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Information on EC 2.6.1.39 - 2-aminoadipate transaminase and Organism(s) Rattus norvegicus and UniProt Accession Q64602
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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: Rattus norvegicus
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
-
-
-
-
2-aminoadipic aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase
-
-
-
-
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9033-00-5
-
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
3,5-di-iodotyrosine + 2-oxoglutarate
3,5-diiodophenylpyruvate + L-glutamate
-
-
-
-
r
DL-2-aminopimelic acid + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
-
-
-
r
L-histidine + 2-oxoglutarate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
-
-
-
r
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
-
-
-
-
r
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
-
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
lysine catabolic pathway
-
-
r
additional information
?
-
2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
KAT and AadAT activities are associated with 2 different proteins
-
-
?
NATURAL SUBSTRATE
NATURAL 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
lysine catabolic pathway
-
-
r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
-
lysine catabolic pathway
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-aminoadipate
-
competitive inhibition against kynurenine or 3-hydroxykynurenine
adipic acid
-
competitive inhibition with respect to L-kynurenine, but not to 2-oxoglutarate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AADAT_RAT
425
0
47784
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 70
-
both activities are not changed by heating at 50°C for 30 min, activities show a parallel decrease with time at 60°C and 70°C, both are completely lost by incubation at 70°C for 20 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 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
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
kynurenine/alpha-aminoadipate aminotransferase cDNA cloned and expressed in HEK-293 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hartline, R.A.
Kynurenine aminotransferase from kidney supernatant
Methods Enzymol.
113
664-672
1985
Rattus norvegicus
Mawal, M.R.; Mukhopadhyay, A.; Deshmukh, D.R.
Purification and properties of kynurenine aminotransferase from rat kidney
Biochem. J.
279
595-599
1991
Rattus norvegicus
-
Mawal, M.R.; Deshmukh, D.R.
alpha-Aminoadipate and kynurenine aminotransferase activities from rat kidney. Evidence for separate identity
J. Biol. Chem.
266
2573-2575
1991
Rattus norvegicus
Takeuchi, F.; Otsuka, H.; Shibata, Y.
Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase
Biochim. Biophys. Acta
743
323-330
1983
Rattus norvegicus, Rattus norvegicus Wistar
Buchli, R.; Alberati-Giani, D.; Malherbe, P.; Kohler, C.; Broger, C.; Cesura, A.M.
Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney
J. Biol. Chem.
270
29330-29335
1995
Rattus norvegicus (Q64602)
Tobes, M.C.; Mason, M.
L-kynurenine aminotransferase and L-alpha-aminoadipate aminotransferase. I. Evidence for identity
Biochem. Biophys. Res. Commun.
62
390-397
1975
Rattus norvegicus
Tobes, M.C.; Mason, M.
alpha-Aminoadipate aminotransferase and kynurenine aminotransferase. Purification, characterization, and further evidence for identity
J. Biol. Chem.
252
4591-4599
1977
Rattus norvegicus
Deshmukh, D.R.; Mungre, S.M.
Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidney
Biochem. J.
261
761-768
1989
Bos taurus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Mawal, M.R.; Deshmukh, D.R.
Purification and properties of alpha-aminoadipate aminotransferase from rat kidney
Prep. Biochem.
21
63-73
1991
Rattus norvegicus
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