The phosphoenolpyruvate : methyl-alpha-d-glucoside phosphotransferase system in Bacillus subtilis Marburg : kinetic studies of enzyme ii and evidence for a phosphoryl enzyme ii intermediate.

@article{Marquet1978TheP,
  title={The phosphoenolpyruvate : methyl-alpha-d-glucoside phosphotransferase system in Bacillus subtilis Marburg : kinetic studies of enzyme ii and evidence for a phosphoryl enzyme ii intermediate.},
  author={Monique Marquet and M C Creignou and Raymond Dedonder},
  journal={Biochimie},
  year={1978},
  volume={60 11-12},
  pages={1283-7}
}
The Enzyme II complex catalyzing the phosphoryl transfer from P-HPr to sugar in the inducible methyl-alpha-D-glucoside : phosphotransferase system in Bacillus subtilis acts according to a ping-pong mechanism, implying a phosphorylated Enzyme II intermediate. This result is supported by the demonstration of a specific transphosphorylation between [14C] alphaMG and glucose-6-phosphate in the presence of an induced Enzyme II preparation. 

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