Binet M R, Bouvet O M
Unité des Entérobactéries, INSERM U389, Institut Pasteur, Paris.
Res Microbiol. 1998 Feb;149(2):83-94. doi: 10.1016/s0923-2508(98)80024-7.
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 mannose 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 32P-PEP. The presence of an enzyme IIAGlc which could play an important role in regulation, as described in other Gram-negative bacteria, was detected. The enzymes of the pentose-phosphate pathway were present in P. multocida growth on glucose. The activity of 6-phosphofructokinase (the key enzyme of the Embden-Meyerhof pathway (EMP)), was very low in cell extracts, suggesting that EMP is not the major pathway for glucose catabolism.
对多杀性巴氏杆菌进行了葡萄糖和甘露糖转运研究。结果表明，多杀性巴氏杆菌拥有磷酸烯醇式丙酮酸（PEP）：甘露糖磷酸转移酶系统（PTS），该系统可转运葡萄糖和甘露糖，其功能与大肠杆菌甘露糖PTS相似。当与32P-PEP一起孵育时，可观察到分子量与大肠杆菌甘露糖PTS蛋白相似的磷酸化蛋白。检测到一种酶IIAGlc，正如在其他革兰氏阴性菌中所描述的，它可能在调节中发挥重要作用。戊糖磷酸途径的酶存在于多杀性巴氏杆菌利用葡萄糖生长的过程中。细胞提取物中6-磷酸果糖激酶（糖酵解途径（EMP）的关键酶）的活性非常低，这表明EMP不是葡萄糖分解代谢的主要途径。
