The Role of Phosphatidylglycerol in the Vectorial Phosphorylation of Sugar by Isolated Bacterial Membrane Preparations
- 1 March 1970
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 65 (3) , 683-690
- https://doi.org/10.1073/pnas.65.3.683
Abstract
Phospholipase D (cabbage) inhibits the vectorial phosphorylation of alpha-methylglucoside by isolated membrane preparations from Escherichia coli ML 308-225 without increasing the efflux of intramembranal alpha-methylglucoside-P. This effect is shown to be related to the ability of phospholipase D to hydrolyze membrane phosphatidylglycerol specifically. After treatment with phospholipase D, the membranes resynthesize phosphatidylglycerol with a return in their ability to take up alpha-methylglucoside. Since proline uptake by the same preparations is only slightly inhibited by phospholipase D, the data indicate that phosphatidylglycerol is required specifically for transport processes which are mediated by the P-enolpyruvate-P-transferase system.Keywords
This publication has 7 references indexed in Scilit:
- REGULATION OF SUGAR TRANSPORT IN ISOLATED BACTERIAL MEMBRANE PREPARATIONS FROM Escherichia coliProceedings of the National Academy of Sciences, 1969
- Proline uptake by disrupted membrane preparations from Escherichia coliArchives of Biochemistry and Biophysics, 1969
- Titles of related papers in other sectionsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1968
- The Role of the Phosphoenolpyruvate-phosphotransferase System in the Transport of Sugars by Isolated Membrane Preparations of Escherichia coliJournal of Biological Chemistry, 1968
- GLYCINE UPTAKE IN ESCHERICHIA COLI .2. GLYCINE UPTAKE EXCHANGE AND METABOLISM BY AN ISOLATED MEMBRANE PREPARATION1968
- Proline uptake by an isolated cytoplasmic membrane preparation of Escherichia coli.Proceedings of the National Academy of Sciences, 1966
- PHOSPHATE BOUND TO HISTIDINE IN A PROTEIN AS AN INTERMEDIATE IN A NOVEL PHOSPHO-TRANSFERASE SYSTEMProceedings of the National Academy of Sciences, 1964