Abstract
Extracts of Mycobacterium smegmatis, M. stercoris and M. phlei contain similar lactic oxidases which catalyze the oxidation of L-lactate to acetate, CO2 and water in the presence of molecular oxygen. The enzyme of M. smegmatis was purified to a considerable degree. A purified fraction (Qo2 200,000) was resolved into 2 yellow proteins, one without activity towards lactate and the other with enhanced activity (Q02, 300,000). It was difficult to identify the prosthetic group due to the presence of a chromoprotein impurity. The prosthetic group is not flavin-adenine dinucleotide.