Two routes for synthesis of phosphoenolpyruvate from C4-dicarboxylic acids in Escherichia coli

Eric J. Hansen, Elliot Juni

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Mutants of E. coli defective in both phosphoenolpyruvate carboxykinase and phosphoenolpyruvate synthetase are unable to use C4-dicarboxylic acids such as succinate and malate as carbon and energy sources for growth. Revertants that have restored function for either one of these enzymes can grow in a malate-mineral medium, but at a reduced rate compared with the growth of wild-type cells. E. coli appears to use two pathways for synthesis of phosphoenolpyruvate from C4-dicarboxylic acids. One of these involves decarboxylation of oxalacetate catalyzed by phosphoenolpyruvate carboxykinase. The second pathway makes use of the combined action of malic enzyme and phosphoenolpyruvate synthetase.

Original languageEnglish (US)
Pages (from-to)1204-1210
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume59
Issue number4
DOIs
StatePublished - Aug 19 1974

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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