α-Glycerophosphate Oxidase in Streptococcus faecium F 24

作者: L. K. Koditschek , W. W. Umbreit

DOI: 10.1128/JB.98.3.1063-1068.1969

关键词: BiochemistryOxidase testEnzymeDihydroxyacetone phosphateCell-free systemYeast extractFlavoproteinCofactorDiaphoraseBiologyMolecular biologyMicrobiology

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.

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