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Information on EC 2.6.1.39 - 2-aminoadipate transaminase and Organism(s) Thermus thermophilus and UniProt Accession Q72LL6
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2.6.1.39 2-aminoadipate transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 2.6.1.39
- 5'-phosphate
-
thermus
- saccharopine
- aminotransferases
- thermophilus
-
transamination
-
dicarboxylic
- semialdehyde
-
kynurenic
- l-kynurenine
- 2-oxoadipate
- l-lysine
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-aminoadipate aminotransferase, aaa-at, 2-aminoadipate aminotransferase, glutamate-alpha-ketoadipate transaminase, kat ii/aadat, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminoadipate aminotransferase
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-
-
-
2-aminoadipic aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
alpha-aminoadipate aminotransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9033-00-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
?
2-oxo-3-methylvalerate + L-glutamate
2-amino-3-methylpentanoate + 2-oxoglutarate
-
-
-
-
?
2-oxoadipate + L-glutamate
L-2-aminoadipate + 2-oxoglutarate
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
-
-
-
-
?
phenylpyruvate + 2-aminoadipate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
?
additional information
?
-
negligible activity is observed for L-Asp
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-
?
additional information
?
-
-
negligible activity is observed for L-Asp
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-
?
additional information
?
-
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AAA-AT can recognize various kinds of substrates using the mobile alpha2 helix
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
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
0.04
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
0.083
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
6.7
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
0.23
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
0.5
L-glutamate
mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
1.2
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
16
L-glutamate
wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C
0.009
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
0.023
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
0.05
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
5.1
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
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
0.021
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
0.06
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
0.091
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
0.097
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
0.2
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
19
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
22
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
4.8
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
5.5
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
24
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
34
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
0.0033
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
0.0057
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
0.0075
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
8.2
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
0.0009
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
0.0081
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
0.014
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
37
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
0.023
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
0.057
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
0.12
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
5.4
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
sedimentation equilibrium analysis, equilibrium constant 2.4 + 10-5 M
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with N-(5'-phosphopyridoxyl)-L-glutamate, vapor diffusion method, using 16% (w/v) PEG3350, 100 mM HEPES, pH 7.0, and 200 mM calcium acetate, at 20°C
crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively
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in complex with pyridoxal 5'-phosphate, with pyridoxal 5'-phosphate and leucine, with N-phosphopyridoxyl-leucine, and with N-phosphopyridoxyl-alpha-aminoadipate, at 2.67, 2.26, 1.75 and 1.67 A resolution, respectively. Enzyme contains a mobile alpha2-helix involved in substrate recognition
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R23A
the mutation causes 4.1fold increase in the Km value for L-2-aminoadipate, the Km value for L-Glu increases 546fold, the Km value for L-Leu is not greatly affected
R23Q
the mutation causes 13.7fold increase in the Km value for L-2-aminoadipate, the Km value for L-Glu increases 134fold, the Km value for L-Leu is not greatly affected
S20E
the mutant shows decreased kcat values compared to the wild type enzyme
additional information
-
enzyme disruption mutant, needs longer lag phase for growth and shows slower growth in minimal medium. Addition of alpha-aminoadipate or lysine shortens the lag phase and improves growth rate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the crystal structures and site-directed mutagenesis reveales that intersubunit-electrostatic interactions contributes to the elevated thermostability of this enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miyazaki, T.; Miyazaki, J.; Yamane, H.; Nishiyama, M.
alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus
Microbiology
150
2327-2334
2004
Thermus thermophilus
Tomita, T.; Miyagawa, T.; Miyazaki, T.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus
Proteins
75
348-359
2008
Thermus thermophilus
Ouchi, T.; Tomita, T.; Miyagawa, T.; Kuzuyama, T.; Nishiyama, M.
Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-aminoadipate aminotransferase from Thermus thermophilus
Biochem. Biophys. Res. Commun.
388
21-27
2009
Thermus thermophilus (Q72LL6), Thermus thermophilus
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