Monoamine Transamination Catalyzed by ω-Amino Acid: Pyruvate Aminotransferase of Pseudomonas sp. F-126

Abstract

ω-Amino acid: pyruvate aminotransferase of Pseudomonas sp. F-126 catalyzes stoichiometrically a transamination between various amines and pyruvate. Most of alkyl and aromatic monoamines served as an amino donor. The enzyme activity was affected by carbon number of straight-chain alkylmonoamines with a maximum activity at 5-carbon unit, n-amylamine. Michaelis constants for n-butylamine and pyruvate were calculated to be 66.6mM and 5.5mM respectively. The enzyme was active in the alkaline range with a maximum at pH 10.5_??_11.0, though not any activity was observed at the pH below 8.0. The optimum temperature for the reaction was at 60°C.