title: Enzyme I: the gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system.
abstract: Regulatory aspects of the bacterial phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) are reviewed. The structure and conformational stability of the first protein (enzyme I) of the PTS, as well as the requirement for enzyme I to dimerize for autophosphorylation by PEP in the presence of MgCl2 are discussed.
authors.affiliation: Section of Protein Chemistry, Laboratory of Biochemistry, National Heart, Blood and Lung Institute, NIH, Bethesda, MD 20892, USA. aog@cu.nih.gov
authors.forename: Ann
authors.initials: A
authors.lastname: Ginsburg
authors.forename: Alan
authors.initials: A
authors.lastname: Peterkofsky
mesh_terms: D019281:Dimerization; D015971:Gene Expression Regulation, Enzymologic; D008954:Models, Biological; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010766:Phosphorylation; D017852:Phosphotransferases (Nitrogenous Group Acceptor) / Q000378:metabolism*; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
chemical_list: D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D017852:Phosphotransferases (Nitrogenous Group Acceptor); C022360:phosphoenolpyruvate-protein phosphotransferase