Abstract
Phospholipase D (cabbage) inhibits the vectorial phosphorylation of α-methylglucoside by isolated membrane preparations from Escherichia coli ML 308-225 without increasing the efflux of intramembranal α-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 α-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.
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Selected References
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