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Literature summary for 2.6.1.57 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
Search for more literature for 2.6.1.57

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Vigna radiata
-
 mung bean
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Vigna radiata
-
shoot
-
 Vigna radiata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 2-oxoglutarate
-
 Vigna radiata phenylpyruvate + L-glutamate
-
 ?
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
L-tyrosine + 2-oxoglutarate reverse reaction at 40% of the forward reaction Vigna radiata p-hydroxyphenylpyruvate + L-glutamate
-
 r

Cofactor

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