2.6.1.1: aspartate transaminase
This is an abbreviated version!
For detailed information about aspartate transaminase, go to the full flat file.
Word Map on EC 2.6.1.1
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2.6.1.1
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alt
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bilirubin
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cholesterol
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creatinine
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necrosis
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albumin
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triglyceride
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dismutase
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hepatotoxicity
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malondialdehyde
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catalase
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hepatoprotective
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hepatocytes
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wistar
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sod
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fibrosis
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hemoglobin
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platelet
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glutamic-pyruvic
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myocardial
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lipoprotein
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postoperative
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bile
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hematological
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transpeptidase
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tetrachloride
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ccl4
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infarct
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cirrhosis
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gg
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gamma-glutamyl
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uric
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admission
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transaminases
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phosphokinase
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albino
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jaundice
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ccl4-induced
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nafld
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c-reactive
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prothrombin
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glutamyl
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globulin
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gamma-glutamyltransferase
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corpuscular
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tetrachloride-induced
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silymarin
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hematocrit
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synthesis
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kinase-mb
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medicine
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biotechnology
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elastography
- 2.6.1.1
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alt
- bilirubin
- cholesterol
- creatinine
- necrosis
- albumin
- triglyceride
- dismutase
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hepatotoxicity
- malondialdehyde
- catalase
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hepatoprotective
- hepatocytes
- wistar
- sod
- fibrosis
- hemoglobin
- platelet
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glutamic-pyruvic
- myocardial
- lipoprotein
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postoperative
- bile
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hematological
- transpeptidase
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tetrachloride
- ccl4
- infarct
- cirrhosis
- gg
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gamma-glutamyl
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uric
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admission
- transaminases
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phosphokinase
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albino
-
jaundice
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ccl4-induced
- nafld
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c-reactive
- prothrombin
-
glutamyl
- globulin
- gamma-glutamyltransferase
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corpuscular
-
tetrachloride-induced
- silymarin
-
hematocrit
- synthesis
-
kinase-mb
- medicine
- biotechnology
-
elastography
Reaction
Synonyms
2-oxoglutarate-glutamate aminotransferase, AAT, AAT-2, AAT-3, AAT3, aatA, AATase, aatB3, all2340, alr1039, alr2765, alr4853, aminotransferase, aspartate, aoa/coa, AsAT, Asp AT, aspartate alpha-ketoglutarate transaminase, aspartate aminotransferase, aspartate aminotransferase 1, aspartate aminotransferase A, aspartate AT, aspartate transaminase, aspartate, 2-oxoglutarate aminotransferase, aspartate-2-oxoglutarate transaminase, aspartate/(R)-cysteate:2-oxoglutarate aminotransferase, aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase, aspartate:2-oxoglutarate amino-transferase, aspartate:2-oxoglutarate aminotransferase, aspartic acid aminotransferase, aspartic aminotransferase, aspartyl aminotransferase, AspAT, AspATSs, aspB, aspC, AspT, AST, AST-Bb, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, C-S lyase, CAA1, cAST, Cgl0240, class Ibeta AAT, EcAspAT, GL50803_91056, glutamate oxaloacetate transaminase, glutamate oxaloacetate transaminase 1, glutamate-oxalacetate aminotransferase, glutamate-oxalate transaminase, glutamate-oxaloacetate transaminase 1, glutamic oxalic transaminase, glutamic oxaloacetic transaminase, glutamic-aspartic aminotransferase, glutamic-aspartic transaminase, glutamic-oxalacetic transaminase, glutamic-oxaloacetic transaminase, GOT, GOT (enzyme), GOT1, GOT1L1, GOT2, KAT IV, L-aspartate aminotransferase, L-aspartate transaminase, L-aspartate-2-ketoglutarate aminotransferase, L-aspartate-2-oxoglutarate aminotransferase, L-aspartate-2-oxoglutarate-transaminase, L-aspartate-alpha-ketoglutarate transaminase, L-aspartate:2-oxoglutarate aminotransferase, L-aspartateartate aminotransferase, L-aspartic aminotransferase, L-AspAT, mitAAT, More, oxaloacetate transferase, oxaloacetate-aspartate aminotransferase, Pat, PfAspAT, plastid aspartate aminotransferase, prephenate aminotransferase, protein TT0402, PT-AAT, Rv3722c, Sar2028, SsAspAT, Tb11.02.2740, transaminase A
ECTree
2.6.1.1 aspartate transaminaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.6.1.1 - aspartate transaminase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(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
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(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-)
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(S)-4-amino-4,5-dihydro-2-furancarboxylic acid
crystal structures of the Escherichi coli aspartate aminotransferase with (S)-4-amino-4,5-dihydro-2-furancarboxylic acid bound to the active site are obtained via cocrystallization at pH 7.5 and 8. The complex structures suggest that (S)-4-amino-4,5-dihydro-2-furancarboxylic acid inhibits the transamination reaction by forming adducts with the catalytic lysine 246 via a covalent bond while producing 1 equivalent of pyridoxamine 5'-phosphate
2-methyl-DL-aspartate
binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex
2-oxoglutaconic acid dimethyl ester
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15% inhibition at 25°C, pH 7.0, 10 mM, after 2 h; pyridoxal 5'-phosphate enzyme form, cytosolic isozyme
4-(1H-indol-4-yl)-N-[2-(trifluoromethyl)phenyl]piperazine-1-carboxamide
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4-(1H-indol-4-yl)-N-[3-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
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4-(1H-indol-4-yl)-N-[3-(trifluoromethyl)phenyl]piperazine-1-carboxamide
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4-(1H-indol-4-yl)-N-[4-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
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4-(1H-indol-4-yl)-N-[4-(trifluoromethyl)phenyl]piperazine-1-carboxamide
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aminoguanidine
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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-)
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aqua[2-([[3-chloro-6-(hydroxy-kappaO)cyclohexa-2,4-dien-1-yl]methylidene]amino-kappaN)benzoato(2-)-kappaO]cuprate(1-)
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chymoptrypsin
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cytosolic isozyme at 1 mg/ml, no inhibition of mitochondrial isozyme
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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
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diaqua[3-([[2-(carboxy-kappaO)phenyl]imino-kappaN]methyl)-4-(hydroxy-kappaO)cyclohexa-1,5-dien-1-yl](hydroxy)oxoammoniumato(2-)copper
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hydroxylamine
inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity
L-2-amino-5-methoxy-5-oxopentanoic acid
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only isozyme AAT2, competitive against L-asparate
L-Cycloserine
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cytosolic isozyme, weak inhibition only after 24 h incubation, 1 mM
L-histidine
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inhibition is relieved by high concentrations of substrates
L-serine O-sulfate
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inhibition of cytosolic enzyme, no inhibition of mitochondrial enzyme
N-5'-phosphopyridoxyl L-aspartate
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cofactor analogue binds covalently to the enzyme
phosphate
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inhibition of cofactor binding to the apoenzyme, cytosolic and mitochondrial isozymes
Pro
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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
Sodium mersalyl
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cytosolic isozyme, 40% inhibition after 60 min at 5 mM and 30°C
2-oxoglutaconate
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2-oxoglutarate protects against inhibition, L-glutamate enhances the inhibitory effect; 30% inhibition at 25°C, pH 7.2, 10 mM, after 2 h; cytosolic and mitochondrial isozymes
2-oxoglutaconate
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2-oxoglutarate protects against inhibition, L-glutamate enhances the inhibitory effect; 30% inhibition at 25°C, pH 7.2, 10 mM, after 2 h; binds the active site of the pyridoxal 5'-phosphate enzyme form, cytosolic isozyme
2-oxoglutarate
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in cell extracts, alanine activity is inhibited by 50% by about 2.5 mM 2-oxoglutarate, while the aspartate activity is unaffected at this concentration. The highly purified enzyme is also inhibited by 2-oxoglutarate, but the extent of inhibition is slightly more than that in extracts. Thus, alanine activity is completely inhibited by 10 mM 2-oxoglutarate, and 36% of the aspartate activity is inhibited
2-oxoglutarate
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cytoplasmic enzyme inhibited above 0.25 mM, mitochondrial enzyme not
aminooxyacetic acid hemihydrochloride
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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
aminooxyacetic acid hemihydrochloride
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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
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
isonicotinic acid hydrazine
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complete inhibition at 0.3 mM, partially reversible by pyridoxyl 5'-phosphate
isonicotinic acid hydrazine
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cytosolic isozyme, only after 24 h incubation, 1 mM
L-glutamate
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product inhibition, noncompetitive to 2-oxoglutarate and competitive against aspartate
Maleate
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78% inhibition of cytosolic isozyme at 4 mM, competitive to 2-oxoglutarate
Maleate
binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme
p-chloromercuribenzoate
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cytosolic isozyme, 50% inhibition after 10 min at 30°C, 1 mM
additional information
the enzyme is not influenced by EDTA
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additional information
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cytosolic isozyme, no inhibition by L-cysteine and EDTA
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additional information
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the activities with 2 mM aspartate or alanine are not inhibited by 10 mM isoleucine, phenylalanine, arginine, asparagine, glutamine, glycine, lysine, methionine, proline, serine, and threonine
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additional information
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acarbose causes no changes in the specific and total activities of AST
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additional information
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no inhibition by dipropylacetic acid, vinyl-GABA
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