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Literature summary for 2.6.1.1 extracted from

  • Smith, D.L.; Almo, S.C.; Toney, M.D.; Ringe, D.
    2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli (1989), Biochemistry, 28, 8161-8167.
    View publication on PubMed
Search for more literature for 2.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
purified mutant K258A, batch method, protein solution: 5.2 mg/ml, 50 mM potassium phosphate, pH 7.5, 53% ammonium sulfate, room temperature, 1 week, preparation of crystals with heavy atom derivatives by soaking crystals for 24 or 48 h, structure analysis Escherichia coli

Protein Variants

Protein Variants Comment Organism
K258A exchange of active site lysine for alanine, binds still pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, but not covalently, the latter forms when bound to the enzyme a covalent stable ketimine with 2-oxoglutarate and effects a beta-decarboxylation of oxaloacetate, followed by transamination to give the pyridoxal 5'-phosphate aldimine of alanine as a final product Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Escherichia coli
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 mutant K258A
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 r

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a pyridoxal 5'-phosphate protein Escherichia coli
pyridoxamine 5'-phosphate reverse reaction Escherichia coli