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Information on EC 2.6.1.39 - 2-aminoadipate transaminase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53090

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.39 2-aminoadipate transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P53090
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-aminoadipate aminotransferase
-
-
-
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2-aminoadipic aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase (gene aro8)
-
-
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
-
-
-
r
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-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
2-oxoadipate
-
pH 7.0, temperature not specified in the publication
3.6
2-oxoglutarate
-
pH 7.0, temperature not specified in the publication
8.8
L-2-aminoadipate
-
pH 7.0, temperature not specified in the publication
26
L-glutamate
-
pH 7.0, temperature not specified in the publication
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
18.4
L-2-aminoadipate
-
pH 7.0, temperature not specified in the publication
12.8
L-glutamate
-
pH 7.0, temperature not specified in the publication
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
glutamate-alpha-ketoadipate transaminase II
Manually annotated by BRENDA team
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glutamate-alpha-ketoadipate transaminase I
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
mitochondrial isoform glutamate-alpha-ketoadipate transaminase I, gel filtration
140000
-
cytoplasmic isoform glutamate-alpha-ketoadipate transaminase II, gel filtration
56168
-
2 * 56168
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 56168
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli BL21-Codon-Plus(DE3)-RIL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuda, M.; Ogur, M.
Separation and specificity of the yeast glutamate-alpha-ketoadipate transaminase
J. Biol. Chem.
244
3352-3358
1969
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Karsten, W.E.; Reyes, Z.L.; Bobyk, K.D.; Cook, P.F.; Chooback, L.
Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
516
67-74
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bulfer, S.L.; Brunzelle, J.S.; Trievel, R.C.
Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase
Protein Sci.
22
1417-1424
2013
Saccharomyces cerevisiae (P53090), Saccharomyces cerevisiae
Manually annotated by BRENDA team