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Literature summary 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.2 50000
-
 2 * 50000, SDS-PAGE Zea mays
2.6.1.2 95000
-
 gel filtration Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.2 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.2
-
 Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.2 leaf
-
 Zea mays
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.2 127.5
-
-
 Zea mays

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.2 pyridoxal 5'-phosphate
-
 Zea mays