α-Glycerophosphate Oxidase in Streptococcus faecium F 24

Abstract

α-Glycerophosphate oxidase, in a strain of Streptococcus faecium , was found to be adaptive to aerated conditions of growth. The enzyme was purified and found to mediate electron transfer from α-glycerophosphate to O 2 , with the production of stoichiometric concentrations of H 2 O 2 and dihydroxyacetone phosphate. The enzyme is an anionic flavoprotein, with flavine adenine dinucleotide as the apparent prosthetic group. By manometric methods, a K m of 6 × 10 −3 m , with reference to substrate concentration, was obtained. An active reduced nicotinamide adenine dinucleotide diaphorase was closely associated with this enzyme in chromatographic mobility on ECTEOLA-cellulose. The purified α-glycerophosphate oxidase was not inhibited by KCN, azide, or sulfhydryl reagents, nor was it stimulated by α-lipoate, yeast extract, or other supplements.