Journal of the Iranian Chemical Society

, Volume 10, Issue 3, pp 593–630

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS): an interface between energy and signal transduction


DOI: 10.1007/s13738-012-0185-1

Cite this article as:
Erni, B. J IRAN CHEM SOC (2013) 10: 593. doi:10.1007/s13738-012-0185-1


The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) mediates the uptake and phosphorylation of carbohydrates, and is involved in signal transduction. It comprises two general phosphotransferase proteins (EI and HPr) and a—species dependent—variable number of sugar-specific enzyme II complexes (IIA, IIB, IIC). EI and HPr transfer phosphoryl groups from PEP to the IIA units. IIA and IIB sequentially transfer phosphates to the sugar, which is translocated by the IIC unit. The ratio of phosphorylated to non-phosphorylated IIA and IIB varies with transport activity, and the phosphorylation state of some of the IIA and IIB serves as signal input for regulation of catabolite repression, intermediate metabolism, gene expression and chemotaxis in response to the availability of carbohydrates and PEP (glycolytic activity). PTS occur in about one-third of all eubacteria and in a few archaebacteria but not in animals and plants. Uniqueness and pleiotropic function make the PTS a potential target for anti-infectives. The PTS transporter for mannose is utilized as a gate for the penetration of bacteriophage lambda DNA across, and insertion of certain bacteriocins (small antimicrobial peptides) into the inner membrane. The PTS of Escherichia coli is in the focus of this review, but occasionally comparisons with other species are made. The topics are: History; Modular design of the E. coli PTS; Structure function and catalytic mechanism of the protein modules; Regulation of and by the PTS; The PTS in pathogenicity and virulence; Computational models; Metabolic engineering.


Bacteriocin Chemotaxis Phosphohistidine Protein phosphorylation Sugar transport Virulence 

Copyright information

© Iranian Chemical Society 2012

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistryUniversity of BernBernSwitzerland