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Literature summary for 2.6.1.57 extracted from

  • Iwasaki, M.; Hayashi, H.; Kagamiyama, H.
    Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis (1994), J. Biochem., 115, 156-161.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R292A same pKa value as wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
r
L-phenylalanine + 2-oxoglutarate
-
Escherichia coli phenylpyruvate + L-glutamate
-
?
L-tryptophan + 2-oxoglutarate
-
Escherichia coli 3-indole-2-oxopropanoate + L-glutamate
-
r
L-tyrosine + 2-oxoglutarate
-
Escherichia coli p-hydroxyphenylpyruvate + L-glutamate
-
r

Synonyms

Synonyms Comment Organism
ArAT
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Shiff base is formed between Lys258 of ArAT and pyridoxal 5'-phosphate Escherichia coli