C
2.4
Mercaptopyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
2.5
Mercaptopyruvate
-
pH 7.5, 45°C
2.8
Mercaptopyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
3.2
Mercaptopyruvate
pH 7.5, 38°C
0.9
oxaloacetate
pH 7.5, 38°C
4.2
oxaloacetate
-
pH 7.5, 45°C
4.9
oxaloacetate
in 100 mM boric acid buffer, pH 9.0, at 45°C
16.8
oxaloacetate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.6
phenylpyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
0.6
phenylpyruvate
-
recombinant enzyme, pH 7.5, 38°C
0.7
phenylpyruvate
pH 7.5, 38°C
0.8
phenylpyruvate
-
pH 7.5, 45°C
1.8
phenylpyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.00085
pyridoxal 5'-phosphate
-
pH 6.5, 37°C
0.0013
pyridoxal 5'-phosphate
Hansenula schneggii
-
pH 8.0, 37°C
0.0175
pyruvate
in 200 mM phosphate buffer, pH 7.5, at 37°C
0.053
pyruvate
-
pH 9.5, 37°C, KAT I
0.1
pyruvate
E61G mutant KAT I from brain
0.7
pyruvate
-
pH 7.5, 37°C, cosubstrate L-kynurenine
0.717
pyruvate
-
pH 7.0, 37°C, KAT II
1.15
pyruvate
-
pH 8.0, 37°C, heart KAT, at 5 mM L-kynurenine
1.2
pyruvate
recombinant brain KAT I
1.63
pyruvate
pH 8.0, 37°C, recombinant mitochondrial enzyme
8.3
pyruvate
pH 7.5, 38°C
9.7
pyruvate
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
10.6
pyruvate
in 100 mM boric acid buffer, pH 9.0, at 45°C
12.1
pyruvate
-
pH 7.5, 45°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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-
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Rattus norvegicus
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Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney
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Homo sapiens
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Rattus norvegicus
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Kynurenic acid and kynurenine aminotransferase in heart
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Partial characterization and distribution of kynurenine aminotransferase activity in the Black Tiger prawn (Penaeus monodon)
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Effects of in vivo sodium azide administration on the immunohistochemical localization of kynurenine aminotransferase in the rat brain
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Kynurenine aminotransferase I activity in human placenta
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Isolation, characterization, and functional expression of kynurenine aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1)
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Effect of 3-nitropropionic acid on kynurenine aminotransferase in the rat brain
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Rattus norvegicus
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Homo sapiens, Rattus norvegicus (Q08415)
brenda
Chon, H.; Matsumura, H.; Shimizu, S.; Maeda, N.; Koga, Y.; Takano, K.; Kanaya, S.
Overproduction and preliminary crystallographic study of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
F61
319-322
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Han, Q.; Li, J.
pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I
Eur. J. Biochem.
271
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2004
Homo sapiens
brenda
Han, Q.; Gao, Y.G.; Robinson, H.; Ding, H.; Wilson, S.; Li, J.
Crystal structures of Aedes aegypti kynurenine aminotransferase
FEBS J.
272
2198-2206
2005
Aedes aegypti
brenda
Han, Q.; Li, J.
Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production
FEBS Lett.
577
381-385
2004
Aedes aegypti (Q95VY4)
brenda
Rossi, F.; Han, Q.; Li, J.; Rizzi, M.
Crystal structure of human kynurenine aminotransferase I
J. Biol. Chem.
279
50214-50220
2004
Homo sapiens (Q16773), Homo sapiens
brenda
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
brenda
Zarnowski, T.; Rejdak, R.; Zagorski, Z.; Juenemann, A.G.; Zrenner, E.; Kocki, T.; Urbanska, E.M.; Turski, W.A.
Content of kynurenic acid and activity of kynurenine aminotransferases in mammalian eyes
Ophthalmic Res.
36
124-128
2004
Bos taurus, Oryctolagus cuniculus, Homo sapiens
brenda
Luchowska, E.; Luchowski, P.; Sarnowska, A.; Wielosz, M.; Turski, W.A.; Urbanska, E.M.
Endogenous level of kynurenic acid and activities of kynurenine aminotransferases following transient global ischemia in the gerbil hippocampus
Pol. J. Pharmacol.
55
443-447
2003
Meriones unguiculatus
brenda
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)
brenda
Kapoor, R.; Lim, K.S.; Cheng, A.; Garrick, T.; Kapoor, V.
Preliminary evidence for a link between schizophrenia and NMDA-glycine site receptor ligand metabolic enzymes, d-amino acid oxidase (DAAO) and kynurenine aminotransferase-1 (KAT-1)
Brain Res.
1106
205-210
2006
Homo sapiens (Q16773)
brenda
Rejdak, R.; Rummelt, C.; Zrenner, E.; Grieb, P.; Zarnowski, T.; Okuno, E.; Schlotzer-Schrehardt, U.; Naumann, G.O.; Kruse, F.; Junemann, A.G.
Immunohistochemical identification of kynurenine aminotransferases in corpora amylacea in the human retina and optic nerve
Folia Neuropathol.
45
66-71
2007
Homo sapiens, Homo sapiens (Q16773), Homo sapiens (Q8N5Z0)
brenda
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
brenda
Hartai, Z.; Klivenyi, P.; Janaky, T.; Penke, B.; Dux, L.; Vecsei, L.
Kynurenine metabolism in plasma and in red blood cells in Parkinsons disease
J. Neurol. Sci.
239
31-35
2005
Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
brenda
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)
brenda
Chon, H.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Crystal structure of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3 at 2.20.ANG. resolution
Proteins
61
685-688
2005
Pyrococcus horikoshii
brenda
Wogulis, M.; Chew, E.R.; Donohoue, P.D.; Wilson, D.K.
Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence
Biochemistry
47
1608-1621
2008
Saccharomyces cerevisiae (P47039)
brenda
Han, Q.; Gao, Y.G.; Robinson, H.; Li, J.
Structural insight into the mechanism of substrate specificity of Aedes kynurenine aminotransferase
Biochemistry
47
1622-1630
2008
Aedes aegypti, Homo sapiens
brenda
Rossi, F.; Garavaglia, S.; Montalbano, V.; Walsh, M.A.; Rizzi, M.
Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia
J. Biol. Chem.
283
3559-3566
2008
Homo sapiens
brenda
Han, Q.; Robinson, H.; Li, J.
Crystal structure of human kynurenine aminotransferase II
J. Biol. Chem.
283
3567-3573
2008
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Bellocchi, D.; Macchiarulo, A.; Carotti, A.; Pellicciari, R.
Quantum mechanics/molecular mechanics (QM/MM) modeling of the irreversible transamination of L-kynurenine to kynurenic acid: the round dance of kynurenine aminotransferase II
Biochim. Biophys. Acta
1794
1802-1812
2009
Homo sapiens
brenda
Han, Q.; Cai, T.; Tagle, D.A.; Robinson, H.; Li, J.
Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
Biosci. Rep.
28
205-215
2008
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
J. Med. Chem.
52
2786-2793
2009
Homo sapiens (Q16773), Homo sapiens
brenda
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
brenda
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Biochemical and structural properties of mouse kynurenine aminotransferase III
Mol. Cell. Biol.
29
784-793
2009
Mus musculus (Q71RI9), Mus musculus
brenda
Battsetseg, B.; Boldbaatar, D.; Battur, B.; Xuan, X.; Fujisaki, K.
Cloning and molecular characterization of tick kynurenine aminotransferase (HlKAT) from Haemaphysalis longicornis (Acari: Ixodidae)
Parasitol. Res.
105
669-679
2009
Haemaphysalis longicornis (B1B6U5)
brenda
Wong, J.; Ray, W.J.; Kornilova, A.Y.
Development of a microplate fluorescence assay for kynurenine aminotransferase
Anal. Biochem.
409
183-188
2011
Homo sapiens
brenda
Akladios, F.N.; Nadvi, N.A.; Park, J.; Hanrahan, J.R.; Kapoor, V.; Gorrell, M.D.; Church, W.B.
Design and synthesis of novel inhibitors of human kynurenine aminotransferase-I
Bioorg. Med. Chem. Lett.
22
1579-1581
2012
Homo sapiens
brenda
Han, Q.; Robinson, H.; Cai, T.; Tagle, D.A.; Li, J.
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
Biosci. Rep.
31
323-332
2011
Mus musculus (P05202), Mus musculus
brenda
Han, Q.; Cai, T.; Tagle, D.; Li, J.
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases
BMC Biochem.
11
0019
2010
Mus musculus (P05202), Mus musculus (Q71RI9), Mus musculus (Q8BTY1), Mus musculus (Q9WVM8), Mus musculus
brenda
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
brenda
Passera, E.; Campanini, B.; Rossi, F.; Casazza, V.; Rizzi, M.; Pellicciari, R.; Mozzarelli, A.
Human kynurenine aminotransferase II--reactivity with substrates and inhibitors
FEBS J.
278
1882-1900
2011
Homo sapiens
brenda
Rossi, F.; Valentina, C.; Garavaglia, S.; Sathyasaikumar, K.V.; Schwarcz, R.; Kojima, S.; Okuwaki, K.; Ono, S.; Kajii, Y.; Rizzi, M.
Crystal structure-based selective targeting of the pyridoxal 5-phosphate dependent enzyme kynurenine aminotransferase II for cognitive enhancement
J. Med. Chem.
53
5684-5689
2010
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Okada, K.; Angkawidjaja, C.; Koga, Y.; Takano, K.; Kanaya, S.
Characteristic features of kynurenine aminotransferase allosterically regulated by (alpha)-ketoglutarate in cooperation with kynurenine
PLoS ONE
7
e40307
2012
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Okada, K.; Angkawidjaja, C.; Koga, Y.; Kanaya, S.
Structural and mechanistic insights into the kynurenine aminotransferase-mediated excretion of kynurenic acid
J. Struct. Biol.
185
257-266
2014
Pyrococcus horikoshii (O57946), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O57946)
brenda
Lu, H.; Kopcho, L.; Ghosh, K.; Witmer, M.; Parker, M.; Gupta, S.; Paul, M.; Krishnamurthy, P.; Laksmaiah, B.; Xie, D.; Tredup, J.; Zhang, L.; Abell, L.M.
Development of a RapidFire mass spectrometry assay and a fluorescence assay for the discovery of kynurenine aminotransferase II inhibitors to treat central nervous system disorders
Anal. Biochem.
501
56-65
2016
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Nematollahi, A.; Sun, G.; Harrop, S.J.; Hanrahan, J.R.; Church, W.B.
Structure of the PLP-form of the human kynurenine aminotransferase II in a novel spacegroup at 1.83 A resolution
Int. J. Mol. Sci.
17
446
2016
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Pinto, J.T.; Krasnikov, B.F.; Alcutt, S.; Jones, M.E.; Dorai, T.; Villar, M.T.; Artigues, A.; Li, J.; Cooper, A.J.
Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate beta-lyase activity and can transaminate L-selenomethionine
J. Biol. Chem.
289
30950-30961
2014
Homo sapiens (Q6YP21), Homo sapiens
brenda
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
brenda
Sun, G.; Nematollahi, A.; Nadvi, N.A.; Kwan, A.H.; Jeffries, C.M.; Church, W.B.
Expression, purification and crystallization of human kynurenine aminotransferase 2 exploiting a highly optimized codon set
Protein Expr. Purif.
121
41-45
2016
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Yang, C.; Zhang, L.; Han, Q.; Liao, C.; Lan, J.; Ding, H.; Zhou, H.; Diao, X.; Li, J.
Kynurenine aminotransferase 3/glutamine transaminase L/cysteine conjugate beta-lyase 2 is a major glutamine transaminase in the mouse kidney
Biochem. Biophys. Rep.
8
234-241
2016
Mus musculus
brenda
Kalliokoski, T.; Rummakko, P.; Rantanen, M.; Blaesse, M.; Augustin, M.; Ummenthala, G.R.; Choudhary, S.; Venaelaeinen, J.
Discovery of sulfonamides and 9-oxo-2,8-diazaspiro[5,5]undecane-2-carboxamides as human kynurenine aminotransferase 2 (KAT2) inhibitors
Bioorg. Med. Chem. Lett.
30
127060
2020
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Wyckelsma, V.L.; Lindkvist, W.; Venckunas, T.; Brazaitis, M.; Kamandulis, S.; Paeaesuke, M.; Ereline, J.; Westerblad, H.; Andersson, D.C.
Kynurenine aminotransferase isoforms display fiber-type specific expression in young and old human skeletal muscle
Exp. Gerontol.
134
110880
2020
Homo sapiens, Homo sapiens (Q6YP21), Homo sapiens (Q8N5Z0)
brenda
Rossi, F.; Miggiano, R.; Ferraris, D.M.; Rizzi, M.
The synthesis of kynurenic acid in mammals an updated kynurenine aminotransferase structural KATalogue
Front. Mol. Biosci.
6
7-7
2019
Mus musculus (P05202), Mus musculus (Q71RI9), Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Jayawickrama, G.; Nematollahi, A.; Sun, G.; Church, W.
Improvement of kynurenine aminotransferase-II inhibitors guided by mimicking sulfate esters
PLoS ONE
13
e0196404
2018
Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Nadvi, N.A.; Salam, N.K.; Park, J.; Akladios, F.N.; Kapoor, V.; Collyer, C.A.; Gorrell, M.D.; Church, W.B.
High resolution crystal structures of human kynurenine aminotransferase-I bound to PLP cofactor, and in complex with aminooxyacetate
Protein Sci.
26
727-736
2017
Homo sapiens (Q16773), Homo sapiens
brenda
Jayawickrama, G.S.; Nematollahi, A.; Sun, G.; Gorrell, M.D.; Church, W.B.
Inhibition of human kynurenine aminotransferase isozymes by estrogen and its derivatives
Sci. Rep.
7
17559
2017
Homo sapiens (Q16773), Homo sapiens (Q8N5Z0), Homo sapiens
brenda
Yoshida, Y.; Fujigaki, H.; Kato, K.; Yamazaki, K.; Fujigaki, S.; Kunisawa, K.; Yamamoto, Y.; Mouri, A.; Oda, A.; Nabeshima, T.; Saito, K.
Selective and competitive inhibition of kynurenine aminotransferase 2 by glycyrrhizic acid and its analogues
Sci. Rep.
9
10243
2019
Homo sapiens (Q8N5Z0)
brenda