Catalytic activities associated with the enzymes II of the bacterial phosphotransferase system

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Abstract
The phosphotransferase system (PTS) in Escherichia coli is a multifunctional, multicomponent enzyme system. Its primary functions deal with carbon source acquisition, while its secondary functions are concerned with the regulation of bacterial physiology. The primary functions of the system include (1) extracellular detection, (2) unidirectional and exchange transmembrane transport, and (3) phosphoenolpyruvate-dependent and sugar phosphate-dependent phosphorylation of the sugar substrates of the system. The secondary functions include (1) regulation of the activities of adenylate cyclase and various non-PTS permeases and (2) regulation of the induced synthesis of several PTS enzymes. Both the primary and secondary functions appear to be elicited by the binding of a sugar substrate to an Enzyme II complex. One of these integral transmembrane enzymes, the mannitol Enzyme II (IImtl), has been solubilized with detergent, purified to homogeneity, and reconstituted in an artificial membrane system. The molecular weight of this protein, IImtl, is 60,000 daltons. It possesses an extracellular sugar binding site and distinct intracellular combining sites for sugar phosphate and phospho-HPr. An essential sulfhydryl group and an antibody combining site are localized to the cytoplasmic surface of the enzyme, while a dextran combining site is localized to the external surface. Preliminary experiments suggest that the different functions of the Enzyme IImtl can be dissected by genetic and biochemical techniques. These studies emphasize the functional complexity of the PTS and its integral membrane protein constituents.