Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system.
Using a polyclonal antibody against glycerol kinase from Enterococcus faecalis, we could demonstrate that glycerol kinase is inducible by growth on glycerol-containing medium and that during growth on glycerol the enzyme is mainly phosphorylated. Glucose and other sugars metabolized via the Embden-Meyerhof pathway strongly repressed the synthesis of glycerol kinase, while if glycerol was also present during growth, low activity, reflecting partial induction and the presence of mainly unphosphorylated, less active enzyme, was found. With gluconate, which is also a substrate of the phosphotransferase system, repression of glycerol kinase was less severe, but the enzyme was mainly present in the less active, unphosphorylated form. Effects of growth on different carbon sources on glycerol uptake are also reported.
Max Planck Institute for Molecular Physiology, Dortmund, Germany.
J
J
Deutscher
B
B
Bauer
H
H
Sauerwald
D001426:Bacterial Proteins / Q000378:metabolism; D001692:Biological Transport; D013293:Enterococcus faecalis / Q000378:metabolism*; D005990:Glycerol / Q000378:metabolism*; D005991:Glycerol Kinase / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation
D001426:Bacterial Proteins; D010750:Phosphoproteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D005991:Glycerol Kinase; D005990:Glycerol