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Information on EC 2.6.1.1 - aspartate transaminase
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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
- creatinine
- triglyceride
-
hepatotoxicity
- catalase
-
hepatoprotective
- wistar
- malondialdehyde
- fibrosis
- gsh
- myocardial
-
glutamic-pyruvic
- platelet
- bile
- infarct
-
gamma-glutamyl
- hemoglobin
- ccl4
-
tetrachloride
- transpeptidase
- cirrhosis
-
postoperative
-
uric
-
phosphokinase
-
hematological
-
portal
-
albino
-
transaminases
- ischemia
-
reperfusion
-
admission
-
ccl4-induced
- biliary
-
prothrombin
-
glutamyl
- silymarin
-
hematocrit
-
aminotransferases
-
globulin
-
thiobarbituric
-
jaundice
- gamma-glutamyltransferase
-
tetrachloride-induced
-
acetaminophen-induced
- gamma-gt
-
corpuscular
- thromboplastin
- synthesis
- biotechnology
- medicine
-
kinase-mb
-
elastography
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
asat, glutamic oxaloacetic transaminase, glutamate oxaloacetate transaminase, glutamic-oxaloacetic transaminase, aspat, glutamic-oxalacetic transaminase, aat-2, aspartic aminotransferase, transaminase a, l-aspartate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate-glutamate aminotransferase
-
-
-
-
AAT
AAT3
aminotransferase, aspartate
-
-
-
-
aoa/coa
AsAT
aspartate alpha-ketoglutarate transaminase
-
-
-
-
aspartate aminotransferase
aspartate-2-oxoglutarate transaminase
-
-
-
-
aspartate/(R)-cysteate:2-oxoglutarate aminotransferase
aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase
-
-
aspartate:2-oxoglutarate aminotransferase
-
-
-
-
aspartic acid aminotransferase
-
-
-
-
aspartic aminotransferase
-
-
-
-
aspartyl aminotransferase
-
-
-
-
AspAT
AspATSs
aspB
AspT
-
-
-
-
AST
C-S lyase
Cgl0240
EcAspAT
wild-type enzyme shows weak desulfination activity and decarboxylation activity
GL50803_91056
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
GOT (enzyme)
-
-
-
-
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-aspartic aminotransferase
-
-
-
-
mitAAT
oxaloacetate transferase
-
-
-
-
oxaloacetate-aspartate aminotransferase
-
-
-
-
protein TT0402
Tb11.02.2740
transaminase A
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-
-
-
additional information
AAT
-
-
-
-
aspartate aminotransferase
-
-
-
-
aspartate/(R)-cysteate:2-oxoglutarate aminotransferase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
AST
-
-
-
-
additional information
-
aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates
additional information
-
EC 2.6.1.57 may be converted to EC 2.6.1.1 by controlled proteolysis with subtilisin, the 2 enzymes are encoded by 2 different genes with high sequence homology
additional information
-
aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
intermediate formation; mechanism
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
active site structure, substrate recognition mechanism
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
active site structure, substrate recognition mechanism
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
bi bi ping pong reaction kinetic
-
-
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Alanine, aspartate and glutamate metabolism, Arginine and proline metabolism, Arginine biosynthesis, Biosynthesis of antibiotics, 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
MetaCyc
(R)-cysteate degradation, anaerobic energy metabolism (invertebrates, cytosol), C4 photosynthetic carbon assimilation cycle, NAD-ME type, C4 photosynthetic carbon assimilation cycle, PEPCK type, coenzyme M biosynthesis II, L-asparagine degradation III (mammalian), L-aspartate biosynthesis, L-aspartate degradation I, L-aspartate degradation II, L-glutamate degradation II, L-phenylalanine biosynthesis I, L-phenylalanine degradation II (anaerobic), L-phenylalanine degradation III, L-phenylalanine degradation IV (mammalian, via side chain), L-phenylalanine degradation VI (Stickland reaction), partial TCA cycle (obligate autotrophs), sulfolactate degradation III
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9000-97-9
-
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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
2-aminohexanedioic acid + 2-oxoglutarate
2-oxohexanedioic acid + L-glutamate
-
i.e. alpha-aminoadipic acid
-
-
?
glycine + 2-oxoglutarate
glyoxylate + L-glutamate
-
7.7% of the activity with aspartate
-
-
?
L-2-amino-4-methoxy-4-oxobutanoic acid + 2-oxoglutarate
4-methoxy-2,4-dioxobutanoic acid + L-glutamate
-
isozymes AAT1 and AAT2, the latter shows lower activity
-
-
?
L-2-amino-4-methoxy-4-oxobutanoic acid + oxaloacetate
4-methoxy-2,4-dioxobutanoic acid + L-aspartate
-
isozymes AAT1 and AAT2, low activity
-
-
?
L-asparagine + 2-oxoglutarate
4-amino-2,4-dioxobutanoate + L-glutamate
O96142
specific activity: 0.14 micromol/min/mg
-
-
?
L-aspartate + 2-oxobutyrate
oxaloacetate + 2-aminobutyrate
-
0.4% activity compared to 2-oxoglutarate
-
-
?
L-aspartate + 2-oxoisocaproate
oxaloacetate + L-leucine
-
1.0% activity compared to 2-oxoglutarate
-
-
?
L-aspartate + 4-hydroxyphenylpyruvate
oxaloacetate + L-tyrosine
Torulopsis candida
-
1.48% of the activity with 2-oxoglutarate
-
-
?
L-aspartate + oxaloacetate
?
relative activity compared to 2-oxoglutarate: 81.5%
-
-
?
L-aspartate + pyruvate
oxaloacetate + L-alanine
-
1.9% activity compared to 2-oxoglutarate
-
-
?
L-erythro-3-hydroxyaspartate + 2-oxoglutarate
erythro-3-hydroxy-2-oxoaspartate + L-glutamate
L-Lys + 2-oxo-4-phenyl-butanoic acid
L-homophenylalanine + 2-keto-6-aminocaproate
-
mutant enzyme R292E/L18H shows a 12.9fold increase in specific activity towards L-Lys and 2-oxo-4-phenylbutanoic acid
2-keto-6-aminocaproate is cyclized nonenzymatically to form DELTA1-piperideine 2-carboxylic acid in the reaction mixture. The low solubility of L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropanoate + L-glutamate
O96142
specific activity: 0.28 micromol/min/mg
-
-
?
L-serine + 2-oxoglutarate
3-hydroxy-2-oxopropionic acid + L-glutamate
-
7.7% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate
O96142
specific activity: 0.16 micromol/min/mg
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
O96142
specific activity: 0.24 micromol/min/mg
-
-
?
(2R,3R)-beta-chloroalanine + 2-mercaptoethanol
3-(2-hydroxyethyl)-cysteine + HCl
-
beta-substitution, reaction occurs with retention of stereochemistry
-
-
?
(2R,3R)-beta-chloroalanine + 2-mercaptoethanol
3-(2-hydroxyethyl)-cysteine + HCl
-
beta-substitution, reaction occurs with retention of stereochemistry
-
-
?
(2R,3S)-beta-chloroalanine + 2-mercaptoethanol
(2R,3S)-3-(2-hydroxyethyl)-cysteine + HCl
-
-
-
-
?
(2R,3S)-beta-chloroalanine + 2-mercaptoethanol
(2R,3S)-3-(2-hydroxyethyl)-cysteine + HCl
-
-
-
-
?
3-aminopropanesulfonate + 2-oxoglutarate
?
-
3-aminopropanesulfonate = homotaurine, lower activity compared to L-cysteate
-
-
?
3-aminopropanesulfonate + 2-oxoglutarate
?
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
3-aminopropanesulfonate = homotaurine, lower activity compared to L-cysteate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
0.7% of the activity with L-aspartate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
activity is not affected by the presence of formate
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
7.7% of the activity with aspartate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
isozyme Asp-DEAE-1 performs preferably the reverse reaction, isozyme the forward reaction
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
relative activity L-aspartate: 100%
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
dolphin
-
role in energy metabolism of diving animals
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
function in C4 acid pathway
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
30% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
reaction mechanism, the strain (unfavourable interaction) of the distorted internal aldimine in the unliganded enzyme is crucial for catalysis. The true driving forces are the strain energy inherent to the respective intermediates. It is described how these strain energies are generated and are used for catalysis
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Escherichia coli B / ATCC 11303
-
30% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Leptosphaeria michotii
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays an important role in numerous metabolic processes
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
absolute specificity for aspartate and 2-oxoglutarate and for glutamate and oxaloacetate
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
key enzyme in assimilation of C and N compounds
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
25.2% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
25.2% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
2-oxoglutarate is the best acceptor substrate
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
45% activity with L-aspartate compared to L-glutamate
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
O96142
specific activity: 2.67 micromol/min/mg
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
34% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
34% of the activity with glutamate
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays the most important role in amino acid metabolism
-
?
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
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
48% of the activity with cysteine sulfinic acid
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
aspartate aminotransferase from Sulfolobus solfataricus does not possess any arginine residue exposed to chemical modifications responsible for the binding of omega-carboxylate of the substrates
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays a central role in nitrogen metabolism of cells
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
best amino acid donor
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?, r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
B0FRH4, B5B1F8
-
-
-
r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + phenylpyruvate
oxaloacetate + L-phenylalanine
-
no activity
-
-
-
L-aspartate + phenylpyruvate
oxaloacetate + L-phenylalanine
Torulopsis candida
-
7.12% of the activity with 2-oxoglutarate
-
-
?
L-cysteate + 2-oxoglutarate
3-sulfopyruvate + L-glutamate
-
L-cysteate = (R)-cysteate
-
-
?
L-cysteate + 2-oxoglutarate
3-sulfopyruvate + L-glutamate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
L-cysteate = (R)-cysteate
-
-
?
L-cysteic acid + 2-oxoglutarate
2-oxo-3-sulfopropionate + L-glutamate
-
no activity
-
-
-
L-cysteic acid + 2-oxoglutarate
2-oxo-3-sulfopropionate + L-glutamate
-
i.e. 2-amino-2-sulfopropionate
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
-
-
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
-
-
-
-
?
L-cysteine + 2-oxoglutarate
2-oxopropionate + L-glutamate
-
26.2% of the activity with L-aspartate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
-
ir
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
-
ir
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
Leptosphaeria michotii
-
only isozyme B, 27% activity compared to L-aspartate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
63% of the activity with aspartate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
27% activity compared to L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
21% of the activity with L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
21% of the activity with L-glutamate
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
best amino acid donor for mitochondrial enzyme
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
Saccharolobus solfataricus MT-4 / DSM 5833
-
-
-
-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionic acid + L-glutamate
-
48% of the activity with L-glutamate
-
-
?
L-erythro-3-hydroxyaspartate + 2-oxoglutarate
erythro-3-hydroxy-2-oxoaspartate + L-glutamate
-
high stabilization of the quinonoid intermediate formed by L-erythro-3-hydroxyaspartate and pyridoxal 5'-phosphate at the active site via Tyr70, kinetic analysis
-
-
?
L-erythro-3-hydroxyaspartate + 2-oxoglutarate
erythro-3-hydroxy-2-oxoaspartate + L-glutamate
-
wild-type, no activity with mutant T70F
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
relative activity compared to L-aspartate: 46.7%
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
dolphin
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
binding of L-Glu to aspartate aminotransferase to form the Michaelis complex does not induce a conformational change in the enzyme. The conformational change to the closed form occurs during the transaldimination step. The hydrophobic residues of the entrance of the active site, including Tyr70, are considered to be important for promoting the transaldimination process and hence the recognition of the C5 substrate
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
the mechanism of the reaction at the early step of the catalysis differs significantly between the substrates L-glutamate and L-aspartate
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
Escherichia coli B / ATCC 11303
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
-
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
-
L-glutamate is best amino acid donor
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
25% of the activity with cysteine sulfinic acid
-
-
?
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
1.0% of the activity with glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
Escherichia coli B / ATCC 11303
-
1.0% of the activity with glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
1.0% of the activity with glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
0.1% activity compared to L-glutamate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
93% of the activity with aspartate
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
Q964F0, Q964F1
-
-
-
?
L-methionine + 2-oxoglutarate
L-glutamate + 4-methylsulfanyl-2-oxobutyric acid
-
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
relative activity compared to L-aspartate: 0.3%
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
low activity
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
low activity
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
dolphin
-
-
-
ir
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
0.07% of the activity with L-aspartate
-
-
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
6.9% of the activity with glutamate
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
7.7% of the activity with L-aspartate
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
i.e. phenylpyruvate
?
L-phenylalanine + 2-oxoglutarate
2-oxo-3-phenylpropionic acid + L-glutamate
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
0.1% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
0.1% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
relative activity compared to L-aspartate: 1.7%
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
11% of the activity with glutamate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
0.08% of the activity with aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
0.08% of the activity with L-aspartate
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
-
-
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
-
?
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropionic acid + L-glutamate
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
relative activity compared to L-aspartate: 0.4
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
low activity
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
low activity
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
dolphin
-
-
-
ir
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
-
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
1.5 of the activity with glutamate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
Escherichia coli B / ATCC 11303
-
1.5 of the activity with glutamate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
0.04% of the activity with aspartate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
0.04% of the activity with L-aspartate
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
1.2% of the activity with glutamate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
84.6% of the activity with aspartate
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
-
i.e. 4-hydroxyphenylpyruvate
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
Q964F0, Q964F1
-
-
-
?
L-tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
-
-
?
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
-
-
-
?
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
B0FRH4, B5B1F8
-
-
-
r
additional information
?
-
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
-
poor substrates are: glyoxylic acid, pyruvate, succinate, maleate, L-asparagine, L-glutamine, L-alanine, glycine
-
-
-
additional information
?
-
-
no activity with L-2-amino-5-methoxy-5-oxopentanoic acid, fumarate, hydroxypyruvate, glutarate, L-proline, L-arginine, and L-lysine
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
-
indole-3-pyruvate, p-hydroxy-phenylpyruvate, and 2-oxo-n-caproate are no substrates
-
-
-
additional information
?
-
no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
-
-
-
additional information
?
-
-
no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine
-
-
-
additional information
?
-
-
no activity with L-cysteine, L-isoleucine, L-leucine, L-valine, L-glutamine, glycine, L-ornithine, L-lysine, L-arginine
-
-
-
additional information
?
-
Q964F0
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
Q964F0
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
additional information
?
-
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
additional information
?
-
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
the cytosolic isoform displays broad substrate specificity
-
-
-
additional information
?
-
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
additional information
?
-
the mitochondrial isoform is highly specific for substrates L-aspartate and 2-oxoglutarate
-
-
-
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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
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
dolphin
-
role in energy metabolism of diving animals
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
function in C4 acid pathway
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Leptosphaeria michotii
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays an important role in numerous metabolic processes
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
key enzyme in assimilation of C and N compounds
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays the most important role in amino acid metabolism
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
P00507
-
-
?
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
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
P14909
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
enzyme plays a central role in nitrogen metabolism of cells
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Q56232
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
active with 1-deazapyridoxal 5'-phosphate a synthetic pyridoxal 5'-phosphate analogue
-
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; isozyme AAT-1: 0.87 mol per mol of subunit, isozyme AAT-2: 0.93 mol per mol of subunit
pyridoxal 5'-phosphate
-
1 mol of pyridoxal phosphate per mol of subunit; apoenzyme can be reconstituted with pyridoxamine 5”phosphate and/or pyridoxal 5'-phosphate, each subunit binding 1 mol of coenzym; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
1 mol of pyridoxal phosphate per mol of subunit
pyridoxal 5'-phosphate
-
2.1 mol of pyridoxal phosphate per mol of enzyme; 2.1mol per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
2 mol of pyridoxal phosphate per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
1.7-1.9 mol per mol of enzyme; a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; bound to the active site
pyridoxal 5'-phosphate
-
a pyridoxal 5'-phosphate protein; bound to the active site
pyridoxal 5'-phosphate
-
binds at the intersubunit active sites and stabilizes the native enzyme form
pyridoxal 5'-phosphate
bound to the active site via a Schiff base to a conserved lysine
pyridoxal 5'-phosphate
bound to the active site via a Schiff base to a conserved lysine
pyridoxal 5'-phosphate
bound to the active site via a Schiff base to a conserved lysine
pyridoxal 5'-phosphate
tight binding to the enzyme, enzyme exhibits catalytic activity without the addition of pyridoxal phosphate to the reaction mixture. The pyridoxal ring is stabilized by the hydrogen bonds with residues Tyr142, Asn191, Asp220, Tyr223, and Lys259
pyridoxamine 5'-phosphate
-
1 mol per mol of subunit; reverse reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
15% inhibition at 25°C, pH 7.0, 10 mM, after 2 h; pyridoxal 5'-phosphate enzyme form, cytosolic isozyme
aminoguanidine
-
competes with the enzyme for pyridoxal 5'-phosphate, forms complexes with pyridoxal 5'-phosphate, 70% enzyme inhibition at 1 mM
chymoptrypsin
-
cytosolic isozyme at 1 mg/ml, no inhibition of mitochondrial isozyme
-
hydroxylamine
O96142
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
-
only isozyme AAT2, competitive against L-asparate
L-Cycloserine
-
cytosolic isozyme, weak inhibition only after 24 h incubation, 1 mM
L-histidine
-
; inhibition is relieved by high concentrations of substrates
L-serine O-sulfate
-
inhibition of cytosolic enzyme, no inhibition of mitochondrial enzyme
N-5'-phosphopyridoxyl L-aspartate
-
cofactor analogue binds covalently to the enzyme
phosphate
-
inhibition of cofactor binding to the apoenzyme, cytosolic and mitochondrial isozymes
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
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
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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aconitate
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activating effect on the activity of the cytoplasmic enzyme form
ethanol
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binge ethanol treatment causes significant increase in blood plasma AST activity
additional information
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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
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additional information
cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function; cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
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additional information
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cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function; cytosolic Hsp70, from bovine brain, protein exclusively binds to the mitochondrial isozyme, regulatory function
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additional information
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carnosine treatment alone does not alter blood plasma AST activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
L-Phe
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pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
0.13
2-oxoglutarate
B0FRH4, B5B1F8
allozyme AAT-2b, pH 7.5, 25°C; allozyme AAT-2c, pH 7.5, 25°C; allozyme AAT-3a, pH 7.5, 25°C
0.48
2-oxoglutarate
-
pH 8, cosubstrate: L-Phe, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
1.33
2-oxoglutarate
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cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
1.95
2-oxoglutarate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
2.6
2-oxoglutarate
-
pH 8, cosubstrate: L-Asp, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
0.43
L-aspartate
-
cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.78
L-aspartate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.5
L-glutamate
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cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.58
L-glutamate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
0.057
oxaloacetate
B0FRH4, B5B1F8
allozyme AAT-2c, pH 7.5, 25°C; allozyme AAT-3b, pH 7.5, 25°C
2.04
oxaloacetate
-
mitochondrial enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 1.6 mM L-aspartate, 4 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase
2.45
oxaloacetate
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cytoplasmic enzyme, in 0.05 M potassium phosphate buffer (pH 7.5) containing 0.9 mM L-aspartate, 2.7 mM 2-oxoglutarate, 0.1 mM NADH, and 1 U/ml malate dehydrogenase