TRANSPORT OF GLUCOSE BY A PHOSPHOENOLPYRUVATE-MANNOSE PHOSPHOTRANSFERASE SYSTEM IN PASTEURELLA-MULTOCIDA

Pasteurella multocida was examined for glucose and mannose transport. P. multocida was shown to possess a phosphoenolpyruvate (PEP):mannose phosphotransferase system (PTS) that transports glucose as well as man nose and was functionally similar to the Escherichia coli mannose PTS. Phosphorylated proteins with molecular masses similar to those of E. coli mannose PTS proteins were visualized when incubated with P-32-PEP . The presence of an enzyme IIA(Glc) which could play an important rol e in regulation, as described in other Gram-negative bacteria, was det ected. The enzymes of the pentose-phosphate pathway were present in P. multocida grown on glucose. The activity of 6-phosphofructokinase (th e key enzyme of the Embden-Meyerhof pathway (EMP)), was very low in ce ll extracts, suggesting that EMP is not the major pathway for glucose catabolism.