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PMID:6986909

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Citation

Misset, O, Brouwer, M and Robillard, GT (1980) Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I. Biochemistry 19:883-90

Abstract

In vitro kinetic measurements have been performed by using purified HPr, EI, and a membrane fraction of EII from the Escherichia coli phosphoenolypyruvate-dependent sugar transport system. These measurements reveal very large lag times in the formation of methyl alpha-glucoside phosphate which are a function of the EI and the EII concentrations. The lag times decrease with increasing concentrations of EI but they increase with increasing concentrations of EII. When EI, together with Mg2+ and phosphoenolpyruvate, is preincubated at 37 degrees C before starting the kinetic measurements, the lag time can be decreased or eliminated. We have shown that the process responsible for the lag time is the activation of EI by dimerization which is influenced by Mg2+ and phosphoenolpyruvate.

Links

PubMed

Keywords

Biological Transport; Carbohydrate Metabolism; Cell Membrane/enzymology; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Magnesium/pharmacology; Mathematics; Methylglucosides/metabolism; Phosphoenolpyruvate Sugar Phosphotransferase System/metabolism; Phosphorylation

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:PT1

enables

GO:0008965: phosphoenolpyruvate-protein phosphotransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ECOLI:PT1

involved_in

GO:0009401: phosphoenolpyruvate-dependent sugar phosphotransferase system

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:PT1

part_of

GO:0019197: phosphoenolpyruvate-dependent sugar phosphotransferase complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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