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 language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Aug 19 1974|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology