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 language | English (US) |
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Pages (from-to) | 1204-1210 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 59 |
Issue number | 4 |
DOIs | |
State | Published - Aug 19 1974 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology