Information on EC 2.6.1.39 - 2-aminoadipate transaminase

Word Map on EC 2.6.1.39
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
Biosynthesis of antibiotics
-
-
L-lysine biosynthesis IV
-
-
L-lysine biosynthesis V
-
-
L-lysine degradation II (L-pipecolate pathway)
-
-
L-lysine degradation V
-
-
L-lysine degradation XI (mammalian)
-
-
Lysine biosynthesis
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
lysine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-00-5
-
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
-
competitive inhibition against kynurenine or 3-hydroxykynurenine
azelaic acid
Decanoic acid
Diethylglutaric acid
Dimethylglutaric acid
-
Glutaric acid
-
6 mM, 5% inhibition
Kynurenic acid
L-serine-O-sulfate
-
-
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, 45°C
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, 45°C
1.4
glutamate
-
pH 8.0, 37°C
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
-
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
Thermus thermophilus
-
pH 7.5, 45°C
22.3
2-oxoadipate
Thermus thermophilus
-
pH 7.5, 45°C
17.8
2-oxoisocaproate
Thermus thermophilus
-
pH 7.5, 45°C
2.1
2-oxoisovalerate
Thermus thermophilus
-
pH 7.5, 45°C
0.011 - 18.4
L-2-aminoadipate
0.23 - 16
L-glutamate
0.009 - 5.1
L-leucine
8.3
L-phenylalanine
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
12.3
L-tyrosine
Saccharomyces cerevisiae
-
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
34
4.8 - 34
2-oxoisocaproate
1174
0.0033 - 8.2
L-2-aminoadipate
1790
0.0009 - 37
L-glutamate
41
0.023 - 5.4
L-leucine
127
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.53
-
-
0.77
-
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
-
alpha-aminoadipate aminotransferase activity
513
-
substrate phenylpyruvate, pH 7.5, 45°C
561
-
substrate 2-oxo-3-methylvalerate, pH 7.5, 45°C
568
-
substrate pyruvate, pH 7.5, 45°C
661
-
substrate oxaloacetate, pH 7.5, 45°C
1102
-
substrate 2-oxoisovalerate, pH 7.5, 45°C
5079
-
substrate 2-oxoisocaproate, pH 7.5, 45°C
6788
-
substrate 2-oxoadipate, pH 7.5, 45°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
kynurenine aminotransferase activity
9 - 9.5
-
isoenzyme AadAT-II
9.5
-
isoenzyme AadAT-I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
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 20°C
crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively; 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
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 45°C, 50°C, 55°C, 60°C, 65°C and 70°C for 10 min
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
60 - 70
-
inactivation is initiated at 60°C and is near completion at 70°C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 mM dithiothreitol improves the stability of the enzyme by 50%
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, crude enzyme, little activity is lost over 3 months
-
-80°C, stable for more than 1 month
-
4°C, partially purified enzyme in 8 mM potassium phosphate buffer, pH 7.1, 100% activity is lost when stored for 14 days
-
4°C, 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
-
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
Show AA Sequence (827 entries)
Please use the Sequence Search for a specific query.