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Literature summary for 2.6.1.27 extracted from

  • Koshiba, T.; Mito, N.; Miyakado, M.
    L- And D-tryptophan aminotransferases from maize coleoptiles (1993), J. Plant Res., 106, 25-29.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
isozyme form L-TAT-2, gel filtration Zea mays
55000
-
D-TAT, gel filtration Zea mays
80000
-
isozyme form L-TAT-1, gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
3 isozymes: L-TAT-1 and L-TAT-2 (L-tryptophan aminotransferases), D-TAT (D-tryptophan aminotransferase)
-

Purification (Commentary)

Purification (Comment) Organism
partial, 3 isozymes: L-TAT-1 and L-TAT-2 (L-tryptophan aminotransferases), and D-TAT (D-tryptophan aminotransferase) Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
coleoptile
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-tryptophan + pyruvate no activity with oxaloacetate and 2-oxoglutarate as amino group acceptors Zea mays 3-indole-2-oxopropanoate + L-alanine
-
?
D-tryptophan + pyruvate D-TAT Zea mays 3-indole-2-oxopropanoate + L-alanine
-
?
L-tryptophan + 2-oxoglutarate 2-oxoglutarate is more effective than pyruvate, oxaloacetate and glyoxylate Zea mays L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tryptophan + glyoxylate isozymes L-TAT-1 and L-TAT-2 Zea mays 3-indole-2-oxopropanoate + glycine
-
?
L-tryptophan + oxaloacetate isozymes L-TAT-1 and L-TAT-2 Zea mays 3-indole-2-oxopropanoate + L-aspartate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
D-TAT Zea mays
50 60 both L-TAT isozymes Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9 isozymes L-TAT-1, L-TAT-2, D-TAT Zea mays

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required for full activation Zea mays