T. Watanabe et al., ENZYMATIC-PROPERTIES OF AN EXTRACELLULAR QUINOPROTEIN, ENACYLOXIN OXIDASE, Bioscience, biotechnology, and biochemistry, 59(1), 1995, pp. 123-125
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 decarbam
oyl ENX IVa, specifically. The optimum pH and temperature for the enzy
me activity were pH 9.0 and 60 degrees C, respectively. It is suggeste
d that the enzyme is a quinoprotein but its redox cofactor is differen
t from pyrroloquinoline quinone.