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 hide
2.6.1.39
-
RECOMMENDED NAME
GeneOntology No.
2-aminoadipate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
show the reaction diagram
A pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation II (L-pipecolate pathway)
-
-
L-lysine degradation V
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-
L-lysine biosynthesis V
-
-
L-lysine degradation XI (mammalian)
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L-lysine biosynthesis IV
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lysine metabolism
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Lysine biosynthesis
-
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Lysine degradation
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Metabolic pathways
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-00-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
-
Q5ACW9
UniProt
Manually annotated by BRENDA team
-
Q5ACW9
UniProt
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoadipate + pyruvate
2-oxoadipate + L-alanine
show the reaction diagram
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
?
show the reaction diagram
-
-
-
?
2-oxoisocaproate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
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
DL-2-aminopimelic acid + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
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
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + 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
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-4-ethylsulfonylbenzoylalanine
-
-
3-methylglutaric acid
adipic acid
alpha-aminoadipate
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competitive inhibition against kynurenine or 3-hydroxykynurenine
azelaic acid
Decanoic acid
Diethylglutaric acid
Dimethylglutaric acid
-
Glutaric acid
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6 mM, 5% inhibition
Kynurenic acid
L-serine-O-sulfate
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-
pimelic acid
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 20
2-Aminoadipate
0.1483
2-oxo-3-methylvalerate
-
pH 7.5, 45C
0.01 - 2.5
2-oxoadipate
0.5
2-oxoadipic acid
0.27 - 3.6
2-oxoglutarate
0.0288 - 0.43
2-oxoisocaproate
0.0133
2-oxoisovalerate
-
pH 7.5, 45C
1.4
glutamate
-
pH 8.0, 37C
0.02 - 11
L-2-aminoadipate
0.46 - 250
L-glutamate
4.6
L-Glutamic acid
0.2 - 0.95
L-leucine
1
L-phenylalanine
-
pH 7.0, temperature not specified in the publication
0.5
L-tyrosine
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pH 7.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
2-oxo-3-methylvalerate
-
pH 7.5, 45C
22.3
2-oxoadipate
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pH 7.5, 45C
17.8
2-oxoisocaproate
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pH 7.5, 45C
2.1
2-oxoisovalerate
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pH 7.5, 45C
0.011 - 18.4
L-2-aminoadipate
0.23 - 16
L-glutamate
0.009 - 5.1
L-leucine
8.3
L-phenylalanine
-
pH 7.0, temperature not specified in the publication
12.3
L-tyrosine
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pH 7.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 22
2-oxoglutarate
4.8 - 34
2-oxoisocaproate
0.0033 - 8.2
L-2-aminoadipate
0.0009 - 37
L-glutamate
0.023 - 5.4
L-leucine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.53
-
-
0.77
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isoenzyme AadAT-I
1.5
-
kynurenine aminotransferase activity
2.65
-
kynurenine aminotransferase activity
6.3
-
alpha-aminoadipate aminotransferase activity
10.68
-
isoenzyme AadAT-II
26.1
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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
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substrate oxaloacetate, pH 7.5, 45C
1102
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substrate 2-oxoisovalerate, pH 7.5, 45C
5079
-
substrate 2-oxoisocaproate, pH 7.5, 45C
6788
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substrate 2-oxoadipate, pH 7.5, 45C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
kynurenine aminotransferase activity
9 - 9.5
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isoenzyme AadAT-II
9.5
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isoenzyme AadAT-I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.6
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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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43845
-
2 * 43845, calculated, 2 * 44000, SDS-PAGE
44000
-
2 * 43845, calculated, 2 * 44000, SDS-PAGE
44500
-
2 * 44500, SDS-PAGE
45500
-
2 * 45500, SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
47789
2 * 47789, amino acid residues
49500
-
2 * 49500, SDS-PAGE
50800
cDNA analysis
56168
-
2 * 56168
69500
Q5ACW9
PAGE
73500
Q5ACW9
gel filtration
82100
-
gel filtration
89000
-
gel filtration
98000
-
isoenzyme AadAT-II, sucrose density gradient centrifugation
100000
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
COMMENTARY hide
LITERATURE
homodimer
-
2 * 56168
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.91 A resolution, and comparison to alpha-aminoadipate aminotransferase LysN from Thermus thermophilus and human kynurenine aminotransferase II. The active site reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
apoenzyme is most stable in this range during purification
636620
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
639983
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 mM dithiothreitol improves the stability of the enzyme by 50%
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, crude enzyme, little activity is lost over 3 months
-
-80C, stable for more than 1 month
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4C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 100% activity is lost when stored for 14 days
-
4C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 15% activity is lost when stored for 14 days
-
freezing and thawing do not alter the activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes, AadAT-I and AadAT-II
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ammonium sulfate precipitation and Superdex 200 gel filtration
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
immobilized metal ion affinity chromatography (Ni2+)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; gene AADAT sequenced
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
Q5ACW9
His-tagged protein expressed in Escherichia coli BL21-Codon-Plus(DE3)-RIL
-
kynurenine/alpha-aminoadipate aminotransferase cDNA cloned and expressed in HEK-293 cells
tagged protein (consisting of a intein and a chitin binding domain) expressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
pharmacology
L-alpha-aminoadipate is a component of the precursor to penicillin and cephalosporin
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