title: Autophosphorylation of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system requires dimerization.
abstract: Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system undergoes a slow monomer-dimer transition. In vitro autophosphorylation of Enzyme I by PEP was studied at limiting concentrations of the protein. Addition to incubation mixtures containing wild-type Enzyme I of inactive or low-activity mutant forms of Enzyme I resulted in stimulation of autophosphorylation activity. The kinetics of the activation fit well to a model in which the active form of Enzyme I is the dimer. These experiments provide support for the argument that only the dimeric form of Enzyme I can be autophosphorylated.
authors.affiliation: Department of Microbiology, College of Natural Sciences, Seoul National University, Korea.
authors.forename: Y J
authors.initials: YJ
authors.lastname: Seok
authors.forename: P P
authors.initials: PP
authors.lastname: Zhu
authors.forename: B M
authors.initials: BM
authors.lastname: Koo
authors.forename: A
authors.initials: A
authors.lastname: Peterkofsky
mesh_terms: D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D010731:Phosphoenolpyruvate Sugar Phosphotransferase System