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Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Rattus norvegicus and UniProt Accession P00507
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2.6.1.1 aspartate transaminaseIUBMB 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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Word Map
- 2.6.1.1
-
alt
- bilirubin
- cholesterol
- creatinine
- necrosis
- albumin
- triglyceride
- dismutase
-
hepatotoxicity
- malondialdehyde
- catalase
-
hepatoprotective
- hepatocytes
- wistar
- sod
- fibrosis
- hemoglobin
- platelet
-
glutamic-pyruvic
- myocardial
- lipoprotein
-
postoperative
- bile
-
hematological
- transpeptidase
-
tetrachloride
- ccl4
- infarct
- cirrhosis
- gg
-
gamma-glutamyl
-
uric
-
admission
- transaminases
-
phosphokinase
-
albino
-
jaundice
-
ccl4-induced
- nafld
-
c-reactive
- prothrombin
-
glutamyl
- globulin
- gamma-glutamyltransferase
-
corpuscular
-
tetrachloride-induced
- silymarin
-
hematocrit
- synthesis
-
kinase-mb
- medicine
- biotechnology
-
elastography
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
AAT
-
-
-
-
aspartate aminotransferase
-
-
-
-
aspartate aminotransferase
-
-
AST
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Alanine, aspartate and glutamate metabolism, Arginine and proline metabolism, Arginine biosynthesis, Biosynthesis of secondary metabolites, Carbon fixation in photosynthetic organisms, Cysteine and methionine metabolism, Isoquinoline alkaloid biosynthesis, Microbial metabolism in diverse environments, Novobiocin biosynthesis, Phenylalanine metabolism, Phenylalanine, tyrosine and tryptophan biosynthesis, Tropane, piperidine and pyridine alkaloid biosynthesis, Tyrosine metabolism
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9000-97-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
2-aminohexanedioic acid + 2-oxoglutarate
2-oxohexanedioic acid + L-glutamate
-
i.e. alpha-aminoadipic acid
-
-
?
L-cysteic acid + 2-oxoglutarate
2-oxo-3-sulfopropionate + L-glutamate
-
i.e. 2-amino-2-sulfopropionate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
best amino acid donor for mitochondrial enzyme
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
best amino acid donor of cytosolic enzyme
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
anti-enzyme antibodies selectively inhibit the uptake of oleate in 3T3-L1 adipocytes by 31-55%, but only poorly in fibroblasts, the antibodies have no effect on uptake of 2-deoxyglucose and octanoate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
anti-enzyme antibodies selectively inhibit the uptake of oleate in 3T3-L1 adipocytes by 31-55%, but only poorly in fibroblasts, the antibodies have no effect on uptake of 2-deoxyglucose and octanoate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aminooxyacetic acid hemihydrochloride
inhibitor of C-S lyase, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
(2-chloro-6-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)copper
-
-
(2-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-hydroxyethyl)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)cuprate(1-)
-
-
aminoguanidine
-
competes with the enzyme for pyridoxal 5'-phosphate, forms complexes with pyridoxal 5'-phosphate, 70% enzyme inhibition at 1 mM
aqua[2-([[3-bromo-6-(hydroxy-kappaO)cyclohexa-2,4-dien-1-yl]methylidene]amino-kappaN)benzoato(2-)-kappaO]cuprate(1-)
-
-
aqua[2-([[3-chloro-6-(hydroxy-kappaO)cyclohexa-2,4-dien-1-yl]methylidene]amino-kappaN)benzoato(2-)-kappaO]cuprate(1-)
-
-
diaqua[2-chloro-6-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]-4-(hydroxymethyl)phenolato-kappaO](2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)copper
-
-
diaqua[3-([[2-(carboxy-kappaO)phenyl]imino-kappaN]methyl)-4-(hydroxy-kappaO)cyclohexa-1,5-dien-1-yl](hydroxy)oxoammoniumato(2-)copper
-
-
L-serine O-sulfate
-
inhibition of cytosolic enzyme, no inhibition of mitochondrial enzyme
Pro
-
hyperprolinemia type II is an autosomal recessive disorder caused by severe deficiency of enzyme DELTA1-pyrroline-5-carboxylic acid dehydrogenase leading to tissue accumulation of proline. Proline has direct inhibitory effect on aspartate transaminase activity of different brain regions leading to lesser synthesis of glutamate thereby causing neurological dysfunctions
2-oxoglutaconate
-
2-oxoglutarate protects against inhibition, L-glutamate enhances the inhibitory effect
additional information
-
no inhibition by dipropylacetic acid, vinyl-GABA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aconitate
-
activating effect on the activity of the cytoplasmic enzyme form
cobalt nanoparticle
-
cobalt nanoparticles with particle size less than 50 nm significantly activate the enzyme in the serum, liver, and kidney of rats at concentration-dependent order with a maximum activation of 175% at 10 mM
ethanol
-
binge ethanol treatment causes significant increase in blood plasma AST activity
additional information
-
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
-
additional information
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
-
additional information
-
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
-
additional information
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
-
additional information
-
intramitochondrial chaperone homologues GroEL and GroES can facilitate the folding of nascent premature mitochondrial isoform pmAspAT in rabbit reticulocyte lysate under conditions where it otherwise would not, GroEL alone inhibits the import into mitochondria, which is reversed by GroES
-
additional information
-
carnosine treatment alone does not alter blood plasma AST activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0072
(2-chloro-6-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)copper
Rattus norvegicus
-
at pH 7.5 and 37°C
0.0036
(2-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)(2-hydroxyethyl)(2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)cuprate(1-)
Rattus norvegicus
-
at pH 7.5 and 37°C
0.078
aqua[2-([[3-bromo-6-(hydroxy-kappaO)cyclohexa-2,4-dien-1-yl]methylidene]amino-kappaN)benzoato(2-)-kappaO]cuprate(1-)
Rattus norvegicus
-
at pH 7.5 and 37°C
0.089
aqua[2-([[3-chloro-6-(hydroxy-kappaO)cyclohexa-2,4-dien-1-yl]methylidene]amino-kappaN)benzoato(2-)-kappaO]cuprate(1-)
Rattus norvegicus
-
at pH 7.5 and 37°C
0.012
bis[4-chloro-2-[(phenylimino-kappaN)methyl]phenolato-kappaO]copper
Rattus norvegicus
-
at pH 7.5 and 37°C
0.017
bis[4-nitro-2-[(phenylimino-kappaN)methyl]phenolato-kappaO]copper
Rattus norvegicus
-
at pH 7.5 and 37°C
0.053
diaqua[2-chloro-6-[[(3,5-dimethyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]-4-(hydroxymethyl)phenolato-kappaO](2-[[(3-methyl-4H-1,2,4-triazol-4-yl)imino-kappaN]methyl]phenolato-kappaO)copper
Rattus norvegicus
-
at pH 7.5 and 37°C
0.072
diaqua[3-([[2-(carboxy-kappaO)phenyl]imino-kappaN]methyl)-4-(hydroxy-kappaO)cyclohexa-1,5-dien-1-yl](hydroxy)oxoammoniumato(2-)copper
Rattus norvegicus
-
at pH 7.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 10
-
pH 7.4: 60% of activity maximum, pH 8.5-10.0: activity maximum, cytosolic enzyme
7.4 - 8.7
-
pH 7.4: 95% of activity maximum, pH 8.7: activity maximum, mitochondrial enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
mature mAspAT and premature pmAspAT forms of the isozyme
additional information
-
cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview
-
additional information
cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview
-
additional information
-
cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview
-
additional information
cytosolic and mitochondrial isozymes bind differently to the 70 kDa heat shock protein Hsp70, which regulates the folding and aggregation process of polypeptides, sequence and distribution of Hsp70-binding regions allow the classification of isozymes into a phylogenetic tree, overview
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AATM_RAT
430
0
47314
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3
-
1 h, 10% loss of activity of cytoplasmic enzyme, 40% loss of activity of mitochondrial enzyme
639829
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
15 min, 10% loss of activity for the mitochondrial isozyme, 80% loss of activity with aspartate for the cytosolic isozyme
additional information
-
cysteine sulfinic acid protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cysteinic acid protects the cytosolic isoform against thermal denaturation, not aspartate or 2-oxoglutarate
-
enzyme is stabilized by the intramitochondrial chaperone homologues GroEL and GroES
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
-
differential centrifugation, Sephadex G-25 gel filtration, DEAE cellulose ion exchange chromatography, and Sephadex G-150 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of a liver cDNA fragment, nucleotides 1-419, into a plasmid for production of cRNA probes
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidinium hydrochloride denatured premature form pmAspAT cannot refold at 30°C, but refolds rapidly in presence of the intramitochondrial chaperone homologues GroEL and GroES
-
unfolding in 6 M guanidine hydrochloride for different periods of time. Reactivation of equilibrium-unfolded mAAT is sigmoidal, reactivation of the short term unfolded protein displays a double exponential behavior consistent with the presence of fast and slow refolding species. The presence of coenzyme does not perturb the kinetics or pathway of refolding. Covalently attached PLP slows down the interconversion between fast and slow folding populations of unfolded states. Additional structural rearrangements occurring both in the unfolded state and in populations of folding intermediates along the folding pathway
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Recasens, M.; Benezra, R.; Mandel, P.
Cysteine sulfinate aminotransferase and aspartate aminotransferase isoenzymes of rat brain. Purification, characterization, and further evidence for identity
Biochemistry
19
4583-4589
1980
Rattus norvegicus
Zhou, S.L.; Stump, D.; Kiang, C.L.; Isola, L.M.; Berk, P.D.
Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake
Proc. Soc. Exp. Biol. Med.
208
263-270
1995
Rattus norvegicus
Okada, M.; Ayabe, Y.
Effects of aminoguanidine and pyridoxal phosphate on glycation reaction of aspartate aminotransferase and serum albumin
J. Nutr. Sci. Vitaminol.
41
43-50
1995
Rattus norvegicus
Kato, Y.; Asano, Y.; Makar, T.K.; Cooper, A.J.
Irreversible inactivation of aspartate aminotransferase by 2-oxoglutaconic acid and its dimethyl ester
J. Biochem.
120
531-539
1996
Mus musculus, Rattus norvegicus, Sus scrofa
Mattingly, J.R., Jr.; Yanez, A.J.; Martinez-Carrion, M.
The folding of nascent mitochondrial aspartate aminotransferase synthesized in a cell-free extract can be assisted by GroEL and GroES
Arch. Biochem. Biophys.
382
113-122
2000
Rattus norvegicus
Artigues, A.; Crawford, D.L.; Iriarte, A.; Martinez-Carrion, M.
Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments
J. Biol. Chem.
273
33130-33134
1998
Rattus norvegicus, Rattus norvegicus (P00507)
Oses-Prieto, J.A.; Bengoechea-Alonso, M.T.; Artigues, A.; Iriarte, A.; Martinez-Carrion, M.
The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase
J. Biol. Chem.
278
49988-49999
2003
Rattus norvegicus
Shanti, N.D.; Shashikumar, K.C.; Desai, P.V.
Influence of proline on rat brain activities of alanine aminotransferase, aspartate aminotransferase and acid phosphatase
Neurochem. Res.
29
2197-2206
2004
Rattus norvegicus
Artigues, A.; Iriarte, A.; Martinez-Carrion, M.
Identification of Hsc70 binding sites in mitochondrial aspartate aminotransferase
Arch. Biochem. Biophys.
450
30-38
2006
Rattus norvegicus
Rakhmanova, T.I.; Popova, T.N.
Regulation of 2-oxoglutarate metabolism in rat liver by NADP-isocitrate dehydrogenase and aspartate aminotransferase
Biochemistry
71
211-217
2006
Rattus norvegicus
Guidetti, P.; Amori, L.; Sapko, M.T.; Okuno, E.; Schwarcz, R.
Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain
J. Neurochem.
102
103-111
2007
Homo sapiens, Mus musculus, Rattus norvegicus
McKenna, M.C.; Hopkins, I.B.; Lindauer, S.L.; Bamford, P.
Aspartate aminotransferase in synaptic and nonsynaptic mitochondria: differential effect of compounds that influence transient hetero-enzyme complex (metabolon) formation
Neurochem. Int.
48
629-636
2006
Rattus norvegicus
Artun, B.; Kueskue-Kiraz, Z.; Gulluoglu, M.; Cevikbas, U.; Kocak-Toker, N.; Uysal, M.
The effect of carnosine pretreatment on oxidative stress and hepatotoxicity in binge ethanol administered rats
Hum. Exp. Toxicol.
29
659-665
2010
Rattus norvegicus
Katayama, R.; Nagata, S.; Iida, H.; Yamagishi, N.; Yamashita, T.; Furuhama, K.
Possible role of cysteine-S-conjugate beta-lyase in species differences in cisplatin nephrotoxicity
Food Chem. Toxicol.
49
2053-2059
2011
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus (P00507)
Rasool, A.; Zulfajri, M.; Gulzar, A.; Hanafiah, M.M.; Unnisa, S.A.; Mahboob, M.
In vitro effects of cobalt nanoparticles on aspartate aminotransferase and alanine aminotransferase activities of wistar rats
Biotechnol. Rep.
26
e00453
2020
Rattus norvegicus
Jia, Y.; Lu, L.; Yuan, C.; Feng, S.; Zhu, M.
Aspartate aminotransferase is potently inhibited by copper complexes Exploring copper complex-binding proteome
J. Inorg. Biochem.
170
46-54
2017
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.6.1.1)
Transporter Classification Database (TCDB): 9.A.70.1.1
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