Phosphorylation of intracellular fructose in Bacillus subtilis mediated by phosphoenolpyruvate-1-fructose phosphotransferase.
Intracellular fructose provided by the sorbitol pathway in Bacillus subtilis can be phosphorylated by the phosphenolpyruvate-1-fructose phosphotransferase which is known to mediate a vectorial metabolism. The fate of this intracellular fructose was studied using mutants lacking either the fructose 1-phosphate pathway or the fructose 6-phosphate pathway. It was shown that the phosphoenolpyruvate-dependent phosphorylation needs a prior exit of the sugar into the medium, this exit being probably catalysed by a transport system. A low affinitiy intracellular phosphenolpyruvate phosphotransferase system was found, which seems to be devoid of a physiological role.
D001412:Bacillus subtilis / Q000201:enzymology*; D003201:Computers; D003470:Culture Media; D005632:Fructose / Q000378:metabolism*; D005636:Fructosephosphates / Q000378:metabolism; D007700:Kinetics; D009154:Mutation; D010085:Oxidative Phosphorylation; D010728:Phosphoenolpyruvate; D010770:Phosphotransferases / Q000378:metabolism*; D013012:Sorbitol / Q000378:metabolism; D013045:Species Specificity
D003470:Culture Media; D005636:Fructosephosphates; D005632:Fructose; D013012:Sorbitol; D010728:Phosphoenolpyruvate; D010770:Phosphotransferases