Enzymatic Properties of an Extracellular Quinoprotein, Enacyloxin Oxidase

Abstract

Some properties of enacyloxin (ENX) oxidase from Frateuria sp. [Oyama et al., Biosci. Biotech. Biochem., 58, 1914-1917 (1994)] were studied. The enzyme catalyzed the oxidation of ENX IVa, ENX IIIa, and decarbamoyl ENX IVa, specifically. The optimum pH and temperature for the enzyme activity were pH 9. 0 and 60°C, respectively. It is suggested that the enzyme is a quinoprotein but its redox cofactor is different from pyrroloquinoline quinone.