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Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Bos taurus

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.1 aspartate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis , some EC 2.6.1.57 activity can be found in this enzyme from other sources ; indeed the enzymes are identical in Trichomonas vaginalis .
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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Synonyms
aspartate transaminase, asat, glutamic oxaloacetic transaminase, glutamate oxaloacetate transaminase, glutamic-oxaloacetic transaminase, asp at, aspat, aspartate at, glutamic-oxalacetic transaminase, aat-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoglutarate-glutamate aminotransferase
-
-
-
-
AAT
-
-
-
-
aminotransferase, aspartate
-
-
-
-
aspartate alpha-ketoglutarate transaminase
-
-
-
-
aspartate aminotransferase
-
-
-
-
aspartate-2-oxoglutarate transaminase
-
-
-
-
aspartate:2-oxoglutarate aminotransferase
-
-
-
-
aspartic acid aminotransferase
-
-
-
-
aspartic aminotransferase
-
-
-
-
aspartyl aminotransferase
-
-
-
-
AspT
-
-
-
-
AST
-
-
-
-
glutamate oxaloacetate transaminase
-
-
-
-
glutamate-oxalacetate aminotransferase
-
-
-
-
glutamate-oxalate transaminase
-
-
-
-
glutamic oxalic transaminase
-
-
-
-
glutamic-aspartic aminotransferase
-
-
-
-
glutamic-aspartic transaminase
-
-
-
-
glutamic-oxalacetic transaminase
-
-
-
-
glutamic-oxaloacetic transaminase
-
-
-
-
GOT (enzyme)
-
-
-
-
L-aspartate transaminase
-
-
-
-
L-aspartate-2-ketoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate-transaminase
-
-
-
-
L-aspartate-alpha-ketoglutarate transaminase
-
-
-
-
L-aspartic aminotransferase
-
-
-
-
oxaloacetate transferase
-
-
-
-
oxaloacetate-aspartate aminotransferase
-
-
-
-
transaminase A
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9000-97-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + 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-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
1-3 mM, at pH 6.0, not at pH 8.0
additional information
-
no inhibition by 4-aminobutyric acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
2-oxoglutarate
-
pH 7.4, 25°C
2
L-aspartate
-
pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
136
-
partially purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AATM_BOVIN
430
0
47514
Swiss-Prot
Mitochondrion (Reliability: 2)
AATC2_BOVIN
407
0
45918
Swiss-Prot
other Location (Reliability: 2)
AATC_BOVIN
413
0
46399
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
-
gel filtration
46500
-
2 * 46500, SDS-PAGE
90000
-
analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 46500, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, 10 mM NaOH-glycine, pH 9.1, polyethylene glycol 4000 18% w/v, 1 week, X-ray analysis
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
380fold
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krista, M.L.; Fonda, M.L.
Beef brain cytoplasmic aspartate aminotransferase. Purification, kinetics, and physical properties
Biochim. Biophys. Acta
309
83-96
1973
Bos taurus
Manually annotated by BRENDA team
Capasso, S.; Garzillo, A.M.; Marino, G.; Mazzarella, L.; Pucci, P.; Sannia, G.
Mitochondrial bovine aspartate aminotransferase. Preliminary sequence and crystallographic data
FEBS Lett.
101
351-354
1979
Bos taurus
Manually annotated by BRENDA team