作者: L. K. Koditschek , W. W. Umbreit
DOI: 10.1128/JB.98.3.1063-1068.1969
关键词: Biochemistry 、 Oxidase test 、 Enzyme 、 Dihydroxyacetone phosphate 、 Cell-free system 、 Yeast extract 、 Flavoprotein 、 Cofactor 、 Diaphorase 、 Biology 、 Molecular biology 、 Microbiology
摘要: Abstract α-Glycerophosphate oxidase, in a strain of Streptococcus faecium, was found to be adaptive aerated conditions growth. The enzyme purified and mediate electron transfer from α-glycerophosphate O2, with the production stoichiometric concentrations H2O2 dihydroxyacetone phosphate. is an anionic flavoprotein, flavine adenine dinucleotide as apparent prosthetic group. By manometric methods, Km 6 × 10−3m, reference substrate concentration, obtained. An active reduced nicotinamide diaphorase closely associated this chromatographic mobility on ECTEOLA-cellulose. oxidase not inhibited by KCN, azide, or sulfhydryl reagents, nor it stimulated α-lipoate, yeast extract, other supplements.