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. 1969 Jun;98(3):1063–1068. doi: 10.1128/jb.98.3.1063-1068.1969

α-Glycerophosphate Oxidase in Streptococcus faecium F 24

L K Koditschek a,1, W W Umbreit a
PMCID: PMC315296  PMID: 5788698

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 O2, with the production of stoichiometric concentrations of H2O2 and dihydroxyacetone phosphate. The enzyme is an anionic flavoprotein, with flavine adenine dinucleotide as the apparent prosthetic group. By manometric methods, a Km of 6 × 10−3m, 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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