The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.

@article{Sliz1997TheSO,
  title={The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.},
  author={Piotr Sliz and Roswitha Engelmann and Wolfgang Hengstenberg and Emil F. Pai},
  journal={Structure},
  year={1997},
  volume={5 6},
  pages={775-88}
}
BACKGROUND The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety of metabolic and transcriptional processes. The PTS consists of two non-specific energy coupling components, enzyme I and a heat stable phosphocarrier protein (HPr), as well as several sugar-specific multiprotein permeases known as enzymes II. In… CONTINUE READING

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