Information on EC 2.6.1.39 - 2-aminoadipate transaminase

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

EC NUMBER
COMMENTARY
2.6.1.39
-
RECOMMENDED NAME
GeneOntology No.
2-aminoadipate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
show the reaction diagram
A pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Lysine biosynthesis
-
lysine biosynthesis IV
-
lysine biosynthesis V
-
Lysine degradation
-
lysine degradation II
-
lysine degradation V
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-aminoadipate aminotransferase
-
-
-
-
2-aminoadipic aminotransferase
-
-
-
-
AAA-AT
Q72LL6
-
AadAT
-
-
AadAT
Rattus norvegicus Sprague-Dawley
-
-
-
alpha-aminoadipate aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase
-
-
alpha-aminoadipate aminotransferase
Q72LL6
-
alpha-aminoadipate aminotransferase (gene aro8)
-
-
aminoadipate aminotransferase
-
-
aminoadipate aminotransferase
Q8N5Z0
-
aminoadipate aminotransferase
-
-
aminoadipate aminotransferase
Q9WVM8
-
aminoadipate aminotransferase
-
-
aminoadipate aminotransferase/kynurenine aminotransferase II
-
-
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
halogenated tyrosine aminotransferase
-
-
KAT II/AADAT
-
bifunctional enzyme with kynurenine aminotransferase activity and aminoadipate aminotransferase function
kynurenine aminotransferase II
-
-
kynurenine aminotransferase II (EC 2.6.1.7)
Q9WVM8
-
kynurenine/alpha-aminoadipate aminotransferase
-
-
additional information
-
KAT II is identical to AADAT (aminoadipate aminotransferase)
CAS REGISTRY NUMBER
COMMENTARY
9033-00-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
human
SwissProt
Manually annotated by BRENDA team
albino rat
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
bakers' yeast, haploid strains MO-11-48A and X1049-2B, diploid strain F2, clonal isolate of commercial bakers' yeast
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoadipate + pyruvate
2-oxoadipate + L-alanine
show the reaction diagram
-
-
-
-
?
2-aminoadipate + pyruvate
2-oxoadipate + L-alanine
show the reaction diagram
-
-
-
-
r
2-oxo-3-methylvalerate + L-glutamate
2-amino-3-methylpentanoate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
2-oxoadipate + L-glutamate
L-2-aminoadipate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + L-2-aminoadipate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + L-tyrosine
L-glutamate + 4-hydroxyphenylpyruvate
show the reaction diagram
-
-
-
-
r
2-oxoisocaproate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
2-oxoisocaproate + L-glutamate
?
show the reaction diagram
Q72LL6, -
-
-
-
?
2-oxoisovalerate + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
3,5-di-iodotyrosine + 2-oxoglutarate
3,5-diiodophenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
3,5-di-iodotyrosine + 2-oxoglutarate
3,5-diiodophenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
DL-2-aminopimelic acid + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
DL-2-aminopimelic acid + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
ir
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
Q64602
-
-
-
ir
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
ir
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-, Q8N5Z0
-
-
-
?
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-, Q8N5Z0
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
Q64602
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
Q72LL6, -
-
-
-
?
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-, Q8N5Z0
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
Q64602
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine and tryptophan metabolism
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
also transamination of methionine, 2-oxocaproic acid, phenylpyruvate and 2-oxo-4-methylthiobutyrate
-
-
?
L-2-aminoadipate + 4-hydroxyphenylpyruvate
2-oxoadipate + L-tyrosine
show the reaction diagram
-
-
-
-
?
L-glutamate + 4-hydroxyphenylpyruvate
2-oxoglutarate + L-tyrosine
show the reaction diagram
-
-
-
-
r
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram
Rattus norvegicus, Bos taurus, Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
Rattus norvegicus, Bos taurus, Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
Q72LL6, -
-
-
-
?
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
Bos taurus, Rattus norvegicus Sprague-Dawley
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
oxaloacetate + L-glutamate
2-aminosuccinate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
phenylpyruvate + 2-aminoadipate
L-phenylalanine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
2 isoenzymes, AadAT-I and AadAT-II, isoenzyme AadAT-II shows additional activity with tryptophan or kynurenine-2-oxoglutarate reaction, only slight activity with asparagine, alanine, arginine, ornithine, isoleucine, valine, leucine, lysine, serine, threonine, phenylalanine, tyrosine, histidine, glutamine, methionine or aspartate with 2-oxoglutarate
-
-
-
additional information
?
-
-
only slight activity with phenylalanine, tryptophan, tyrosine, aspartate or alanine as amino group donors, glyoxylate is no amino group acceptor
-
-
-
additional information
?
-
-
less than 2% activity with L-aspartate, L-alanine, L-alpha-aminobutyrate, glycine, L-valine, L-leucine, L-isoleucine, L-norvaline, L-epsilon-aminocaproate, L-threonine, L-serine, L-homoserine, L-cysteine, L-methionine, L-lysine, L-arginine, L-citrulline, L-ornithine, L-histidine, L-tyrosine, L-tryptophan, L-phenylalanine, L-proline and L-glutamate
-
-
-
additional information
?
-
-
no kynurenine aminotransferase activity
-
-
-
additional information
?
-
-
2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein
-
-
-
additional information
?
-
Q64602
2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein
-
-
-
additional information
?
-
-
2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein
-
-
-
additional information
?
-
-
KAT and AadAT activities are associated with 2 different proteins
-
-
-
additional information
?
-
-
AAA-AT can recognize various kinds of substrates using the mobile alpha2 helix
-
-
-
additional information
?
-
Q72LL6, -
negligible activity is observed for L-Asp
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
only slight activity with phenylalanine, tryptophan, tyrosine, aspartate or alanine as amino group donors, glyoxylate is no amino group acceptor, 2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein
-
-
-
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-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-, Q8N5Z0
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
Q64602
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
lysine and tryptophan metabolism
-
-
r
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-, Q8N5Z0
-
pyridoxal 5'-phosphate
Q72LL6, -
-
pyridoxal 5'-phosphate
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(S)-4-ethylsulfonylbenzoylalanine
-
-
3-methylglutaric acid
-
6 mM, 2% inhibition
3-methylglutaric acid
-
6 mM, 38% inhibition
Adipic acid
-
competitive inhibition with respect to L-kynurenine, but not to 2-oxoglutarate
Adipic acid
-
6 mM, 48% inhibition
Adipic acid
-
6 mM, 60% inhibition
alpha-aminoadipate
-
competitive inhibition against kynurenine or 3-hydroxykynurenine
azelaic acid
-
6 mM, 36% inhibition
azelaic acid
-
6 mM, 38% inhibition
Decanoic acid
-
6 mM, 50% inhibition
Decanoic acid
-
6 mM, 45% inhibition
Diethylglutaric acid
-
6 mM, 20% inhibition
Dimethylglutaric acid
-
6 mM, 15% inhibition
-
Dimethylglutaric acid
-
6 mM, 42% inhibition
-
Glutaric acid
-
6 mM, 5% inhibition
Kynurenic acid
-
1 mM, 30% inhibition
Kynurenic acid
-
1 mM, 40% inhibition
pimelic acid
-
6 mM, 28% inhibition
pimelic acid
-
6 mM, 32% inhibition
L-serine-O-sulfate
-
-
additional information
-
oxaloacetic acid is no inhibitor
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
2-Aminoadipate
-
pH 8.0, 37C isoenzyme AadAT-II
20
-
2-Aminoadipate
-
pH 8.0, 37C
0.1483
-
2-oxo-3-methylvalerate
-
pH 7.5, 45C
0.01
-
2-oxoadipate
-
pH 6.5, 37C
0.024
-
2-oxoadipate
-
pH 7.5, 45C
0.12
-
2-oxoadipate
-
pH 7.0, temperature not specified in the publication
1
-
2-oxoadipate
-
pH 8.0, 37C isoenzyme AadAT-II
2.5
-
2-oxoadipate
-
pH 8.0, 37C isoenzyme AadAT-I
0.5
-
2-oxoadipic acid
-
pH 7.0, 37C
0.27
-
2-oxoglutarate
Q72LL6, -
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 45C
0.3
-
2-oxoglutarate
Q72LL6, -
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 45C
0.4
-
2-oxoglutarate
Q72LL6, -
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 45C
0.41
-
2-oxoglutarate
Q72LL6, -
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 45C
0.42
-
2-oxoglutarate
Q72LL6, -
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 45C
0.54
-
2-oxoglutarate
Q72LL6, -
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 45C
0.55
-
2-oxoglutarate
Q72LL6, -
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 45C
0.61
-
2-oxoglutarate
Q72LL6, -
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 45C
1.1
-
2-oxoglutarate
-
pH 8.0, 37C isoenzyme AadAT-I
3.2
-
2-oxoglutarate
-
pH 8.0, 37C isoenzyme AadAT-II
3.6
-
2-oxoglutarate
-
pH 7.0, temperature not specified in the publication
0.0288
-
2-oxoisocaproate
-
pH 7.5, 45C
0.048
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.05
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.091
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.43
-
2-oxoisocaproate
Q72LL6, -
wild type enzyme, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.0133
-
2-oxoisovalerate
-
pH 7.5, 45C
1.4
-
glutamate
-
pH 8.0, 37C
0.81
-
L-2-Aminoadipate
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
3.3
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
7
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
8.8
-
L-2-Aminoadipate
-
pH 7.0, temperature not specified in the publication
11
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.46
-
L-glutamate
Q72LL6, -
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 45C
12.5
-
L-glutamate
-
pH 8.0, 37C, isoenzyme AadAT-II
26
-
L-glutamate
-
pH 7.0, temperature not specified in the publication
62
-
L-glutamate
Q72LL6, -
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 45C
82
-
L-glutamate
Q72LL6, -
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 45C
250
-
L-glutamate
Q72LL6, -
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 45C
4.6
-
L-Glutamic acid
-
pH 7.0, 37C
0.2
-
L-leucine
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.39
-
L-leucine
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.88
-
L-leucine
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.95
-
L-leucine
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
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
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.5
-
2-oxo-3-methylvalerate
-
pH 7.5, 45C
22.3
-
2-oxoadipate
-
pH 7.5, 45C
17.8
-
2-oxoisocaproate
-
pH 7.5, 45C
2.1
-
2-oxoisovalerate
-
pH 7.5, 45C
0.011
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.04
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.083
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
6.7
-
L-2-Aminoadipate
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
18.4
-
L-2-Aminoadipate
-
pH 7.0, temperature not specified in the publication
0.23
-
L-glutamate
Q72LL6, -
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 45C
0.5
-
L-glutamate
Q72LL6, -
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 45C
1.2
-
L-glutamate
Q72LL6, -
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 45C
12.8
-
L-glutamate
-
pH 7.0, temperature not specified in the publication
16
-
L-glutamate
Q72LL6, -
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 45C
0.009
-
L-leucine
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.023
-
L-leucine
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
0.05
-
L-leucine
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
5.1
-
L-leucine
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
8.3
-
L-phenylalanine
-
pH 7.0, temperature not specified in the publication
12.3
-
L-tyrosine
-
pH 7.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.015
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
0.021
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
0.06
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
0.091
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
0.097
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
0.2
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
19
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
22
-
2-oxoglutarate
Q72LL6, -
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 45C
2883
4.8
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
2896
5.5
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
2896
24
-
2-oxoisocaproate
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
2896
34
-
2-oxoisocaproate
Q72LL6, -
wild type enzyme, in 50 mM HEPESNaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45C
2896
0.0033
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
11982
0.0057
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
11982
0.0075
-
L-2-Aminoadipate
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
11982
8.2
-
L-2-Aminoadipate
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
11982
0.0009
-
L-glutamate
Q72LL6, -
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 45C
12211
0.0081
-
L-glutamate
Q72LL6, -
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 45C
12211
0.014
-
L-glutamate
Q72LL6, -
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 45C
12211
37
-
L-glutamate
Q72LL6, -
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 45C
12211
0.023
-
L-leucine
Q72LL6, -
mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
12291
0.057
-
L-leucine
Q72LL6, -
mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
12291
0.12
-
L-leucine
Q72LL6, -
mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
12291
5.4
-
L-leucine
Q72LL6, -
wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45C
12291
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.53
-
-
-
0.77
-
-
isoenzyme AadAT-I
1.5
-
-
kynurenine aminotransferase activity
1.56
-
Q64602
-
2.65
-
-
kynurenine aminotransferase activity
6.3
-
-
alpha-aminoadipate aminotransferase activity
10.68
-
-
isoenzyme AadAT-II
26.1
-
-
alpha-aminoadipate aminotransferase activity
513
-
-
substrate phenylpyruvate, pH 7.5, 45C
561
-
-
substrate 2-oxo-3-methylvalerate, pH 7.5, 45C
568
-
-
substrate pyruvate, pH 7.5, 45C
661
-
-
substrate oxaloacetate, pH 7.5, 45C
1102
-
-
substrate 2-oxoisovalerate, pH 7.5, 45C
5079
-
-
substrate 2-oxoisocaproate, pH 7.5, 45C
6788
-
-
substrate 2-oxoadipate, pH 7.5, 45C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
kynurenine aminotransferase activity
7
8
Q9WVM8
-
9
9.5
-
isoenzyme AadAT-II
9.5
-
-
isoenzyme AadAT-I
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9.6
-
The V/Et and V/Kalpha-ketoadipateEt pH profiles are pH independent from pH 6.5 to 9.6, while the V/KL-tyrosine pH-rate profile decreases below a single pKa of 7.0 0.1
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
59
-
Q9WVM8
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
glutamate-alpha-ketoadipate transaminase II
Manually annotated by BRENDA team
-
isoenzyme AadAT-I
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
glutamate-alpha-ketoadipate transaminase I
Manually annotated by BRENDA team
-
isoenzyme AadAT-II
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50800
-
-, Q8N5Z0
cDNA analysis
82100
-
-
gel filtration
85000
-
-
sucrose density gradient centrifugation
89000
-
-
gel filtration
98000
-
-
isoenzyme AadAT-II, sucrose density gradient centrifugation
100000
-
Q64602
gel filtration
100000
-
-
mitochondrial isoform glutamate-alpha-ketoadipate transaminase I, gel filtration
104000
-
-
isoenzyme AadAT-I, sucrose density gradient centrifugation
140000
-
-
cytoplasmic isoform glutamate-alpha-ketoadipate transaminase II, gel filtration
additional information
-
-
sedimentation equilibrium analysis, equilibrium constant 2.4 + 10-5 M
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 49500, SDS-PAGE
dimer
Q64602
2 * 45000, SDS-PAGE; 2 * 47789, amino acid residues
dimer
-
2 * 45500, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 44500, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 43845, calculated, 2 * 44000, SDS-PAGE
dimer
Rattus norvegicus Sprague-Dawley
-
2 * 41000, SDS-PAGE
-
dimer
Rattus norvegicus Wistar
-
2 * 49500, SDS-PAGE
-
homodimer
-
2 * 56168
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 20C
Q72LL6, -
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; 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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
apoenzyme is most stable in this range during purification
9
9.5
-
isoenzyme AadAT-I, sensitive to pH changes, activity is quickly lost at a higher pH, isoenzyme AadAT-II is less sensitive to pH changes
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
70
-
stable against heating at 45C, 50C, 55C, 60C, 65C and 70C for 10 min
50
70
-
both activities are not changed by heating at 50C for 30 min, activities show a parallel decrease with time at 60C and 70C, both are completely lost by incubation at 70C for 20 min
60
70
-
inactivation is initiated at 60C and is near completion at 70C
additional information
-
-
the crystal structures and site-directed mutagenesis reveales that intersubunit-electrostatic interactions contributes to the elevated thermostability of this enzyme
additional information
-
Q9WVM8
midpoint temperature of protein melting 65.9C, calculated half life time value at 65C 27.4 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.1 mM dithiothreitol improves the stability of the enzyme by 50%
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 100% activity is lost when stored for 14 days
-
freezing and thawing do not alter the activity
Q9WVM8
-15C, crude enzyme, little activity is lost over 3 months
-
-80C, stable for more than 1 month
-
4C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 15% activity is lost when stored for 14 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 isoenzymes, AadAT-I and AadAT-II
-
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
Q9WVM8
immobilized metal ion affinity chromatography (Ni2+)
-
ammonium sulfate precipitation and Superdex 200 gel filtration
Q72LL6, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; gene AADAT sequenced
-, Q8N5Z0
tagged protein (consisting of a intein and a chitin binding domain) expressed in Escherichia coli
Q9WVM8
kynurenine/alpha-aminoadipate aminotransferase cDNA cloned and expressed in HEK-293 cells
Q64602
His-tagged protein expressed in Escherichia coli BL21-Codon-Plus(DE3)-RIL
-
expressed in Escherichia coli BL21(DE3) cells
Q72LL6, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R23A
Q72LL6, -
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
Q72LL6, -
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
Q72LL6, -
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
-, Q8N5Z0
L-alpha-aminoadipate is a component of the precursor to penicillin and cephalosporin
medicine
Q64602
L-2-aminoadipate, the substrate for AadAT, is a well known astroglial-specific toxin, knowledge of the cerebral disposition of this compound is instrumental for the elucidation of its mechanism of toxicity and possible relevance in pathology