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Literature summary for 2.6.1.2 extracted from

  • Orzechowski, S.; Socha-Hanc, J.; Paszkowski, A.
    Purification and properties of alanine aminotransferase from maize (Zea mays L.) leaves (1999), Acta Physiol. Plant., 21, 323-330.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
2 * 50000, SDS-PAGE Zea mays
95000
-
gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
127.5
-
-
Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + 2-oxoglutarate highly specific for alanine and 2-oxoglutarate Zea mays pyruvate + L-glutamate
-
r

Subunits

Subunits Comment Organism
dimer 2 * 50000, SDS-PAGE Zea mays

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Zea mays