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Literature summary extracted from

  • Simpson, R.M.; Nonhebel, H.M.; Christie, D.L.
    Partial purification and characterization of an aromatic amino acid aminotransferase from mung bean (1997), Planta, 201, 71-77.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.57 additional information not inhibited by idoleacetic acid Vigna radiata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.57 0.07
-
L-phenylalanine
-
Vigna radiata
2.6.1.57 0.08
-
L-tyrosine
-
Vigna radiata
2.6.1.57 0.095
-
L-tryptophan
-
Vigna radiata
2.6.1.57 0.1
-
Indolepyruvate
-
Vigna radiata
2.6.1.57 0.8
-
hydroxyphenylpyruvate
-
Vigna radiata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.57 55000 59000
-
Vigna radiata

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.57 Vigna radiata
-
mung bean
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.57 ammonium sulfate, gel filtration, anion exchange chromatography, Mono Q, phenyl-Superose Vigna radiata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.57 leaf
-
Vigna radiata
-
2.6.1.57 shoot
-
Vigna radiata
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.57 L-phenylalanine + 2-oxoglutarate
-
Vigna radiata phenylpyruvate + L-glutamate
-
?
2.6.1.57 L-tryptophan + 2-oxoglutarate best amino donor, reverse reaction at 30% of the forward reaction, enzyme is able to transaminate alanine, arginine, aspartate, leucine and lysine to a lesser extent, enzyme uses oxaloacetate oxaloacetate and pyruvate as amino acceptors Vigna radiata 3-indole-2-oxopropanoate + L-glutamate
-
r
2.6.1.57 L-tyrosine + 2-oxoglutarate reverse reaction at 40% of the forward reaction Vigna radiata p-hydroxyphenylpyruvate + L-glutamate
-
r

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.57 additional information addition of pyridoxal 5'-phosphate increases the activity of the purified enzyme only slightly Vigna radiata