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Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Gallus gallus

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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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Gallus gallus
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The taxonomic range for the selected organisms is: Gallus gallus
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
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-
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AAT
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-
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aminotransferase, aspartate
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-
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aspartate alpha-ketoglutarate transaminase
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-
-
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aspartate aminotransferase
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-
-
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aspartate-2-oxoglutarate transaminase
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-
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aspartate:2-oxoglutarate aminotransferase
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aspartic acid aminotransferase
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-
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aspartic aminotransferase
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-
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aspartyl aminotransferase
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-
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AspAT
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AspT
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-
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AST
-
-
-
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glutamate oxaloacetate transaminase
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-
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glutamate-oxalacetate aminotransferase
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-
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glutamate-oxalate transaminase
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-
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glutamic oxalic transaminase
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-
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glutamic-aspartic aminotransferase
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-
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glutamic-aspartic transaminase
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-
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glutamic-oxalacetic transaminase
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glutamic-oxaloacetic transaminase
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GOT (enzyme)
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L-aspartate transaminase
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L-aspartate-2-ketoglutarate aminotransferase
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L-aspartate-2-oxoglutarate aminotransferase
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L-aspartate-2-oxoglutarate-transaminase
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-
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L-aspartate-alpha-ketoglutarate transaminase
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L-aspartic aminotransferase
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oxaloacetate transferase
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oxaloacetate-aspartate aminotransferase
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transaminase A
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
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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
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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
pyridoxamine 5'-phosphate
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reverse reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.8
2-oxoglutarate
0.09 - 2.9
L-aspartate
additional information
additional information
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kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 187
2-oxoglutarate
4 - 187
L-aspartate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150
-
purified, mitochondrial isozyme
18.8
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purified mitochondrial isozyme from liver
22.6
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purified mitochondrial isozyme from heart
74
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purified cytosolic isozyme from liver
83.5
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purified cytosolic isozyme from heart
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.4 - 7.6
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7.5
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recombinant enzyme, assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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_CHICK
423
0
47241
Swiss-Prot
Mitochondrion (Reliability: 1)
AATC_CHICK
412
0
45935
Swiss-Prot
other Location (Reliability: 5)
F1P180_CHICK
423
0
47251
TrEMBL
Mitochondrion (Reliability: 1)
A0A1L1RPR4_CHICK
427
0
47987
TrEMBL
other Location (Reliability: 5)
F1NTM7_CHICK
412
0
45908
TrEMBL
other Location (Reliability: 5)
Q7LZ21_CHICK
8
0
963
TrEMBL
other Location (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified cytosolic enzyme, variation of crystallization conditions resulting in different crystal types, influence of various divalent metal ions, dioxane and non-ionic detergent beta-octylglucoside, structure analysis
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vapour diffusion method with hanging drops, protein solution: 10 mg/ml, 50 mM sodium phosphate, pH 7.5, 8-24% polyethylene glycol 2000-20000, reservoir solution: 8-24% polyethylene glycol 2000-20000, equal amounts, room temperature, X-ray structure analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C166A
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site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB
C166S
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site-directed mutagenesis of isozyme mAspAT, decreased ability to undergo transition from the open to the closed conformation essential for the reaction mechanism, reduced reactivity with DTNB
additional information
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construction of deletion mutant DELTA3-11mAspAT of isozyme mAspAT, enhanced thermostability, reduced kcat and Km, enhanced reactivity of Cys166 with DTNB
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
15 min, stable
70
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t1/2 wild-type of mature mitochondrial isozyme: 2.7 min
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic isozyme
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mitochondrial isozyme
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recombinant mAspAT, pmAspAT and mutants from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type mAspAT and pmAspAT and mutants in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eichele, G.; Ford, G.C.; Jansonius, J.N.
Crystallization of pig mitochondrial aspartate aminotransferase by seeding with crystals of the chicken mitochondrial isoenzyme
J. Mol. Biol.
135
513-516
1979
Gallus gallus, Sus scrofa
Manually annotated by BRENDA team
Gehring, H.; Christen, P.; Eichele, G.; Glor, M.; Jansonius, J.N.; Reimer, A.S.; Smit, J.D.G.; Thaller, C.
Isolation, crystallization and preliminary crystallographic data of aspartate aminotransferase from chicken heart mitochondria
J. Mol. Biol.
115
97-101
1977
Gallus gallus
Manually annotated by BRENDA team
Malashkevich, V.N.; Sinitzina, N.I.
New crystal form of cytosolic chicken aspartate aminotransferase suitable for high-resolution X-ray analysis
J. Mol. Biol.
221
61-63
1991
Gallus gallus
Manually annotated by BRENDA team
Quiroga, C.; Imperial, S.; Busquets, M.; Cortes, A.
Comparison of some of the properties of the holoenzymes and apoenzymes of the molecular forms of chicken liver cytoplasmic aspartate aminotransferase
Biochem. Soc. Trans.
19
74S
1991
Gallus gallus
Manually annotated by BRENDA team
Shrawder, E.J.; Martinez-Carrion, M.
Simultaneous isolation and characterization of chicken supernatant and mitochondrial isoenzymes of aspartate transaminase
J. Biol. Chem.
248
2140-2146
1973
Gallus gallus
Manually annotated by BRENDA team
Azzariti, A.; Vacca, R.A.; Giannattasio, S.; Merafina, R.S.; Marra, E.; Doonan, S.
Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferase
Biochim. Biophys. Acta
1386
29-38
1998
Gallus gallus
Manually annotated by BRENDA team