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Literature summary for 4.1.1.28 extracted from

  • Dominici, P.; Moore, P.S.; Voltattorni, C.B.
    Modified purification of L-aromatic amino acid decarboxylase from pig kidney (1993), Protein Expr. Purif., 4, 345-347.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Sus scrofa catalyzes the decarboxylation of aromatic amino acids into their corresponding amines ?
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.851
-
-
Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information catalyzes the decarboxylation of aromatic amino acids into their corresponding amines Sus scrofa ?
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate contains 1 mol of coenzyme per dimer Sus scrofa