PMID:9753638

Citation	Seok, YJ, Zhu, PP, Koo, BM and Peterkofsky, A (1998) Autophosphorylation of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system requires dimerization. Biochem. Biophys. Res. Commun. 250:381-4
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.
Links	PubMed Online version:10.1006/bbrc.1998.9323
Keywords	Dimerization; Escherichia coli/enzymology; Phosphoenolpyruvate Sugar Phosphotransferase System/chemistry; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Phosphorylation
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.