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Literature summary extracted from

  • Tomita, T.; Miyagawa, T.; Miyazaki, T.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
    Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus (2008), Proteins, 75, 348-359.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.39 crystal structures of AAA-AT in four forms: with pyridoxal 5'-phosphate (PLP) (PLP complex), with PLP and leucine (PLP/Leu complex), with N-phosphopyridoxyl-leucine (PPL) (PPL complex), and with N-phosphopyridoxyl-alpha-aminoadipate (PPA) at 2.67, 2.26, 1.75, and 1.67 A resolution, respectively Thermus thermophilus
2.6.1.39 in complex with pyridoxal 5'-phosphate, with pyridoxal 5'-phosphate and leucine, with N-phosphopyridoxyl-leucine, and with N-phosphopyridoxyl-alpha-aminoadipate, at 2.67, 2.26, 1.75 and 1.67 A resolution, respectively. Enzyme contains a mobile alpha2-helix involved in substrate recognition Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.39 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.39 2-aminoadipate + pyruvate
-
 Thermus thermophilus 2-oxoadipate + L-alanine
-
 ?
2.6.1.39 2-oxoadipate + L-glutamate
-
 Thermus thermophilus L-2-aminoadipate + 2-oxoglutarate
-
 ?
2.6.1.39 L-leucine + 2-oxoglutarate
-
 Thermus thermophilus 4-methyl-2-oxopentanoate + L-glutamate
-
 ?
2.6.1.39 additional information AAA-AT can recognize various kinds of substrates using the mobile alpha2 helix Thermus thermophilus ?
-
 ?
2.6.1.39 phenylpyruvate + 2-aminoadipate
-
 Thermus thermophilus L-phenylalanine + 2-oxoglutarate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.39 AAA-AT
-
 Thermus thermophilus
2.6.1.39 alpha-aminoadipate aminotransferase
-
 Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.39 additional information
-
 the crystal structures and site-directed mutagenesis reveales that intersubunit-electrostatic interactions contributes to the elevated thermostability of this enzyme Thermus thermophilus