Information on EC 2.6.1.39 - 2-aminoadipate transaminase:
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EC NUMBERCOMMENTARY
2.6.1.39-

RECOMMENDED NAMEGeneOntology No.
2-aminoadipate transaminaseGO:0047536

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
show the reaction diagram		A pyridoxal-phosphate protein---

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
amino group transfer----

PATHWAYKEGG LinkMetaCyc Link
lysine biosynthesis IV-LYSINE-AMINOAD-PWY
lysine biosynthesis V-PWY-3081
lysine degradation II-LYSINE-DEG1-PWY
lysine degradation V-PWY-5283

SYSTEMATIC NAMEIUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferaseA pyridoxal-phosphate protein.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
2-aminoadipate aminotransferase----
2-aminoadipic aminotransferase----
AAA-ATThermus thermophilus--689965, 702069
AadATRattus norvegicus--636621, 636622, 636625, 639979, 639981
AadATBos taurus--639979
AadATHomo sapiens--639983, 639985, 702779
AATRattus norvegicus--639975
alpha-aminoadipate aminotransferase----
alpha-aminoadipate aminotransferaseThermus thermophilus--689965, 702069
aminoadipate aminotransferaseHomo sapiensQ8N5Z0-702779
aminoadipate aminotransferase/kynurenine aminotransferase IIHomo sapiensQ8N5Z0-702779
GKATSaccharomyces cerevisiae--639974
glutamate-alpha-ketoadipate transaminase----
glutamic-ketoadipic transaminase----
halogenated tyrosine aminotransferaseRattus norvegicus--639978
KAT II/AADATHomo sapiensQ8N5Z0bifunctional enzyme with kynurenine aminotransferase activity and aminoadipate aminotransferase function702779
kynurenine aminotransferase IIHomo sapiensQ8N5Z0-702779
kynurenine/alpha-aminoadipate aminotransferaseRattus norvegicusQ64602-636625
additional informationHomo sapiensQ8N5Z0KAT II is identical to AADAT (aminoadipate aminotransferase)702779

CAS REGISTRY NUMBERCOMMENTARY
9033-00-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bos taurusbovine639979--Manually annotated by BRENDA team
Homo sapiens-702779Q8N5Z0SwissProtManually annotated by BRENDA team
Homo sapienshuman639983, 639985--Manually annotated by BRENDA team
Homo sapienshuman639985Q8N5Z0SwissProtManually annotated by BRENDA team
Rattus norvegicus-636621, 636622, 639975, 639978, 639981--Manually annotated by BRENDA team
Rattus norvegicus-636625Q64602SwissProtManually annotated by BRENDA team
Rattus norvegicusalbino rat639976--Manually annotated by BRENDA team
Rattus norvegicusSprague-Dawley639979--Manually annotated by BRENDA team
Rattus norvegicusWistar636623--Manually annotated by BRENDA team
Saccharomyces cerevisiaebakers' yeast, haploid strains MO-11-48A and X1049-2B, diploid strain F2, clonal isolate of commercial bakers' yeast639974--Manually annotated by BRENDA team
Thermus thermophilus-659885, 689965--Manually annotated by BRENDA team
Thermus thermophilus-702069Q72LL6SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoadipate + pyruvate2-oxoadipate + L-alanine
show the reaction diagram		Thermus thermophilus--689965--?
2-aminoadipate + pyruvate2-oxoadipate + L-alanine
show the reaction diagram		Rattus norvegicus, Bos taurus--639979--r
2-oxo-3-methylvalerate + L-glutamate2-amino-3-methylpentanoate + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885--?
2-oxoadipate + L-glutamateL-2-aminoadipate + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885, 689965--?
2-oxoisocaproate + L-glutamateL-leucine + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885--?
2-oxoisocaproate + L-glutamate?
show the reaction diagram		Thermus thermophilusQ72LL6-702069--?
2-oxoisovalerate + L-glutamateL-valine + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885--?
3,5-di-iodotyrosine + 2-oxoglutarate3,5-diiodophenylpyruvate + L-glutamate
show the reaction diagram		Rattus norvegicus--639978, 639979--r
3,5-di-iodotyrosine + 2-oxoglutarate3,5-diiodophenylpyruvate + L-glutamate
show the reaction diagram		Bos taurus--639979--r
DL-2-aminopimelic acid + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus--639978, 639979--r
DL-2-aminopimelic acid + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Bos taurus--639979--r
kynurenine + 2-oxoglutaratekynurenic acid + L-glutamate
show the reaction diagram		Homo sapiens--639983--ir
kynurenine + 2-oxoglutaratekynurenic acid + L-glutamate
show the reaction diagram		Rattus norvegicusQ64602-636625--ir
kynurenine + 2-oxoglutaratekynurenic acid + L-glutamate
show the reaction diagram		Rattus norvegicus--639979--ir
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiensQ8N5Z0-702779--?
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiens--639983-639983r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiensQ8N5Z0-639985-639985r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus--636621--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicusQ64602-636625--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus--639975, 639976, 639978--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus--639979-639979r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Saccharomyces cerevisiae--639974-639974r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Bos taurus--639979-639979r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Thermus thermophilusQ72LL6-702069--?
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiensQ8N5Z0lysine catabolic pathway639985--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus-lysine catabolic pathway636621--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicusQ64602lysine catabolic pathway636625--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus-lysine catabolic pathway639975, 639976, 639979--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Bos taurus-lysine catabolic pathway639979--r
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiens-lysine and tryptophan metabolism639983--r
L-histidine + 2-oxoglutarate3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
show the reaction diagram		Rattus norvegicus, Bos taurus--639979--r
L-histidine + pyruvate3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram		Rattus norvegicus, Bos taurus--639979--r
L-leucine + 2-oxoglutarate4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram		Thermus thermophilus--689965--?
L-leucine + 2-oxoglutarate4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram		Thermus thermophilusQ72LL6-702069--?
L-norleucine + 2-oxoglutarate2-oxohexanoate + L-glutamate
show the reaction diagram		Rattus norvegicus--639978, 639979--r
L-norleucine + 2-oxoglutarate2-oxohexanoate + L-glutamate
show the reaction diagram		Bos taurus--639979--r
oxaloacetate + L-glutamate2-aminosuccinate + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885--?
phenylpyruvate + 2-aminoadipateL-phenylalanine + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885, 689965--?
pyruvate + L-glutamateL-alanine + 2-oxoglutarate
show the reaction diagram		Thermus thermophilus--659885--?
L-tryptophan + 2-oxoglutarate3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram		Homo sapiens--639983--?
additional information?-Homo sapiens-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-oxoglutarate639983---
additional information?-Rattus norvegicus, Bos taurus-only slight activity with phenylalanine, tryptophan, tyrosine, aspartate or alanine as amino group donors, glyoxylate is no amino group acceptor639979---
additional information?-Rattus norvegicus-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-glutamate639978---
additional information?-Bos taurus-no kynurenine aminotransferase activity639979---
additional information?-Rattus norvegicus-2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein636623---
additional information?-Rattus norvegicusQ646022-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein636625---
additional information?-Rattus norvegicus-2-aminoadipate aminotransferase and kynurenine aminotransferase, EC 2.6.1.7, activities are properties of a single protein639975, 639976, 639978, 639979---
additional information?-Rattus norvegicus-KAT and AadAT activities are associated with 2 different proteins636621, 636622---
additional information?-Thermus thermophilus-AAA-AT can recognize various kinds of substrates using the mobile alpha2 helix689965---
additional information?-Thermus thermophilusQ72LL6negligible activity is observed for L-Asp702069---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus--639978--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Saccharomyces cerevisiae--639974-639974
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiensQ8N5Z0lysine catabolic pathway639985--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus-lysine catabolic pathway636621--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicusQ64602lysine catabolic pathway636625--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Rattus norvegicus-lysine catabolic pathway639975, 639976, 639979--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Bos taurus-lysine catabolic pathway639979--
L-2-aminoadipate + 2-oxoglutarate2-oxoadipate + L-glutamate
show the reaction diagram		Homo sapiens-lysine and tryptophan metabolism639983--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateSaccharomyces cerevisiae--639974 2D-image
pyridoxal 5'-phosphateRattus norvegicus--639976, 639979 2D-image
pyridoxal 5'-phosphateBos taurus--639979 2D-image
pyridoxal 5'-phosphateHomo sapiensQ8N5Z0-639985 2D-image
pyridoxal 5'-phosphateThermus thermophilusQ72LL6-702069 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3-methylglutaric acidBos taurus-6 mM, 2% inhibition639979 2D-image
3-methylglutaric acidRattus norvegicus-6 mM, 38% inhibition639979 2D-image
Adipic acidRattus norvegicus-competitive inhibition with respect to L-kynurenine, but not to 2-oxoglutarate639975 2D-image
Adipic acidBos taurus-6 mM, 48% inhibition639979 2D-image
Adipic acidRattus norvegicus-6 mM, 60% inhibition639979 2D-image
alpha-aminoadipateRattus norvegicus-competitive inhibition against kynurenine or 3-hydroxykynurenine636623 2D-image
azelaic acidBos taurus-6 mM, 36% inhibition639979 2D-image
azelaic acidRattus norvegicus-6 mM, 38% inhibition639979 2D-image
Decanoic acidBos taurus-6 mM, 50% inhibition639979 2D-image
Decanoic acidRattus norvegicus-6 mM, 45% inhibition639979 2D-image
Diethylglutaric acidBos taurus, Rattus norvegicus-6 mM, 20% inhibition639979 2D-image
Dimethylglutaric acidBos taurus-6 mM, 15% inhibition639979-
Dimethylglutaric acidRattus norvegicus-6 mM, 42% inhibition639979-
Glutaric acidRattus norvegicus-6 mM, 5% inhibition639979 2D-image
Kynurenic acidBos taurus-1 mM, 30% inhibition639979 2D-image
Kynurenic acidRattus norvegicus-1 mM, 40% inhibition639979 2D-image
pimelic acidBos taurus-6 mM, 28% inhibition639979 2D-image
pimelic acidRattus norvegicus-6 mM, 32% inhibition639979 2D-image
L-serine-O-sulfateRattus norvegicus--639976 2D-image
additional informationBos taurus, Rattus norvegicus-oxaloacetic acid is no inhibitor639979-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.25-2-AminoadipateHomo sapiens-pH 8.0, 37°C isoenzyme AadAT-II639983 2D-image
20-2-AminoadipateHomo sapiens-pH 8.0, 37°C639983 2D-image
0.1483-2-oxo-3-methylvalerateThermus thermophilus-pH 7.5, 45°C659885 2D-image
0.01-2-oxoadipateRattus norvegicus-pH 6.5, 37°C636623 2D-image
0.024-2-oxoadipateThermus thermophilus-pH 7.5, 45°C659885 2D-image
1-2-oxoadipateHomo sapiens-pH 8.0, 37°C isoenzyme AadAT-II639983 2D-image
2.5-2-oxoadipateHomo sapiens-pH 8.0, 37°C isoenzyme AadAT-I639983 2D-image
0.5-2-oxoadipic acidBos taurus, Rattus norvegicus-pH 7.0, 37°C639979 2D-image
0.27-2-oxoglutarateThermus thermophilusQ72LL6wild 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°C702069 2D-image
0.3-2-oxoglutarateThermus thermophilusQ72LL6wild 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°C702069 2D-image
0.4-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
0.41-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
0.42-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
0.54-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
0.55-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
0.61-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
1.1-2-oxoglutarateHomo sapiens-pH 8.0, 37°C isoenzyme AadAT-I639983 2D-image
3.2-2-oxoglutarateHomo sapiens-pH 8.0, 37°C isoenzyme AadAT-II639983 2D-image
0.0288-2-oxoisocaproateThermus thermophilus-pH 7.5, 45°C659885 2D-image
0.048-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.05-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.091-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.43-2-oxoisocaproateThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.0133-2-oxoisovalerateThermus thermophilus-pH 7.5, 45°C659885 2D-image
1.4-glutamateHomo sapiens-pH 8.0, 37°C639983 2D-image
0.81-L-2-AminoadipateThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
3.3-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
7-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
11-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.46-L-glutamateThermus thermophilusQ72LL6wild 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°C702069 2D-image
12.5-L-glutamateHomo sapiens-pH 8.0, 37°C, isoenzyme AadAT-II639983 2D-image
62-L-glutamateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
82-L-glutamateThermus thermophilusQ72LL6mutant enzyme S20E, 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°C702069 2D-image
250-L-glutamateThermus thermophilusQ72LL6mutant enzyme R23A, 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°C702069 2D-image
4.6-L-Glutamic acidBos taurus, Rattus norvegicus-pH 7.0, 37°C639979 2D-image
0.2-L-leucineThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.39-L-leucineThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.88-L-leucineThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.95-L-leucineThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3.5-2-oxo-3-methylvalerateThermus thermophilus-pH 7.5, 45°C659885 2D-image
22.3-2-oxoadipateThermus thermophilus-pH 7.5, 45°C659885 2D-image
17.8-2-oxoisocaproateThermus thermophilus-pH 7.5, 45°C659885 2D-image
2.1-2-oxoisovalerateThermus thermophilus-pH 7.5, 45°C659885 2D-image
0.011-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.04-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.083-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
6.7-L-2-AminoadipateThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.23-L-glutamateThermus thermophilusQ72LL6mutant enzyme R23A, 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°C702069 2D-image
0.5-L-glutamateThermus thermophilusQ72LL6mutant 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°C702069 2D-image
1.2-L-glutamateThermus thermophilusQ72LL6mutant enzyme S20E, 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°C702069 2D-image
16-L-glutamateThermus thermophilusQ72LL6wild 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°C702069 2D-image
0.009-L-leucineThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.023-L-leucineThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
0.05-L-leucineThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image
5.1-L-leucineThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C702069 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.015-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
0.021-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
0.06-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
0.091-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
0.097-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
0.2-2-oxoglutarateThermus thermophilusQ72LL6mutant 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°C7020692883
19-2-oxoglutarateThermus thermophilusQ72LL6wild 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°C7020692883
22-2-oxoglutarateThermus thermophilusQ72LL6wild 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°C7020692883
4.8-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C7020692896
5.5-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C7020692896
24-2-oxoisocaproateThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C7020692896
34-2-oxoisocaproateThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C7020692896
0.0033-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206911982
0.0057-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206911982
0.0075-L-2-AminoadipateThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206911982
8.2-L-2-AminoadipateThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206911982
0.0009-L-glutamateThermus thermophilusQ72LL6mutant enzyme R23A, 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°C70206912211
0.0081-L-glutamateThermus thermophilusQ72LL6mutant 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°C70206912211
0.014-L-glutamateThermus thermophilusQ72LL6mutant enzyme S20E, 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°C70206912211
37-L-glutamateThermus thermophilusQ72LL6wild 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°C70206912211
0.023-L-leucineThermus thermophilusQ72LL6mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206912291
0.057-L-leucineThermus thermophilusQ72LL6mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206912291
0.12-L-leucineThermus thermophilusQ72LL6mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206912291
5.4-L-leucineThermus thermophilusQ72LL6wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C70206912291

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.53-Bos taurus--639979
0.77-Homo sapiens-isoenzyme AadAT-I639983
1.5-Rattus norvegicus-kynurenine aminotransferase activity636623
1.56-Rattus norvegicusQ64602-636625
2.65-Rattus norvegicus-kynurenine aminotransferase activity639976, 639978
6.3-Rattus norvegicus-alpha-aminoadipate aminotransferase activity636623
10.68-Homo sapiens-isoenzyme AadAT-II639983
26.1-Rattus norvegicus-alpha-aminoadipate aminotransferase activity639976, 639978
513-Thermus thermophilus-substrate phenylpyruvate, pH 7.5, 45°C659885
561-Thermus thermophilus-substrate 2-oxo-3-methylvalerate, pH 7.5, 45°C659885
568-Thermus thermophilus-substrate pyruvate, pH 7.5, 45°C659885
661-Thermus thermophilus-substrate oxaloacetate, pH 7.5, 45°C659885
1102-Thermus thermophilus-substrate 2-oxoisovalerate, pH 7.5, 45°C659885
5079-Thermus thermophilus-substrate 2-oxoisocaproate, pH 7.5, 45°C659885
6788-Thermus thermophilus-substrate 2-oxoadipate, pH 7.5, 45°C659885

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.5-Rattus norvegicus-kynurenine aminotransferase activity636623
7-Bos taurus, Rattus norvegicus--639979
8.5-Saccharomyces cerevisiae--639974
99.5Homo sapiens-isoenzyme AadAT-II639983
9.5-Homo sapiens-isoenzyme AadAT-I639983

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
heartHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
kidneyRattus norvegicus--636621, 636622, 636625, 639975, 639976, 639978, 639979, 639981Manually annotated by BRENDA team
kidneyBos taurus--639979Manually annotated by BRENDA team
kidneyHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
liverRattus norvegicus--636622, 636623, 639975, 639979Manually annotated by BRENDA team
liverHomo sapiens--639983, 639985Manually annotated by BRENDA team
ovaryHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
pancreasHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
prostateHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team
testisHomo sapiensQ8N5Z0-639985Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytoplasmSaccharomyces cerevisiae-glutamate-alpha-ketoadipate transaminase II5737639974Manually annotated by BRENDA team
cytoplasmBos taurus, Rattus norvegicus--5737639979Manually annotated by BRENDA team
cytoplasmHomo sapiens-isoenzyme AadAT-I5737639983Manually annotated by BRENDA team
cytoplasmHomo sapiensQ8N5Z0-5737702779Manually annotated by BRENDA team
cytosolHomo sapiens--5829639983Manually annotated by BRENDA team
mitochondrionRattus norvegicus--5739636622, 636623, 639978, 639979Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae-glutamate-alpha-ketoadipate transaminase I5739639974Manually annotated by BRENDA team
mitochondrionBos taurus--5739639979Manually annotated by BRENDA team
mitochondrionHomo sapiens-isoenzyme AadAT-II5739639983Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2qlr, downloadSCOP (2qlr)CATH (2qlr)Homo sapiens
2r2n, downloadSCOP (2r2n)CATH (2r2n)Homo sapiens
2vgz, downloadSCOP (2vgz)CATH (2vgz)Homo sapiens
2xh1, downloadSCOP (2xh1)CATH (2xh1)Homo sapiens
3dc1, downloadSCOP (3dc1)CATH (3dc1)Homo sapiens
3ue8, downloadSCOP (3ue8)CATH (3ue8)Homo sapiens
4gdy, downloadSCOP (4gdy)CATH (4gdy)Homo sapiens
4ge4, downloadSCOP (4ge4)CATH (4ge4)Homo sapiens
4ge7, downloadSCOP (4ge7)CATH (4ge7)Homo sapiens
4ge9, downloadSCOP (4ge9)CATH (4ge9)Homo sapiens
2egy, downloadSCOP (2egy)CATH (2egy)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
2z1y, downloadSCOP (2z1y)CATH (2z1y)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
2zp7, downloadSCOP (2zp7)CATH (2zp7)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
2zyj, downloadSCOP (2zyj)CATH (2zyj)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
3cbf, downloadSCOP (3cbf)CATH (3cbf)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
50800-Homo sapiensQ8N5Z0cDNA analysis639985
82100-Rattus norvegicus-gel filtration639976
85000-Rattus norvegicus-sucrose density gradient centrifugation639976
85000-Rattus norvegicus--639978
89000-Rattus norvegicus-gel filtration639981
98000-Homo sapiens-isoenzyme AadAT-II, sucrose density gradient centrifugation639983
100000-Rattus norvegicusQ64602gel filtration636625
100000-Saccharomyces cerevisiae-mitochondrial isoform glutamate-alpha-ketoadipate transaminase I, gel filtration639974
104000-Homo sapiens-isoenzyme AadAT-I, sucrose density gradient centrifugation639983
140000-Saccharomyces cerevisiae-cytoplasmic isoform glutamate-alpha-ketoadipate transaminase II, gel filtration639974
additional information-Thermus thermophilus-sedimentation equilibrium analysis, equilibrium constant 2.4 + 10-5 M659885

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerRattus norvegicus-2 * 49500, SDS-PAGE636623
dimerRattus norvegicusQ646022 * 45000, SDS-PAGE; 2 * 47789, amino acid residues636625
dimerRattus norvegicus-2 * 45500, SDS-PAGE639976
dimerRattus norvegicus-2 * 45000, SDS-PAGE639978
dimerBos taurus, Rattus norvegicus-2 * 41000, SDS-PAGE639979
dimerRattus norvegicus-2 * 44500, SDS-PAGE639981
dimerHomo sapiens-2 * 46000, SDS-PAGE639983
dimerThermus thermophilus-2 * 43845, calculated, 2 * 44000, SDS-PAGE659885

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

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 20°CThermus thermophilusQ72LL6702069
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 recognitionThermus thermophilus-689965

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
6.57.5Rattus norvegicus-apoenzyme is most stable in this range during purification639978
99.5Homo sapiens-isoenzyme AadAT-I, sensitive to pH changes, activity is quickly lost at a higher pH, isoenzyme AadAT-II is less sensitive to pH changes639983

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4570Saccharomyces cerevisiae-stable against heating at 45°C, 50°C, 55°C, 60°C, 65°C and 70°C for 10 min639974
5070Rattus norvegicus-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 min636623
6070Rattus norvegicus-inactivation is initiated at 60°C and is near completion at 70°C639976
additional information-Thermus thermophilus-the crystal structures and site-directed mutagenesis reveales that intersubunit-electrostatic interactions contributes to the elevated thermostability of this enzyme689965

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
0.1 mM dithiothreitol improves the stability of the enzyme by 50%Bos taurus-639979

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 100% activity is lost when stored for 14 daysBos taurus-639979
-15°C, crude enzyme, little activity is lost over 3 monthsRattus norvegicus-639975
-80°C, stable for more than 1 monthRattus norvegicus-636623
4°C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 15% activity is lost when stored for 14 daysRattus norvegicus-639979

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bos taurus-639979
2 isoenzymes, AadAT-I and AadAT-IIHomo sapiens-639983
-Rattus norvegicus-636621, 636622, 636623, 636625, 639975, 639976, 639978, 639979, 639981
partialSaccharomyces cerevisiae-639974
ammonium sulfate precipitation and Superdex 200 gel filtrationThermus thermophilusQ72LL6702069

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
; gene AADAT sequencedHomo sapiensQ8N5Z0639985
kynurenine/alpha-aminoadipate aminotransferase cDNA cloned and expressed in HEK-293 cellsRattus norvegicusQ64602636625
-Thermus thermophilus-659885
expressed in Escherichia coli BL21(DE3) cellsThermus thermophilusQ72LL6702069

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
R23AThermus thermophilusQ72LL6the 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 affected702069
R23QThermus thermophilusQ72LL6the 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 affected702069
S20EThermus thermophilusQ72LL6the mutant shows decreased kcat values compared to the wild type enzyme702069
additional informationThermus thermophilus-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 rate659885

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
pharmacologyHomo sapiensQ8N5Z0L-alpha-aminoadipate is a component of the precursor to penicillin and cephalosporin639985
medicineRattus norvegicusQ64602L-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 pathology636625

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
636621Mawal, M.R.; Mukhopadhyay, A.; Deshmukh, D.R.Purification and properties of kynurenine aminotransferase from rat kidneyBiochem. J.279595-5991991Rattus norvegicus-
636622Mawal, M.R.; Deshmukh, D.R.alpha-Aminoadipate and kynurenine aminotransferase activities from rat kidney. Evidence for separate identityJ. Biol. Chem.2662573-25751991Rattus norvegicus PubMed
636623Takeuchi, F.; Otsuka, H.; Shibata, Y.Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferaseBiochim. Biophys. Acta743323-3301983Rattus norvegicus PubMed
636625Buchli, 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 kidneyJ. Biol. Chem.27029330-293351995Rattus norvegicus PubMed
639974Matsuda, M.; Ogur, M.Separation and specificity of the yeast glutamate-alpha-ketoadipate transaminaseJ. Biol. Chem.2443352-33581969Saccharomyces cerevisiae PubMed
639975Tobes, M.C.; Mason, M.L-kynurenine aminotransferase and L-alpha-aminoadipate aminotransferase. I. Evidence for identityBiochem. Biophys. Res. Commun.62390-3971975Rattus norvegicus PubMed
639976Tobes, M.C.; Mason, M.alpha-Aminoadipate aminotransferase and kynurenine aminotransferase. Purification, characterization, and further evidence for identityJ. Biol. Chem.2524591-45991977Rattus norvegicus PubMed
639978Hartline, R.A.Kynurenine aminotransferase from kidney supernatantMethods Enzymol.113664-6721985Rattus norvegicus PubMed
639979Deshmukh, D.R.; Mungre, S.M.Purification and properties of 2-aminoadipate: 2-oxoglutarate aminotransferase from bovine kidneyBiochem. J.261761-7681989Bos taurus, Rattus norvegicus PubMed
639981Mawal, M.R.; Deshmukh, D.R.Purification and properties of alpha-aminoadipate aminotransferase from rat kidneyPrep. Biochem.2163-731991Rattus norvegicus PubMed
639983Okuno, E.; Tsujimoto, M.; Nakamura, M.; Kido, R.2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human liver: a plausible physiological role in lysine and tryptophan metabolismEnzyme Protein47136-1481993Homo sapiens PubMed
639985Goh, D.L.; Patel, A.; Thomas, G.H.; Salomons, G.S.; Schor, D.S.; Jakobs, C.; Geraghty, M.T.Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)Mol. Genet. Metab.76172-1802002Homo sapiens PubMed
659885Miyazaki, T.; Miyazaki, J.; Yamane, H.; Nishiyama, M.alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilusMicrobiology1502327-23342004Thermus thermophilus PubMed
689965Tomita, T.; Miyagawa, T.; Miyazaki, T.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilusProteins75348-3592008Thermus thermophilus PubMed
702069Ouchi, 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 thermophilusBiochem. Biophys. Res. Commun.38821-272009Thermus thermophilus PubMed
702779Han, Q.; Cai, T.; Tagle, D.A.; Robinson, H.; Li, J.Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase IIBiosci. Rep.28205-2152008Homo sapiens PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.39)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)