Analysis of glycerol and dihydroxyacetone metabolism in Enterococcus faecium | Zendy

Cindy Staerck | Zendy; Valentin Wasselin | Zendy; Aurélie BudinVerneuil | Zendy; Isabelle Rincé | Zendy; Margherita Cacaci | Zendy; Markus Weigel | Zendy; Caroline Giraud | Zendy; Torsten Hain | Zendy; Axel Hartke | Zendy; Eliette Riboulet-Bisson | Zendy

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Analysis of glycerol and dihydroxyacetone metabolism in Enterococcus faecium

Author(s) -

Cindy Staerck,

Valentin Wasselin,

Aurélie BudinVerneuil,

Isabelle Rincé,

Margherita Cacaci,

Markus Weigel,

Caroline Giraud,

Torsten Hain,

Axel Hartke,

Eliette Riboulet-Bisson

Publication year - 2021

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.899

H-Index - 151

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1093/femsle/fnab043

Subject(s) - dihydroxyacetone , dihydroxyacetone phosphate , operon , biochemistry , enterococcus faecium , biology , glycerol , bacteria , oxidase test , glycerol kinase , nad+ kinase , acetate kinase , metabolism , mutant , enzyme , gene , escherichia coli , genetics , antibiotics

Glycerol (Gly) can be dissimilated by two pathways in bacteria. Either this sugar alcohol is first oxidized to dihydroxyacetone (DHA) and then phosphorylated or it is first phosphorylated to glycerol-3-phosphate (GlyP) followed by oxidation. Oxidation of GlyP can be achieved by NAD-dependent dehydrogenases or by a GlyP oxidase. In both cases, dihydroxyacetone phosphate is the product. Genomic analysis showed that Enterococcus faecium harbors numerous genes annotated to encode activities for the two pathways. However, our physiological analyses of growth on glycerol showed that dissimilation is limited to aerobic conditions and that despite the presence of genes encoding presumed GlyP dehydrogenases, the GlyP oxidase is essential in this process. Although E. faecium contains an operon encoding the phosphotransfer protein DhaM and DHA kinase, which are required for DHA phosphorylation, it is unable to grow on DHA. This operon is highly expressed in stationary phase but its physiological role remains unknown. Finally, data obtained from sequencing of a transposon mutant bank of E. faecium grown on BHI revealed that the GlyP dehydrogenases and a major intrinsic family protein have important but hitherto unknown physiological functions.

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