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Biochem Biophys Res Commun. 1998 Sep 18;250(2):381-4.

Autophosphorylation of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system requires dimerization.

Author information

1
Department of Microbiology, College of Natural Sciences, Seoul National University, Korea.

Erratum in

  • Biochem Biophys Res Commun 1998 Dec 18;253(2):547.

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.

PMID:
9753638
DOI:
10.1006/bbrc.1998.9323
[Indexed for MEDLINE]

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