2.6.1.39: 2-aminoadipate transaminase
This is an abbreviated version!
For detailed information about 2-aminoadipate transaminase, go to the full flat file.
Word Map on EC 2.6.1.39
-
2.6.1.39
-
5'-phosphate
-
thermus
-
saccharopine
-
aminotransferases
-
thermophilus
-
transamination
-
dicarboxylic
-
semialdehyde
-
kynurenic
-
l-kynurenine
-
2-oxoadipate
-
l-lysine
-
pharmacology
-
medicine
- 2.6.1.39
- 5'-phosphate
-
thermus
- saccharopine
- aminotransferases
- thermophilus
-
transamination
-
dicarboxylic
- semialdehyde
-
kynurenic
- l-kynurenine
- 2-oxoadipate
- l-lysine
- pharmacology
- medicine
Reaction
Synonyms
2-aminoadipate aminotransferase, 2-aminoadipic aminotransferase, AAA-AT, AadAT, AAT, alpha-aminoadipate aminotransferase, alpha-aminoadipate aminotransferase (gene aro8), aminoadipate aminotransferase, aminoadipate aminotransferase/kynurenine aminotransferase II, Aro8, GKAT, glutamate-alpha-ketoadipate transaminase, glutamic-ketoadipic transaminase, halogenated tyrosine aminotransferase, KAT II/AADAT, kynurenine aminotransferase II, kynurenine aminotransferase II (EC 2.6.1.7), kynurenine/alpha-aminoadipate aminotransferase, More
ECTree
2.6.1.39 2-aminoadipate transaminaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.6.1.39 - 2-aminoadipate transaminase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1
L-phenylalanine
-
pH 7.0, temperature not specified in the publication
0.5
L-tyrosine
-
pH 7.0, temperature not specified in the publication
0.12
2-oxoadipate
-
pH 7.0, temperature not specified in the publication
0.27
2-oxoglutarate
wild type enzyme, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.3
2-oxoglutarate
wild type enzyme, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.4
2-oxoglutarate
mutant enzyme S20E, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.41
2-oxoglutarate
mutant enzyme S20E, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.42
2-oxoglutarate
mutant enzyme R23Q, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.54
2-oxoglutarate
mutant enzyme R23A, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.55
2-oxoglutarate
mutant enzyme R23Q, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.61
2-oxoglutarate
mutant enzyme R23A, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
3.6
2-oxoglutarate
-
pH 7.0, temperature not specified in the publication
0.048
2-oxoisocaproate
mutant enzyme R23A, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.05
2-oxoisocaproate
mutant enzyme S20E, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.091
2-oxoisocaproate
mutant enzyme R23Q, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.43
2-oxoisocaproate
wild type enzyme, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.81
L-2-aminoadipate
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
3.3
L-2-aminoadipate
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
7
L-2-aminoadipate
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
8.8
L-2-aminoadipate
-
pH 7.0, temperature not specified in the publication
11
L-2-aminoadipate
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.46
L-glutamate
wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
26
L-glutamate
-
pH 7.0, temperature not specified in the publication
62
L-glutamate
mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
82
L-glutamate
mutant enzyme S20E, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
250
L-glutamate
mutant enzyme R23A, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.2
L-leucine
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.39
L-leucine
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.88
L-leucine
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.95
L-leucine
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
