Pyruvic oxime dioxygenase from the heterotrophic nitrifier Alcaligenes faecalis: Purification, and molecular and enzymatic properties

From the heterotrophic nitrifier Alcaligenes faecalis IFO 13111, an enzyme was purified which oxidized pyruvic oxime to nitrite. The molecular mass of the enzyme was 115 kDa and its molecule was composed of three molecules of subunits with the same molecular mass of 40 kDa. The enzyme contained 3 at oms of nonheme iron in the molecule and was active when the iron atoms were in a ferrous state. The enzyme consumed one mol of O-2 to form one mol eac h of nitrite and pyruvate from one mol of pyruvic oxime. Therefore, the enz yme was thought to be a pyruvic oxime dioxygenase.