Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.6.1.7
-
RECOMMENDED NAME
GeneOntology No.
kynurenine-oxoglutarate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
show the reaction diagram
transamination of the amino acid to a transient keto acid intermediate which spontaneously undergoes ring closure
-
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
show the reaction diagram
mechanism
Hansenula schneggii
-
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
tryptophan degradation XI (mammalian, via kynurenine)
-
Tryptophan metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-kynurenine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminoadipate aminotransferase
Q9WVM8
-
aminotransferase, kynurenine
-
-
-
-
aspartate aminotransferase
P05202
-
cysteine conjugate beta-lyase 1
Q8BTY1
-
cysteine conjugate beta-lyase 2
Q71RI9
-
glutamic-oxaloacetic transaminase 2
P05202
-
glutamine transaminase K
Q8BTY1
-
KAT
Q08415
-
KAT
Q64602
-
KAT I
-
also called GTK or CCBL1
KAT I
Q16773
-
KAT I
-
also called GTK or CCBL1
KAT I
-
also called GTK or CCBL1
KAT II
-
also called AADAT
KAT II
-
identical with alpha-aminoadipate aminotransferase
KAT II
Q8N5Z0
-
KAT II
-
also called AADAT
KAT II
-
also called AADAT
KAT II
-
identical with alpha-aminoadipate aminotransferase
KAT III
-
also called CCBL2
KAT III
Q71RI9
-
KAT III
-
also called CCBL2
KAT IV
-
also called mitochondrial ASAT or GOT2
KAT-1
Q16773
-
KAT-I
-
-
KAT-I
Q08415
-
KAT-II
-
isoform
kynurenine 2-oxoglutarate transaminase
-
-
-
-
kynurenine aminotransferase
-
-
-
-
kynurenine aminotransferase
-
-
kynurenine aminotransferase I
-
-
kynurenine aminotransferase I
Q8BTY1
-
kynurenine aminotransferase I
-
-
kynurenine aminotransferase II
-
-
kynurenine aminotransferase II
Q8N5Z0
-
kynurenine aminotransferase II
Q9WVM8
-
kynurenine aminotransferase II
-
-
kynurenine aminotransferase II
-
-
kynurenine aminotransferase III
Q6YP21
-
kynurenine aminotransferase III
Q71RI9
-
kynurenine aminotransferase III
Q58FK9
-
kynurenine aminotransferase IV
P05202
-
kynurenine aminotransferase-1
Q16773
-
kynurenine aminotransferase-I
-
-
kynurenine aminotransferase-I
Q08415
-
kynurenine aminotransferase-IV
P05202
-
kynurenine aminotransferases I
Q08415
-
kynurenine aminotransferases II
Q64602
-
kynurenine pyruvate aminotransferase
-
i.e. KAT-I
kynurenine transaminase (cyclizing)
-
-
-
-
kynurenine-2-oxoglutarate aminotransferase
-
i.e. KAT-II
L-kynurenine aminotransferase
-
-
-
-
PhKAT
O57946
-
type II kynurenine aminotransferase
-
-
mitochondrial aspartate aminotransferase
P05202
-
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
-
not identical with EC 2.6.1.39
additional information
Rattus norvegicus Wistar
-
enzyme from mitochondria may be identical with EC 2.6.1.39
-
CAS REGISTRY NUMBER
COMMENTARY
9030-38-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
yellow fever mosquito
SwissProt
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
Debaryomyces globosus
low activity
-
-
Manually annotated by BRENDA team
Hansenula schneggii
yeast
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
expression in Sf9 system
-
-
Manually annotated by BRENDA team
isoform KAT II
-
-
Manually annotated by BRENDA team
isoform KAT II
SwissProt
Manually annotated by BRENDA team
kynurenine aminotransferase I and II, i.e. KAT I and KAT II, in elderly Down syndrome patients
-
-
Manually annotated by BRENDA team
isoforms KAT I and KAT II, no change of enzyme activity 24 and 72 h after transient global ischemia episode
-
-
Manually annotated by BRENDA team
black tiger prawn
-
-
Manually annotated by BRENDA team
strain OT3, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
adult albino
-
-
Manually annotated by BRENDA team
adult albino; male
-
-
Manually annotated by BRENDA team
brain KAT I
SwissProt
Manually annotated by BRENDA team
brain KAT I
-
-
Manually annotated by BRENDA team
cytosolic KAT I
SwissProt
Manually annotated by BRENDA team
Donryu; isoenzyme 2
-
-
Manually annotated by BRENDA team
identical to kidney soluble cysteine conjugate beta-lyase also referred to as glutamine transaminase K, K stands for kidney
-
-
Manually annotated by BRENDA team
isoforms KAT I and KAT II
-
-
Manually annotated by BRENDA team
KAT I and KAT II
-
-
Manually annotated by BRENDA team
KAT II accounts for more than 70% of kynurenate production under physiological conditiones
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Donryu
Donryu
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
isoform Bna3 is not an formyl kynurenine formamidase, but kynurenine aminotransferase
UniProt
Manually annotated by BRENDA team
Saccharomyces fragilis
low activity
-
-
Manually annotated by BRENDA team
Saccharomyces marxianus
-
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
KAT-II is the enzymatic isoform that mainly accounts for the synthesis of cerebral kynurenic acid
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobutyrate + glyoxylate
?
show the reaction diagram
-
-
-
-
?
3,5-diiodo-L-tyrosine + 2-oxoglutarate
3-(2,5-diiodo-4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
slightly better than L-kynurenine
-
?
3-hydroxykynurenine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
3-hydroxykynurenine + pyruvate
?
show the reaction diagram
B1B6U5
-
-
-
?
L-2-aminoheptane-1,7-dioate + 2-oxoglutarate
2-oxoheptane-1,7-dioate + L-glutamate
show the reaction diagram
-
at 39.7% of the activity with 2-aminohexane-1,6-dioate
-
?
L-2-aminohexane-1,6-dioate + 2-oxoglutarate
2-oxohexane-1,6-dioate + L-glutamate
show the reaction diagram
Hansenula schneggii
-
at about 60% the rate of L-kynurenine
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
ir
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
Q64602
-
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
no activity with D-isomer
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
-
KAT I, no good substrate
-
-
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
Hansenula schneggii
-
at about 45% the rate of L-kynurenine
-
?
L-3-hydroxykynurenine + 2-oxoglutarate
xanthurenic acid + L-glutamate
show the reaction diagram
Rattus norvegicus Donryu
-
-
-
-
L-4-chloro-kynurenine + 2-oxoglutarate
L-7-chloro-kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-5-chloro-kynurenine + 2-oxoglutarate
L-6-chloro-kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxobutanoate
pyruvate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-alanine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-asparagine + 2-oxobutanoate
2-oxosuccinamic acid + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-asparagine + glyoxylate
?
show the reaction diagram
-
KAT II has high transamination activity toward L-asparagine
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
show the reaction diagram
-
-
-
-
?
L-cysteine + 2-oxobutanoate
2-aminobutanoate + 3-mercapto-2-oxopropanoate
show the reaction diagram
-
-
-
-
?
L-cysteine + 2-oxobutanoate
? + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-cysteine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxobutanoate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-glutamine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-histidine + 2-oxobutanoate
3-(1H-imidazol-4-yl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-histidine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
?
show the reaction diagram
B1B6U5
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenate + L-methionine
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxo-4-methylthiobutyrate
kynurenic acid + L-methionine
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
Q95VY4
25% of activity with pyruvate
-
?
L-kynurenine + 2-oxoadipate
kynurenic acid + 2-aminoadipate + H2O
show the reaction diagram
Q64602
91% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxoadipate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutanoate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
Hansenula schneggii
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate + H2O
show the reaction diagram
Q64602
28% of activity with 2-oxoglutarate
-
?
L-kynurenine + 2-oxobutyrate
?
show the reaction diagram
B1B6U5
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenate + ?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxobutyrate
kynurenic acid + 2-aminobutanoate
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + 2-oxocaproate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxocaproic acid
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxocaproic acid
kynurenic acid + 2-aminohexanoate
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Debaryomyces globosus
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Q8N5Z0
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
broad specificity
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
broad specificity
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
best substrates
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
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
show the reaction diagram
-
no activity with D-kynureinine
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q64602
enzyme has both kynurenine aminotransferase and alpha-aminoadipate aminotransferase activity
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Q08415
enzyme has both kynurenine aminotransferase and glutamine transaminase K activity
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
KAT I shows far higher activity with 2-oxoisohexanoate than with 2-oxoglutarate
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
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
show the reaction diagram
Q95VY4
31% of activity with pyruvate
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
initial reaction in quinaldine pathway of kynurenine catabolism
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
inducible enzyme of tryptophan catabolism
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
inducible enzyme of tryptophan catabolism
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Rattus norvegicus Donryu
-
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
show the reaction diagram
Rattus norvegicus Donryu
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Rattus norvegicus Wistar
-
best substrates
-
ir
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)2,4-dioxobutanoate + L-glutamate
show the reaction diagram
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
?
show the reaction diagram
-
poor cosubstrate for KAT III
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
Q8BTY1, Q9WVM8
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
Q8BTY1, Q9WVM8
highest activity with aspartate and glutamate as substrate, but also active with other amino acids
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxohexanedioate
kynurenic acid + 2-aminohexanedioate + H2O
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
?
L-kynurenine + 2-oxohexanoate
kynurenic acid + L-norleucine + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisocaproate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-leucine
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
-
KAT I shows far higher activity with 2-oxoisohexanoate than with 2-oxoglutarate
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxoisohexanoate
kynurenic acid + 2-aminoisohexanoate + H2O
show the reaction diagram
-
heart KAT, low activity
-
-
L-kynurenine + 2-oxoisopentanoate
kynurenic acid + 2-aminoisopentanoate + H2O
show the reaction diagram
-
poor substrate
-
?
L-kynurenine + 2-oxomethylthiobutyric acid
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxopentanoate
kynurenic acid + L-norvaline + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxopentanoate
kynurenic acid + L-norvaline + H2O
show the reaction diagram
Hansenula schneggii
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + 2-oxovalerate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxovalerate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 2-oxovalerate
kynurenic acid + 2-aminopentanoater
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + 3-indole-2-oxopropanoate
kynurenic acid + L-tryptophan + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 3-indole-2-oxopropanoate
kynurenic acid + L-tryptophan + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 3-methyl-2-oxobutanoate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
kynurenic acid + L-isoleucine + H2O
show the reaction diagram
-
poor substrate
-
?
L-kynurenine + 3-methyl-2-oxopentanoate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
-
-
L-kynurenine + 3-phenyl-2-oxopropanoate
kynurenic acid + L-phenylalanine + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 4-methyl-2-oxopentanoate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + 4-methyl-2-oxovalerate
kynurenic acid + 2,4-dimethylvalerate + H2O
show the reaction diagram
Q64602
5.9% of activity with 2-oxoglutarate
-
?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
kynurenic acid + L-methionine + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + 4-methylsulfanyl-2-oxobutyrate
kynurenic acid + L-methionine + H2O
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine + H2O
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
poor substrate
-
?
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
-
-
-
-
?
L-kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
-
glyoxylate shows a relatively low affinity for KAT II
-
-
?
L-kynurenine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine
show the reaction diagram
Q8BTY1, Q9WVM8
2-oxobutyrate is also a co-substrate
-
-
?
L-kynurenine + glyoxylate
kynurenic acid + glycine
show the reaction diagram
Q8BTY1, Q9WVM8
alpha-ketobutyrate is also a co-substrate
-
-
?
L-kynurenine + hydroxyphenylpyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + hydroxyphenylpyruvate
kynurenic acid + L-tyrosine
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + indo-3-pyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + indol-3-ylpyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + indole-3-pyruvate
kynurenic acid + L-tryptophan
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + mercaptopyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine
show the reaction diagram
-
-
-
-
?
L-kynurenine + mercaptopyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + mercaptopyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + mercaptopyruvate
kynurenic acid + ?
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
Q95VY4
90% of activity with pyruvate
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate + H2O
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + oxaloacetate
4-(2-aminophenyl)-2,4-dioxobutanoate + 2-aminosuccinate
show the reaction diagram
-
-
-
-
?
L-kynurenine + oxaloacetate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + oxaloacetate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + oxaloacetate
kynurenate + L-aspartate
show the reaction diagram
-
-
-
-
?
L-kynurenine + oxaloacetate
kynurenic acid + L-aspartate
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + p-hydroxyphenylpyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + phenylpyruvate
phenylalanine + L-glutamate + H2O
show the reaction diagram
Q64602
43% of activity with 2-oxoglutarate
-
?
L-kynurenine + phenylpyruvate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
L-kynurenine + phenylpyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + phenylpyruvate
?
show the reaction diagram
-
-, poor cosubstrate for KAT III
-
-
?
L-kynurenine + phenylpyruvate
kynurenic acid + L-phenylalanine
show the reaction diagram
P05202
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
-
-
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
-
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
-
-
-
-
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Q08415
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
B1B6U5
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
placental KAT I, higher activity than with 2-oxoglutarate
-
-
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
best substrate of heart KAT
-
-
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Q64602
3% of activity with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
KAT I shows far higher activity with 2-oxoisohexanoate and pyruvate than with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
-
100fold higher maximal velocity than with 2-oxoglutarate
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Q95VY4
best amino acceptor
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Rattus norvegicus Donryu
-
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine + H2O
show the reaction diagram
Rattus norvegicus Wistar
-
less effective than 2-oxoglutarate
-
?
L-kynurenine + pyruvate
4-(2-aminophenyl)2,4-dioxobutanoate + L-alanine
show the reaction diagram
-
-
-
-
?
L-kynurenine + pyruvate
?
show the reaction diagram
-
-
-
-
?
L-kynurenine + pyruvate
?
show the reaction diagram
-
poor cosubstrate for KAT III
-
-
?
L-kynurenine + pyruvate
kynurenic acid + L-alanine
show the reaction diagram
P05202
-
-
-
?
L-kyruneine + pyruvate
kynurenic acid + L-alanine
show the reaction diagram
-
-
-
-
ir
L-leucine + 2-oxobutanoate
2-oxoisocaproate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-leucine + 2-oxobutanoate
alpha-ketoleucine + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
Hansenula schneggii
-
-
-
-
-
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
Hansenula schneggii
-
at about 85% the rate of L-kynurenine
-
?
L-lysine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + 2-oxobutanoate
4-methylsulfanyl-2-oxobutanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
show the reaction diagram
-
12% the rate of L-kynurenine
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + glutamate
show the reaction diagram
Hansenula schneggii
-
at about 36% the rate of L-kynurenine
-
?
L-methionine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
-
at about 30% the rate of L-kynurenine
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 2-oxobutanoate
phenylpyruvate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-phenylalanine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-serine + 2-oxobutanoate
3-hydroxy-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-serine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxobutanoate
3-indole-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
poor substrate
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
Hansenula schneggii
-
at about 60% the rate of L-kynurenine
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
16% the rate of L-kynurenine
-
?
L-tryptophan + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxobutanoate
3-(4-hydroxyphenyl)-2-oxopropanoate + 2-aminobutanoate
show the reaction diagram
Q95VY4
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
?
L-tyrosine + glyoxylate
?
show the reaction diagram
-
-
-
-
?
L-vinylglycine
2-oxobutyrate + NH3
show the reaction diagram
Hansenula schneggii
-
deamination at 1% the rate of kynurenine, suicide substrate
-
?
L-vinylglycine + 1-propanethiol
S-n-propylhomocysteine
show the reaction diagram
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
-
?
L-vinylglycine + 2-oxobutyrate
2-aminobutyrate + 2-oxo-3-butenoate
show the reaction diagram
Hansenula schneggii
-
-
-
?
L-vinylglycine + ethanethiol
ethionine
show the reaction diagram
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
i.e. S-ethylhomocysteine
?
L-vinylglycine + methanethiol
methionine
show the reaction diagram
Hansenula schneggii
-
gamma-addition reaction in the presence of alkanethiols
-
?
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
?
-
B1B6U5
the purified recombinant KAT shows dose-dependent inhibition effect on the growth of equine babesial parasite, Babesia caballi, in in vitro culture
-
-
-
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
?
-
-
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, 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 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 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 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 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 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, 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 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
?
-
B1B6U5
no activity towards L-tryptophan and pyruvic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
initial reaction in quinaldine pathway of kynurenine catabolism
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
-
inducible enzyme of tryptophan catabolism
-
-
-
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
Hansenula schneggii
-
inducible enzyme of tryptophan catabolism
-
-
-
additional information
?
-
B1B6U5
the purified recombinant KAT shows dose-dependent inhibition effect on the growth of equine babesial parasite, Babesia caballi, in in vitro culture
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
Km-value: 0.001 mM
pyridoxal 5'-phosphate
-
Km-value: 0.00085 mM
pyridoxal 5'-phosphate
Hansenula schneggii
-
Km-value: 0.0013 mM; required for activity, 2 mol per mol holoenzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Hansenula schneggii
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q8N5Z0
enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes, crystallization data
pyridoxal 5'-phosphate
B1B6U5
a highly conserved pyridoxal 5'-phosphate binding site (Gly-Ser-Ala-Gly-Lys-Thr-Phe-Ser) is located between Gly-219 and Ser-226
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
additional information
-
pyridoxamine 5'-phosphate is not a cofactor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CaCl2
-
approx. 4fold increase in activity at pH 6.4
additional information
-
not activated by chloride salts of Mg2+, Mn2+, Na+, K+ or NH4+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(R)-2-amino-4-(4-(ethylsulfonyl))-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, 25C
-
(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
2-oxoglutarate
-
substrate inhibition
2-oxoglutarate
-
inhibited by high concentrations, allosterically regulated
3-(2-carboxyethyl)-5-chloro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
-
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-hydroxykynurenine
-
less than 35% inhibition at 5 mM
3-hydroxykynurenine
-
5 mM decreases KAT II activity
3-hydroxykynurenine
-
-
3-indolepropionic acid
-
specific inhibition of KAT I activity
3-indolepropionic acid
-
-
3-Methyl-2-benzothiazolone hydrazone hydrochloride
Hansenula schneggii
-
0.1 mM, complete inhibition, reversible by pyridoxal phosphate
4-carboxy-3-hydroxyphenylglycine
-
inhibition of brain KAT II
4-chloromercuribenzoate
Hansenula schneggii
-
1 mM, 78% inhibition
4-chloromercuribenzoate
Hansenula schneggii
-
-
4-chloromercuribenzoate
-
-
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
-
-
Adipate
Hansenula schneggii
-
10 mM, 39% inhibition
Adipate
-
strong inhibition
alpha-aminoadipate
-
strong inhibition of KAT II
amino-2,3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid
-
inhibitory in whole cells
aminoadipate
-
less than 35% inhibition at 5 mM
aminoadipate
-
5 mM decreases KAT II activity
aminooxyacetic acid
-
inhibitory in whole cells
anthranilate
-
weak inhibition
aspartate
Q8BTY1, Q9WVM8
-
azelaic acid
-
-
cysteine
Q8BTY1, Q9WVM8
;
cysteine sulfinate
-
poor substrate that undergoes slow transamination, KM-value 12.3 mM, pH 7.5, 25C
Decanoic acid
-
-
Dicarboxylic acids
-
C-2 to C-10
Dicarboxylic acids
Hansenula schneggii
-
-
Diethylglutaric acid
-
-
Dimethylglutaric acid
-
-
-
DL-indole-3-lactic acid
-
specific inhibition of KAT I activity
DL-indole-3-lactic acid
-
-
EGTA
-
strong inhibiton at pH 6.8 and Ca2+ concentrations below 0.5 mM
glutamate
-
weak inhibition
glutamate
Q8BTY1, Q9WVM8
-
glutamine
-
0.08 mM; inhibition of KAT I
glutamine
-
strong inhibition of KAT I, phenylpyruvate, 2-oxo-4-methiolbutyrate or 2-oxo-isocaproate protect
glutamine
-
strong inhibition of KAT I
glutamine
-
0.08 mM; 50% inhibition of placental KAT I
glutamine
Q8BTY1, Q9WVM8
;
Hg2+
Hansenula schneggii
-
0.1 mM, 89% inhibition
Hg2+
Hansenula schneggii
-
-
Hg2+
-
strong inhibition
histidine
Q8BTY1, Q9WVM8
-
hydroxylamine
-
complete inhibition
hydroxylamine
Hansenula schneggii
-
0.1 mM, complete inhibition after 30 min
indole-3-acetic acid
-
-
Indole-3-propionic acid
-
-
Indole-3-propionic acid
Q8BTY1, Q9WVM8
-
Indole-3-pyruvate
-
5 mM, complete inhibition
indole-3-pyruvic acid
-
-
iodoacetate
Hansenula schneggii
-
1 mM, 64% inhibition
iodoacetate
Hansenula schneggii
-
-
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-2-Aminoadipate
-
-
L-4-chlorokynurenine
-
-
L-5-chlorokynurenine
-
-
L-asparagine
-
less than 35% inhibition at 5 mM
L-asparagine
-
5 mM decreases KAT II activity
L-aspartate
-
0.72 mM, 50% inhibition of brain KAT I, 0.073 mM, 50% inhibition of brain KAT II
L-aspartate
-
specific inhibitor of KAT IV
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
-
inhibition of KAT I
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
L-cysteine
-
inhibitory in whole cells
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
-
-
L-cysteine sulfinate
-
0.002 mM, 50% inhibition of brain KAT II
L-glutamate
-
1.3 mM, 50% inhibition of brain KAT I, 0.79 mM, 50% inhibition of brain KAT II
L-glutamate
-
less than 35% inhibition at 5 mM
L-glutamine
-
inhibition of KAT I activity at 2 mM
L-glutamine
-
-
L-histidine
-
less than 35% inhibition at 5 mM
L-histidine
-
5 mM decreases KAT II activity
L-histidine
-
-
L-Homocysteate
-
5.0 mM, 50% inhibition of brain KAT I, 2.1 mM, 50% inhibition of brain KAT II
L-Homocysteine sulfinate
-
1.59 mM, 50% inhibition of brain KAT II
L-kynurenine
-
inhibition above 5 mM
L-kynurenine
-
substrate inhibition above 6 mM
L-leucine
-
inhibitory in whole cells
L-leucine
-
-
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-methionine
-
-
L-Penicillamine
Hansenula schneggii
-
0.1 mM, 62% inhibition, reversible by pyridoxal phosphate
L-phenylalanine
-
inhibition of KAT I
L-phenylalanine
-
strong inhibition of KAT I
L-phenylalanine
-
-
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-serine-O-phosphate
-
inhibition of brain KAT II
L-tryptophan
-
inhibition of KAT I
L-tryptophan
-
strong inhibition of KAT I
L-tryptophan
-
-
L-tryptophan
-
inhibitory in whole cells
L-tryptophan
-
1 mM, isoform KAT I, 3% residual activity, isoform KAT II, 129% activity
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
leucine
Q8BTY1, Q9WVM8
-
methionine
-
KAT III is greatly inhibited by 5 mM methionine
N-ethylmaleimide
Hansenula schneggii
-
-
N-omega-nitro-L-arginine
-
-
nicotinate
-
weak inhibition
phenylalanine
Q8BTY1, Q9WVM8
;
phenylhydrazine
Hansenula schneggii
-
0.1 mM, 81% inhibition, reversible by pyridoxal phosphate
pimelate
Hansenula schneggii
-
10 mM, 53% inhibition
pyridoxal 5'-phosphate
-
at high concentrations
quinolinic acid
-
strong inhibiton at pH 6.8 and Ca2+ concentrations below 0.5 mM
quisqualate
-
0.52 mM, 50% inhibition of KAT II, 2 mM, 80% inhibition
quisqualate
-
inhibition of brain KAT II
Quisqualic acid
-
1 mM, isoform KAT I, 81% residual activity, isoform KAT II, 1% residual activity
S-dichlorovinyl-L-cysteine
-
strong inhibition of KAT I
S-dichlorovinyl-L-cysteine
-
2 mM, 90% inhibition of KAT I and KAT II
Sulfate or phosphate esters of steroids
-
-
-
trans-3-indolacrylic acid
-
-
trans-pyrrolidine-2,4-dicarboxylate
-
inhibition of brain KAT II
-
Tris
-
Tris buffer pH 7.5, low activity, pH 8.0, no 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
tryptophan
-
KAT I is greatly inhibited by 2 mM tryptophan
tryptophan
-
-
tryptophan
Q8BTY1, Q9WVM8
-
xanthurenate
-
weak inhibition
methionine
Q8BTY1, Q9WVM8
-
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
Hansenula schneggii
-
not inhibited by EDTA, 2,2'-dipyridyl
-
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 II is not inhibited by glutamine, tryptophan and phenylalanine
-
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
-
not inhibited by glyoxylate
-
additional information
-
KAT I is not inhibited by 2 mM methionine
-
additional information
-
KAT III is not inhibited by 5 mM tryptophan; KAT I is not inhibited by 5 mM L-methionine
-
additional information
-
glycerol is not a functional inhibitor of KAT I
-
additional information
-
KAT is not inhibited by UPF 648
-
additional information
-
indol-3ylpyruvate shows no noticeable inhibition of KAT III
-
additional information
-
(S)-(4)-(ethylsulfonyl)benzoylalanine shows no inhibition (inhibitor of the rat enzyme)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
L-cysteine
Q95VY4
at 1.25 mM, 3fold stimulation, at 10 mM, 70% inhibition
L-kynurenine
-
allosterically regulated
L-tryptophan
-
2 mM, 84% increase in activity of heart KAT at pH 8.0
pyridoxamine 5'-phosphate
Hansenula schneggii
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
21.3
-
2-Aminobutanoate
-
pH 7.5, 45C
92.7
-
2-Aminobutanoate
Q95VY4
pH 8.5, 45C
0.00241
-
2-oxo-4-methylthiobutyrate
-
0.1 mM L-kynurenine, pH 7.5, 25C
0.00438
-
2-oxo-4-methylthiobutyrate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
2.4
-
2-oxo-4-methylthiobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
5.7
-
2-oxo-4-methylthiobutyrate
-
pH 7.5, 38C
0.01
-
2-oxoadipate
-
-
20.9
-
2-oxoadipate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
3
-
2-oxobutanoate
-
pH 7.5, 45C
0.000217
-
2-oxobutyrate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.00173
-
2-oxobutyrate
-
0.1 mM L-kynurenine, pH 7.5, 25C
1
-
2-oxobutyrate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
12.7
-
2-oxobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
42.2
-
2-oxobutyrate
-
pH 7.5, 38C
1.5
-
2-oxocaproate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.5
-
2-oxocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
10.4
-
2-oxocaproic acid
-
pH 7.5, 38C
0.013
-
2-oxoglutarate
-
cosubstrate hydroxykynurenine
0.02
-
2-oxoglutarate
-
cosubstrate L-kynurenine
0.024
-
2-oxoglutarate
-
pH 9.5, 37C, KAT I
0.045
-
2-oxoglutarate
-
pH 8.0, 37C, recombinant enzyme, cosubstrate L-kyrunenine
0.096
-
2-oxoglutarate
-
pH 8.0, 37C, recombinant mitochondrial enzyme
0.62
-
2-oxoglutarate
-
pH 8.0, 37C, heart KAT, at 5 mM L-kynurenine
0.7
-
2-oxoglutarate
-
pH 7.5, 37C, cosubstrate L-kynurenine
0.879
-
2-oxoglutarate
-
pH 7.0, 37C, KAT II
1
-
2-oxoglutarate
-
pH 6.5, 37C
1.1
-
2-oxoglutarate
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate L-kynurenine
1.1
-
2-oxoglutarate
Hansenula schneggii
-
-
1.2
-
2-oxoglutarate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1.2
-
2-oxoglutarate
-
pH not specified in the publication, temperature not specified in the publication
2.4
-
2-oxoglutarate
-
pH 7.5, 38C
8.1
-
2-oxoglutarate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1
-
2-oxoisocaproate
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate L-kynurenine
1
-
2-oxoisocaproate
Hansenula schneggii
-
-
1
-
2-oxoisocaproate
-
pH 7.5, 45C
5.3
-
2-oxoisocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.2
-
2-oxovalerate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3.4
-
2-oxovalerate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
10.9
-
2-oxovalerate
-
pH 7.5, 38C
1.9
-
3-(2-aminobenzoyl)-L-alanine
Hansenula schneggii
-
pH 8.0, 37C
0.2062
-
3-hydroxykynurenine
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
12.9
-
3-methyl-2-oxobutanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
14.2
-
3-methyl-2-oxobutanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
3.3
-
4-methyl-2-oxopentanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.4
-
alpha-oxo-gamma-methiol-butyric acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.2
-
beta-phenylpyruvate
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate L-kynurenine
1.2
-
beta-phenylpyruvate
Hansenula schneggii
-
-
0.4
-
glyoxylate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.5
-
glyoxylate
-
pH 7.5, 45C
4.2
-
glyoxylate
-
pH 7.5, 38C
18
-
glyoxylate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1
-
hydroxyphenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.5
-
hydroxyphenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1.6
-
hydroxyphenylpyruvate
-
pH 7.5, 38C
0.5
-
indo-3-pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.4
-
indo-3-pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
3.6
-
Indole-3-pyruvate
-
pH 7.5, 38C
1.36
-
L-3-Hydroxykynurenine
-
pH 8.0, 37C, recombinant enzyme
2
-
L-3-Hydroxykynurenine
-
pH 6.5, 37C
2.5
-
L-3-Hydroxykynurenine
-
pH 7.2, 37C, kidney mitochondria
5
-
L-3-Hydroxykynurenine
-
pH 7.2, 37C, liver supernatant
5.3
-
L-3-Hydroxykynurenine
-
pH 7.2, 37C, kidney supernatant
6.3
-
L-3-Hydroxykynurenine
-
pH 7.2, 37C, liver mitochondria
6.2
-
L-alanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
246
-
L-alanine
Q95VY4
pH 8.5, 45C
1.4
-
L-asparagine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
6.1
-
L-asparagine
Q95VY4
pH 8.5, 45C
23.1
-
L-asparagine
-
pH 7.5, 45C
0.7
-
L-cysteine
-
pH 7.5, 45C
0.7
-
L-cysteine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.3
-
L-cysteine
Q95VY4
pH 8.5, 45C
5.6
-
L-glutamate
-
pH 8.0, 37C, alpha-aminoadipate aminotransferase activity
0.7
-
L-glutamine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
2.8
-
L-glutamine
-
pH 7.5, 45C
3.8
-
L-glutamine
Q95VY4
pH 8.5, 45C
0.7
-
L-histidine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.5
-
L-histidine
Q95VY4
pH 8.5, 45C
5.4
-
L-histidine
-
pH 7.5, 45C
0.083
-
L-kynurenine
-
pH 8.0, 37C, recombinant enzyme, cosubstrate 2-oxoglutarate
0.1116
-
L-kynurenine
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.2
-
L-kynurenine
-
E61G mutant KAT I from brain
0.25
-
L-kynurenine
-
pH 8.0. 30C
0.95
-
L-kynurenine
-
pH 8.0, 37C, recombinant enzyme
0.96
-
L-kynurenine
-
discontinuous assay, pH 7.5, 45C
1.2
-
L-kynurenine
-
pH 8.0, 37C, recombinant enzyme, cosubstrate pyruvate
1.4
-
L-kynurenine
-
pH 6.5, 37C
1.4
-
L-kynurenine
-
recombinant brain KAT I
1.5
-
L-kynurenine
-
pH 7.5, 37C
1.5
-
L-kynurenine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.6
-
L-kynurenine
-
pH 6.5, 37C, enzyme from supernatant
1.7
-
L-kynurenine
-
pH 8.0, 37C, cosubstrate pyruvate
2.09
-
L-kynurenine
-
continuous assay, pH 7.5, 45C
2.2
-
L-kynurenine
Hansenula schneggii
-
-
2.5
-
L-kynurenine
-
pH 7.2, 37C, kidney supernatant
2.5
-
L-kynurenine
-
pH 6.5, 37C, mitochondrial enzyme
3
-
L-kynurenine
-
pH 7.2, 37C, liver supernatant
3.4
-
L-kynurenine
-
pH 7.2, 37C, kidney mitochondria
4
-
L-kynurenine
-
-
4.3
-
L-kynurenine
-
-
4.3
-
L-kynurenine
Q95VY4
pH 8.5, 45C
4.7
-
L-kynurenine
-
pH 7.5, 45C
4.7
-
L-kynurenine
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
5
-
L-kynurenine
-
pH 7.2, 37C, liver mitochondria
20
-
L-kynurenine
-
pH 8.0, 37C, heart KAT, cosubstrate 5 mM pyruvate
27
-
L-kynurenine
-
pH 8.0, 37C, heart KAT, cosubstrate 5 mM 2-oxoglutarate
5
-
L-leucine
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate 2-oxoglutarate
5
-
L-leucine
Hansenula schneggii
-
-
7.6
-
L-leucine
-
pH 7.5, 45C
34.5
-
L-leucine
Q95VY4
pH 8.5, 45C
0.9
-
L-methionine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.4
-
L-methionine
Q95VY4
pH 8.5, 45C
5
-
L-methionine
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate 2-oxoglutarate
5
-
L-methionine
Hansenula schneggii
-
-
6.4
-
L-methionine
-
pH 7.5, 45C
1.1
-
L-phenylalanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.7
-
L-phenylalanine
-
pH 7.5, 45C
3.5
-
L-phenylalanine
Q95VY4
pH 8.5, 45C
3
-
L-serine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
32.7
-
L-serine
Q95VY4
pH 8.5, 45C
1.2
-
L-tryptophan
-
pH 7.5, 45C
2.6
-
L-tryptophan
Hansenula schneggii
-
pH 8.0, 37C, cosubstrate 2-oxoglutarate
2.6
-
L-tryptophan
Hansenula schneggii
-
-
7.1
-
L-tryptophan
-
in 100 mM boric acid buffer, pH 9.0, at 45C
12.9
-
L-tryptophan
Q95VY4
pH 8.5, 45C
0.9
-
L-tyrosine
Q95VY4
pH 8.5, 45C
2.7
-
L-tyrosine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3.2
-
L-tyrosine
-
pH 7.5, 45C
2.7
-
L-Vinylglycine
Hansenula schneggii
-
pH 8.0. 25C
2.4
-
Mercaptopyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
2.5
-
Mercaptopyruvate
-
pH 7.5, 45C
2.8
-
Mercaptopyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.9
-
oxaloacetate
-
pH 7.5, 38C
4.2
-
oxaloacetate
-
pH 7.5, 45C
4.9
-
oxaloacetate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
16.8
-
oxaloacetate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.6
-
phenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
0.7
-
phenylpyruvate
-
pH 7.5, 38C
0.8
-
phenylpyruvate
-
pH 7.5, 45C
1.8
-
phenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.00085
-
pyridoxal 5'-phosphate
-
pH 6.5, 37C
0.0013
-
pyridoxal 5'-phosphate
Hansenula schneggii
-
pH 8.0, 37C
0.0032
-
pyridoxamine 5'-phosphate
Hansenula schneggii
-
pH 8.0, 37C
0.0175
-
pyruvate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.053
-
pyruvate
-
pH 9.5, 37C, KAT I
0.1
-
pyruvate
-
E61G mutant KAT I from brain
0.7
-
pyruvate
-
pH 7.5, 37C, cosubstrate L-kynurenine
0.717
-
pyruvate
-
pH 7.0, 37C, KAT II
1.15
-
pyruvate
-
pH 8.0, 37C, heart KAT, at 5 mM L-kynurenine
1.2
-
pyruvate
-
recombinant brain KAT I
1.63
-
pyruvate
-
pH 8.0, 37C, recombinant mitochondrial enzyme
8.3
-
pyruvate
-
pH 7.5, 38C
9.7
-
pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
10.6
-
pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
12.1
-
pyruvate
-
pH 7.5, 45C
3.2
-
Mercaptopyruvate
-
pH 7.5, 38C
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
-
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, 0.25 pM/g wet tissue/hour, retina, 1.65, isoform KAT II, vitreous body, 0.25 pM/g wet tissue/hour, retina 2.37
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
38.3
-
2-Aminobutanoate
-
pH 7.5, 45C
317
-
2-Aminobutanoate
Q95VY4
pH 8.5, 45C
0.16
-
2-oxo-4-methylthiobutyrate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.41
-
2-oxo-4-methylthiobutyrate
-
pH 7.5, 38C
4.27
-
2-oxo-4-methylthiobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
4.84
-
2-oxoadipate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
234
-
2-oxobutanoate
-
pH 7.5, 45C
0.0018
-
2-oxobutyrate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.69
-
2-oxobutyrate
-
pH 7.5, 38C
2.93
-
2-oxobutyrate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3.49
-
2-oxobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
4.83
-
2-oxocaproate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.41
-
2-oxocaproic acid
-
pH 7.5, 38C
2.59
-
2-oxocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
0.37
-
2-oxoglutarate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
0.53
-
2-oxoglutarate
-
pH 7.5, 38C
7.67
-
2-oxoglutarate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
296
-
2-oxoisocaproate
-
pH 7.5, 45C
0.74
-
2-oxoisocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
0.13
-
2-oxovalerate
-
pH 7.5, 38C
2.66
-
2-oxovalerate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
2.7
-
2-oxovalerate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
65.12
-
3-hydroxykynurenine
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
0.92
-
3-methyl-2-oxobutanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.92
-
3-methyl-2-oxopentanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
2.51
-
4-methyl-2-oxopentanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1.02
-
alpha-oxo-gamma-methiol-butyric acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
0.19
-
glyoxylate
-
pH 7.5, 38C
2.71
-
glyoxylate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3.64
-
glyoxylate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
263
-
glyoxylate
-
pH 7.5, 45C
0.39
-
hydroxyphenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.41
-
hydroxyphenylpyruvate
-
pH 7.5, 38C
1.48
-
hydroxyphenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.03
-
indo-3-pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1.49
-
indo-3-pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.49
-
Indole-3-pyruvate
-
pH 7.5, 38C
1.53
-
L-alanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1540
-
L-alanine
Q95VY4
pH 8.5, 45C
2.93
-
L-asparagine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
14.4
-
L-asparagine
-
pH 7.5, 45C
230
-
L-asparagine
Q95VY4
pH 8.5, 45C
1.3
-
L-cysteine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
9.6
-
L-cysteine
-
pH 7.5, 45C
206
-
L-cysteine
Q95VY4
pH 8.5, 45C
2.27
-
L-glutamine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
440
-
L-glutamine
-
pH 7.5, 45C
561
-
L-glutamine
Q95VY4
pH 8.5, 45C
2
-
L-histidine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
143
-
L-histidine
-
pH 7.5, 45C
168
-
L-histidine
Q95VY4
pH 8.5, 45C
1.8
-
L-kynurenine
-
continuous assay, pH 7.5, 45C
2.2
-
L-kynurenine
-
discontinuous assay, pH 7.5, 45C
2.3
-
L-kynurenine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
9.76
-
L-kynurenine
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
55.5
-
L-kynurenine
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
172
-
L-kynurenine
Q95VY4
pH 8.5, 45C
201
-
L-kynurenine
-
pH 7.5, 45C
339
-
L-leucine
-
pH 7.5, 45C
758
-
L-leucine
Q95VY4
pH 8.5, 45C
2.43
-
L-methionine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
163
-
L-methionine
Q95VY4
pH 8.5, 45C
215
-
L-methionine
-
pH 7.5, 45C
2.7
-
L-phenylalanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
91
-
L-phenylalanine
-
pH 7.5, 45C
283
-
L-phenylalanine
Q95VY4
pH 8.5, 45C
2.17
-
L-serine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
345
-
L-serine
Q95VY4
pH 8.5, 45C
3.57
-
L-tryptophan
-
in 100 mM boric acid buffer, pH 9.0, at 45C
43.1
-
L-tryptophan
-
pH 7.5, 45C
283
-
L-tryptophan
Q95VY4
pH 8.5, 45C
1.03
-
L-tyrosine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
91
-
L-tyrosine
-
pH 7.5, 45C
139
-
L-tyrosine
Q95VY4
pH 8.5, 45C
0.44
-
Mercaptopyruvate
-
pH 7.5, 38C
3.28
-
Mercaptopyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3.59
-
Mercaptopyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
234
-
Mercaptopyruvate
-
pH 7.5, 45C
0.065
-
oxaloacetate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.32
-
oxaloacetate
-
pH 7.5, 38C
3.68
-
oxaloacetate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
143
-
oxaloacetate
-
pH 7.5, 45C
0.63
-
phenylpyruvate
-
pH 7.5, 38C
2.53
-
phenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
4.73
-
phenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
110
-
phenylpyruvate
-
pH 7.5, 45C
0.36
-
pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
0.37
-
pyruvate
-
pH 7.5, 38C
1.87
-
pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
2.02
-
pyruvate
B1B6U5
in 200 mM phosphate buffer, pH 7.5, at 37C
29
-
pyruvate
-
pH 7.5, 45C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2-oxo-4-methylthiobutyrate
-
pH 7.5, 38C
5100
1.75
-
2-oxo-4-methylthiobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
5100
0.23
-
2-oxoadipate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1184
0.02
-
2-oxobutyrate
-
pH 7.5, 38C
371
0.27
-
2-oxobutyrate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
371
2.93
-
2-oxobutyrate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
371
8.2
-
2-oxobutyrate
B1B6U5
in 200 mM phosphate buffer, pH7.5, at 37C
371
3.13
-
2-oxocaproate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
3676
0.04
-
2-oxocaproic acid
-
pH 7.5, 38C
14934
5.18
-
2-oxocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
14934
0.045
-
2-oxoglutarate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
34
0.22
-
2-oxoglutarate
-
pH 7.5, 38C
34
6.24
-
2-oxoglutarate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
34
0.14
-
2-oxoisocaproic acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
27233
0.01
-
2-oxovalerate
-
pH 7.5, 38C
1316
0.78
-
2-oxovalerate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1316
2.25
-
2-oxovalerate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
1316
315
-
3-hydroxykynurenine
B1B6U5
in 200 mM phosphate buffer, pH7.5, at 37C
2461
0.07
-
3-methyl-2-oxobutanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
829
0.065
-
3-methyl-2-oxopentanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
1133
0.76
-
4-methyl-2-oxopentanoate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
722
36.8
-
alpha-keto-gamma-methylthiobutyrate
B1B6U5
in 200 mM phosphate buffer, pH7.5, at 37C
177096
2.54
-
alpha-oxo-gamma-methiol-butyric acid
-
in 100 mM boric acid buffer, pH 9.0, at 45C
27232
0.05
-
glyoxylate
-
pH 7.5, 38C
101
0.2
-
glyoxylate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
101
6.78
-
glyoxylate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
101
0.26
-
hydroxyphenylpyruvate
-
pH 7.5, 38C
3899
0.27
-
hydroxyphenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
3899
1.48
-
hydroxyphenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
3899
1.08
-
indo-3-pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
12081
2.07
-
indo-3-pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
12081
0.13
-
Indole-3-pyruvate
-
pH 7.5, 38C
2408
0.25
-
L-alanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
103
2.095
-
L-asparagine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
266
1.86
-
L-cysteine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
74
3.24
-
L-glutamine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
102
2.86
-
L-histidine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
349
1.53
-
L-kynurenine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
409
3.27
-
L-kynurenine
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
409
500
-
L-kynurenine
B1B6U5
in 200 mM phosphate buffer, pH7.5, at 37C
409
2.7
-
L-methionine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
88
2.45
-
L-phenylalanine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
104
0.72
-
L-serine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
95
0.5
-
L-tryptophan
-
in 100 mM boric acid buffer, pH 9.0, at 45C
119
0.38
-
L-tyrosine
-
in 100 mM boric acid buffer, pH 9.0, at 45C
109
0.14
-
Mercaptopyruvate
-
pH 7.5, 38C
5576
1.23
-
Mercaptopyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
5576
1.37
-
Mercaptopyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
5576
0.09
-
oxaloacetate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
57
0.35
-
oxaloacetate
-
pH 7.5, 38C
57
0.75
-
oxaloacetate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
57
0.96
-
phenylpyruvate
-
pH 7.5, 38C
198
2.62
-
phenylpyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
198
4.22
-
phenylpyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
198
0.04
-
pyruvate
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37C
31
0.05
-
pyruvate
-
pH 7.5, 38C
31
0.18
-
pyruvate
-
in 100 mM boric acid buffer, pH 9.0, at 45C
31
116
-
pyruvate
B1B6U5
in 200 mM phosphate buffer, pH7.5, at 37C
31
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02011
-
2-oxoglutarate
-
pH 7.5, 25C
13
-
Adipate
Hansenula schneggii
-
-
0.013
-
cysteine sulfinate
-
17.2 mM dissociation constant for dissociation of the inhibitor from the enzyme substrate complex, pH 7.5, 25C
9.5
-
pimelate
Hansenula schneggii
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00091
-
(S)-(-)-9-(4-aminopiperazin-1-yl)-8-fluoro-3-methyl-6-oxo-2,3-dihydro-6H-1-oxa-3a-azaphenalene-5-carboxylic acid
-
0.0015 mM or the two enantiomers, pH 8.0, 37C
-
0.293
-
3-(2-carboxyethyl)-5-chloro-1H-indole-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.666
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.02
-
5-(2-(3-chlorophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.021
-
5-(2-(4-bromophenyl)hydrazono)-6-ethoxy-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.02
-
5-(2-(4-chlorophenyl) hydrazono)-6-ethoxy-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.271
-
5-bromo-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.034
-
6-ethoxy-5-(2-(4-iodophenyl)hydrazono)-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.043
-
6-ethoxy-5-(2-(4-methoxyphenyl)hydrazono)-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.179
-
6-ethoxy-5-(2-(4-nitrophenyl)hydrazono)-6-oxohexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.033
-
6-ethoxy-6-oxo-5-(2-p-tolylhydrazono)hexanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.002
-
cysteine sulfinate
-
pH 7.5, 25C
0.14
-
Indole-3-propionic acid
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.13
-
-
isoenzyme 2
0.13
-
-
hydroxykynurenine
0.17
-
Hansenula schneggii
-
-
1.5
-
-
L-kynurenine
1.5
-
-
L-kynurenine
16.9
-
Hansenula schneggii
-
-
71.7
-
-
pH 7.0, 55C
additional information
-
-
prawns at intermoult show significant higher KAT activity compared to prawns from premoult
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
with L-kynurenine as substrate
7
7.5
-
KAT II
7
8
-
KAT II from brain
7
8
Q8BTY1, Q9WVM8
-
7
9
-
KAT IV
7
-
-
KAT II
7.4
10
-
KAT I
7.5
-
-
with L-alpha-aminoadipate as substrate
7.5
-
-
liver KAT I
8
9
-
heart enzyme
8
9
-
heart KAT I
8
-
Hansenula schneggii
-
-
8
-
-
KAT IV
8
-
Q8BTY1, Q9WVM8
-
8.3
-
-
KAT I
8.5
-
Q95VY4
optima at pH 8.5 and 10.0
8.8
-
-
total placental KAT activity
9
10
-
KAT III
9
9.5
-
KAT I
9
-
Q8BTY1, Q9WVM8
;
9.5
10
-
optimal pH range of human brain and placenta KAT I
9.6
10
-
KAT I from brain, sharp optimum
9.8
-
-
placental KAT I activity
10
-
Q95VY4
optima at pH 8.5 and 10.0
additional information
-
-
pI: 6.56
additional information
-
Hansenula schneggii
-
pI: 4.95
additional information
-
-
pI: 6.56
additional information
-
-
pI: 5.9
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
9.2
-
approx. half-maximal activity at pH 6.2, approx. 60% of maximal activity at pH 9.2
6.5
8.8
-
maximal activity at pH 6.5, approx. half-maximal activity at pH 8.8
7.5
9
-
-
8
11
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
Hansenula schneggii
-
assay at
50
60
-
-
50
-
-
-
59
-
Q8BTY1, Q9WVM8
-
60
70
Q8BTY1, Q9WVM8
-
60
-
Hansenula schneggii
-
-
60
-
Q95VY4
recombinant enzyme
60
-
Q8BTY1, Q9WVM8
;
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
45
-
linear increase in activity
20
60
Hansenula schneggii
-
linear increase of activity
40
70
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
B1B6U5
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
astrocytes in the substantia nigra express KAT-I under normal conditions. The amount of this enzyme increases after administration of 6-hydroxydopamine
Manually annotated by BRENDA team
-
KAT I activity is significantly lower in plasma of patients with Parkinson's disease when compared with normal individuals; KAT II activity is significantly lower in plasma of patients with Parkinson's disease when compared with normal individuals
Manually annotated by BRENDA team
-
frontal and temporal cortex
Manually annotated by BRENDA team
-
KAT I and KAT II
Manually annotated by BRENDA team
-
KAT I activity in glial cells of striatum, in astrocytes of the hippocampus and in glial cells of the temporal lobe
Manually annotated by BRENDA team
-
no difference in mRNA levels for KAT-1 when schizophrenic individuals are compared with normal individuals
Manually annotated by BRENDA team
-
in some parts, only faint expression of isoform KAT II, and occasionally no staining. No association of staining variability for KAT II and localization of Corpora amylacea
Manually annotated by BRENDA team
-
KAT II may be involved in mechanisms of retinal ageing and neurodegeneration leading to formation of corpora amylacea; KAT I may be involved in mechanisms of retinal ageing and neurodegeneration leading to formation of corpora amylacea
Manually annotated by BRENDA team
-
increase in KAT II activity in plasma of patients with Parkinson's disease when compared with normal individuals; no difference in KAT I activity between normal individuals and patients with Parkinson's disease
Manually annotated by BRENDA team
-
highest activity in cerebral ganglion, low activity in thoracic and abdominal ganglion
Manually annotated by BRENDA team
-
microglial cells become KAT-I immunoreactive only after treatment with 6-hydroxydopamine
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
KAT I and KAT II, major activity is performed by KAT II, KAT I contributes to 1/15 of total kynurenine aminotransferase activity
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
neuronal culture prepared from cortices of 18-day-old fetuses; neuronal culture prepared from cortices of 18-day-old fetuses
Manually annotated by BRENDA team
-
oligodendrocyte cell line
Manually annotated by BRENDA team
-
expression of both isoforms KAT I and KAT II. KAT I immunoreactivity is more intense than KAT II, and its staining is more pronounced in the retrolaminar part of the optic nerve
Manually annotated by BRENDA team
-
KAT I, low activity
Manually annotated by BRENDA team
-
no difference in mRNA levels for KAT-1 when schizophrenic individuals are compared with normal individuals
Manually annotated by BRENDA team
-
expression of both isoforms KAT I and KAT II. KAT I immunoreactivity is more intense than KAT II, and its staining is more pronounced in the retrolaminar part of the optic nerve. Isoform KAT I is observed on Mueller cell endfeet while KAT II is expressed in retinal ganglion cells; KAT II is expressed in retinal ganglion cells; KAT I is observed on Mller cell endfeet
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
KAT 1, low activity
Manually annotated by BRENDA team
-
pars compacta. Neurons and glial cells. Treatment with 6-hydroxydopamine produces loss of the majority of nigral neurons. KAT-I diminished considerably in the remaining neurons. Astrocytes in the substantia nigra express KAT-I under normal conditions, the amount of this enzyme increases after administration of 6-hydroxydopamine. Microglial cells become KAT-I immunoreactive only after treatment with 6-hydroxydopamine
Manually annotated by BRENDA team
-
KAT I, low activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q08415
KAT I, the enzyme exists in a cytosolic and in a mitochondrial form because of the presence of 2 different KAT I mRNAs coding for a protein respectively with and without leader sequence targeting the protein into mitochondria
Manually annotated by BRENDA team
-
KAT I of astroglial cells is associated with ribosomes of the endoplasmic reticulum
Manually annotated by BRENDA team
-
10% of liver total activity at pH 6.5
Manually annotated by BRENDA team
Rattus norvegicus Donryu
-
10% of liver total activity at pH 6.5
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
40% of kidney total activity; 80% of liver total activity
Manually annotated by BRENDA team
-
cDNA encodes for a kynurenine aminotransferase that is identical to a soluble form but carries an additional stretch of 32 amino acids resembling a mitochondrial import sequence
Manually annotated by BRENDA team
Q95VY4
deduced amino acid sequence contains a mitochondrial leader sequence
Manually annotated by BRENDA team
Rattus norvegicus Donryu
-
;
-
Manually annotated by BRENDA team
-
60% of kidney total activity
-
Manually annotated by BRENDA team
-
12% of liver total activity at pH 6.5
-
Manually annotated by BRENDA team
-
brain KAT I
-
Manually annotated by BRENDA team
Rattus norvegicus Donryu
-
; 12% of liver total activity at pH 6.5
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
additional information
Rattus norvegicus Donryu
-
subcellular distribution
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43100
-
B1B6U5
gel filtration
45000
-
B1B6U5
SDS-PAGE
46480
-
B1B6U5
calculated from amino acid sequence
85000
-
-
gel filtration, sucrose density gradient centrifugation
90000
100000
-
gel filtration
91000
-
-
gel filtration
97000
-
Q95VY4
truncated recombinant enzyme, gel filtration
98000
-
Hansenula schneggii
-
sedimentation equilibrium
100000
-
-
isoenzyme 2, sucrose density gradient centrifugation
100000
-
-
gel filtration
102000
-
Hansenula schneggii
-
native PAGE
106000
-
Hansenula schneggii
-
gel filtration
additional information
-
Hansenula schneggii
-
amino acid composition
additional information
-
-
amino acid composition
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q95VY4
x * 53000, SDS-PAGE; x * 53490, deduced from nucleotide sequence
?
-
x * 46000, SDS-PAGE, x * 47875, calculated
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE in the absence of 2-mercaptoethanol; 2 * 45500, SDS-PAGE in the presence of 2-mercaptoethanol
dimer
Hansenula schneggii
-
2 * 52000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE in the absence of 2-mercaptoethanol
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 49500, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
Q95VY4
2 * 48000, truncated recombinant enzyme, SDS-PAGE
dimer
-
2 * 49000, SDS-PAGE
dimer
-
crystallization data
dimer
Pyrococcus horikoshii OT-3
-
2 * 49000, SDS-PAGE
-
dimer
Rattus norvegicus Wistar
-
2 * 49500, SDS-PAGE
-
homodimer
-
x-ray crystallography
homodimer
-
crystal structure analysis
homodimer
-
2 * 48000, SDS-PAGE, crystal structure
homodimer
O57946
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
-
Hansenula schneggii
-
5-pyridoxal phosphate and pyridoxamine form and in complex with competing substrate L-phenylalanine
-
Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does
-
in complex with 3-indolepropionic acid or DL-indole-3-lactic acid, hanging drop vapor diffusion method, using 22% (w/v) PEG 4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5
-
KAT II complex with 2-oxoglutarate, hanging drop vapor diffusion method
-
native enzyme and selenomethionine derivative, diffraction to 2.3 A and 2.4 A resolution, respectively. Structure reveals an antiparallel strand-loopstrand motif that forms an unprecedented intersubunit beta-sheet in the functional KAT II dimer. The N-terminal regions of KAT II and aspartate aminotransferase appear to have converged to highly similar although 2fold symmetry-related conformations, which fulfill the same functional role. Structural comparison of isoforms KAT I and KAT II reveals a larger and more aliphatic character to the active site of KAT II due to the absence of the aromatic cage involved in ligand binding in KAT I
-
native enzyme, diffraction to 2.16 A resolution, in complex with kynurenine, diffraction to 1.95 A. Enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes and shows a unique folding of its first 65 N-terminal residues
Q8N5Z0
PEG 3350
-
hanging-drop vapor diffusion method, PEG 4000,
-
in complex with L-kynurenine and L-glutamine, hanging drop vapor diffusion method, using 21% (w/v) polyethylene glycol 400, 10% glycerol, 150 mM CaCl2, and 100 mM HEPES, pH 7.5
-
monomer structure model of phKAT-II is refined at a resolution of 2.20 A. A single molecule of phKAT-II is present in an asymmetric unit of the crystal
-
sitting-drop vapor diffusion method
-
the crystal structure of the enzyme in complex with pyridoxamine phosphates, kynurenine and kynurenic acid, 1.85 A resolution
O57946
diffraction to 2.0 A resolution, comparison with crystallization data from Aspergillus fumigatus, Dictyostelium discoideum, Aedes aegypti, Trypanosoma brucei, Rattus norvegicus, and Homo sapiens
P47039
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
75 min, inactivation, t1/2: 30 min
5
-
-
and below, inactivation even in the presence of pyridoxal phosphate
6.5
7.5
-
most stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
phosphate buffer, pH 6.3, inactivation within a few min, pyridoxal phosphate restores activity, only slow inactivation at pH 7.4, 2-oxoglutarate protects
40
-
-
and above, 5 min, decreasing activity
50
-
Hansenula schneggii
-
and below, 5 min stable between pH 6.0 and pH 10.0
50
-
-
in 20% glycerol, 0.1 mM DTT, 2 mM pyridoxal phosphate, 25 mM imidazole-HCl buffer, pH 7, 30 min stable
55
-
B1B6U5
the enzymatic activities starts to decrease dramatically when the temperature is above 55C
65
-
Hansenula schneggii
-
above, rapid inactivation
70
-
-
5 min, complete inactivation
70
-
-
20 min, inactivation
additional information
-
Q8BTY1, Q9WVM8
midpoint temperature of protein melting 64.8C, calculated half life time value at 65C 3.9 min; midpoint temperature of protein melting 65.9C, calculated half life time value at 65C 27.4 min; midpoint temperature of protein melting 66.5C, calculated half life time value at 65C 6.5 min; midpoint temperature of protein melting 68.8C, calculated half life time value at 65C 69.7 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated freeze-thawing inactivates enzyme irriversible in dilute solution, below 0.1 mg/ml
Hansenula schneggii
-
alcohol fractionation inactivates
-
ammonium sulfate fractionation inactivates
-
dialysis against phosphate buffer inactivates, 2-oxoglutarate protects to some extent
-
dialysis of the apoenzyme against Tris-HCl or imidazole-HCl buffer inactivates
-
freeze-thawing inactivates
-
slightly acidic buffer solutions inactivate, pyridoxal phosphate or pyridoxamine phosphate restores activity, 2-oxoglutarate protects
-
stable in phosphate buffer supplemented with pyridoxal phosphate
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, at protein concentrations above 0.6 mg/ml, 0.02 mM pyridoxal phosphate, 0.01% mercaptoethanol, several weeks, no loss of activity
Hansenula schneggii
-
4C, crystalline enzyme as suspension in 70% saturated ammonium sulfate, pH 7.2, more than 6 months
Hansenula schneggii
-
-80C, isolated KAT II, no noticeable decrease in specific activity
-
freezing and thawing do not alter the activity
-
full activity after 12 month at -80C, 50 mM HEPES/NaOH, pH 7.5, 100 mM NaCl
-
-20C, in 10 mM phosphate buffer, pH 7, 50% glycerol, at least 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
truncated recombinant enzyme, DEAE-Sepharose, native PAGE
Q95VY4
glutathione-Sepharose column chromatography
B1B6U5
-
Hansenula schneggii
-
polyethyleneimine, DEAE-cellulose, Bio-Gel P-300, hydroxyapatite, crystallization
Hansenula schneggii
-
DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant protein
-
affinity chromatography, ion exchange chromatography (Q-Sepharose), gel filtration
-
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration; chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration; chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration; chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
Q8BTY1, Q9WVM8
DEAE Sepharose column chromatography, hydroxyapatite column chromatography, Mono-Q column chromatography, and gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant protein
-
acid precipitation, ammonium sulfate, DEAE-cellulose, hydroxylapatite
-
ammonium sulfate, DEAE-Sepharose, phenyl-Sepharose, Mono Q, Mono P
-
DEAE-cellulose, heat treatment, hydroxyapatite, CM-Sephadex C-25, Sephadex G-100
-
DEAE-Sepharose, ammonium sulfate, Sephadex G-25, partial purification of KAT I and KAT II
-
DEAE-Sepharose, phenyl-Sepharose, Superose 12, Mono Q
-
partial purification
-
partial purification of kynurenine apotransaminase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of full length enzyme and truncated version lacking the mitochondrial leader sequence in Sf9 insect cells
Q95VY4
expressed as a glutathione S-transferase fusion protein in soluble form Escherichia coli DH5alpha cells
B1B6U5
expression in Escherichia coli
-
expression of KAT I in Cos-1 cells
-
His-tagged protein expressed in Sf21 cells, hydrophobic interaction chromatography, gel filtration
-
maltose-binding protein fusion protein expressed in Escherichia coli BL21(DE3)
-
chitin-binding domain fusion proteinfusionexpressed in Escherichia coli
-
expressed in Sf9 insect cells
-
tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli; tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli; tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli; tagged protein (consisting of an intein and a chitin binding domain) expressed in Escherichia coli
Q8BTY1, Q9WVM8
His-tagged protein expressed in Escherichia coli BL21-CodonPlus (DE3)
-
transient expression in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protein expression levels increase during the blood-feeding course
B1B6U5
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Y142F
-
active site mutation
E61G
-
40-60% of wild-type activity, Km for L-kynurenine and pyruvate is reduced, missense mutation found in spontaneously hypertensive rats
E64G
-
the naturally occurring mutation in rat KAT I results in dramatically impaired kynurenic acid synthesis and in an associated spontaneously hypertensive phenotype
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
isoforms KAT I and KAT II, no change of enzyme activity 24 and 72 h after transient global ischemia episode