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EC Tree
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 .
The taxonomic range for the selected organisms is: Thermus thermophilus 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,
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2-oxoglutarate-glutamate aminotransferase
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aminotransferase, aspartate
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aspartate alpha-ketoglutarate transaminase
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aspartate aminotransferase
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aspartate-2-oxoglutarate transaminase
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aspartate:2-oxoglutarate aminotransferase
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aspartic acid aminotransferase
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aspartic aminotransferase
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aspartyl aminotransferase
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glutamate oxaloacetate transaminase
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glutamate-oxalacetate aminotransferase
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glutamate-oxalate transaminase
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glutamic oxalic transaminase
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glutamic-aspartic aminotransferase
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glutamic-aspartic transaminase
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glutamic-oxalacetic transaminase
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glutamic-oxaloacetic transaminase
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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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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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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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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
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amino group transfer
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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
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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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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L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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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
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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pyridoxal 5'-phosphate
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a pyridoxal 5'-phosphate protein
pyridoxal 5'-phosphate
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enzyme-bound
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2-methyl-DL-aspartate
binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex
Maleate
binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme
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2.4
2-oxoglutarate
wild-type, pH 8.0, 25°C
1.7
L-aspartate
wild-type, pH 8.0, 25°C
additional information
additional information
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additional information
additional information
kinetics
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additional information
additional information
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kinetics
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additional information
additional information
wild-type and mutants
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additional information
additional information
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wild-type and mutants
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additional information
additional information
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kinetics
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additional information
additional information
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recombinant enzyme
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120
2-oxoglutarate
wild-type, pH 8.0, 25°C
120
L-aspartate
wild-type, pH 8.0, 25°C
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112.1
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purified recombinant enzyme
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Uniprot
brenda
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native and selenomethionine-substituted TT0402 proteins are crystallized in hanging drops at 4°C
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K109S
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine, increase in pKa value
K109V
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine
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additional information
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high thermostability, extra prolyl residues, located at the surface of the protein, are involved
additional information
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thermal denaturation is irreversible
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recombinant from overproducing Escherichia coli AB1157 cells, 66fold
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gene aspC, expression of wild-type and K109 mutants in Escherichia coli BL21(DE3)
cloning, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli AB1157
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expression in Escherichia coli
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Okamoto, A.; Kato, R.; Masui, R.; Yamagishi, A.; Oshima, T.; Kuramitsu, S.
An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
J. Biochem.
119
135-144
1996
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Nobe, Y.; Kawaguchi, S.; Ura, H.; Nakai, T.; Hirotsu, K.; Kato, R.; Kuramitsu, S.
The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8
J. Biol. Chem.
273
29554-29564
1998
Escherichia coli, Thermus thermophilus (Q56232), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q56232)
brenda
Ktasura, Y.; Shirouzu, M.; Yamaguchi, H.; Ishitani, R.; Nureki, O.; Kuramitsu, S.; Hayashi, H.; Yokoyama, S.
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV
Proteins Struct. Funct. Bioinform.
55
487-492
2004
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Transporter Classification Database (TCDB):
9.A.70.1.1