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Literature summary extracted from

  • Okamoto, A.; Kato, R.; Masui, R.; Yamagishi, A.; Oshima, T.; Kuramitsu, S.
    An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (1996), J. Biochem., 119, 135-144.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.1 cloning, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli AB1157 Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.1 additional information
-
additional information kinetics Thermus thermophilus
2.6.1.1 additional information
-
additional information recombinant enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate Thermus thermophilus
-
oxaloacetate + L-glutamate
-
?
2.6.1.1 L-aspartate + 2-oxoglutarate Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
oxaloacetate + L-glutamate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.1 Thermus thermophilus
-
-
-
2.6.1.1 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.1 recombinant from overproducing Escherichia coli AB1157 cells, 66fold Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.1 L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate bi bi ping pong reaction kinetic Thermus thermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.1 112.1
-
purified recombinant enzyme Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate
-
Thermus thermophilus oxaloacetate + L-glutamate
-
?
2.6.1.1 L-aspartate + 2-oxoglutarate
-
Thermus thermophilus oxaloacetate + L-glutamate
-
r
2.6.1.1 L-aspartate + 2-oxoglutarate
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 oxaloacetate + L-glutamate
-
?
2.6.1.1 L-aspartate + 2-oxoglutarate
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 oxaloacetate + L-glutamate
-
r

Synonyms

EC Number Synonyms Comment Organism
2.6.1.1 AspAT
-
Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.1 25
-
assay at Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.1 additional information
-
high thermostability, extra prolyl residues, located at the surface of the protein, are involved Thermus thermophilus
2.6.1.1 additional information
-
thermal denaturation is irreversible Thermus thermophilus
2.6.1.1 75
-
stable up to Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.1 8
-
assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.1 pyridoxal 5'-phosphate a pyridoxal 5'-phosphate protein Thermus thermophilus
2.6.1.1 pyridoxal 5'-phosphate enzyme-bound Thermus thermophilus