REGULATION OF GLYCEROL METABOLISM IN ENTEROCOCCUS-FAECALIS BY PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHORYLATION OF GLYCEROL KINASE CATALYZED BYENZYME-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 gr owth on glycerol-containing medium and that during growth on glycerol the enzyme is mainly phosphorylated. Glucose and other sugars metaboli zed via the Embden-Meyerhof pathway strongly repressed the synthesis o f glycerol kinase, while if glycerol was also present during growth, l ow activity, reflecting partial induction and the presence of mainly u nphosphorylated, less active enzyme, was found. With gluconate, which is also a substrate of the phosphotransferase system, repression of gl ycerol kinase was less severe, but the enzyme was mainly present in th e less active, unphosphorylated form. Effects of growth on different c arbon sources on glycerol uptake are also reported.