Phospholipase D activity of gram negative bacteria

Abstract

A phospholipase hydrolizing cardiolipin to phosphatidic acid and phosphatidyl glycerol was characterized in gram negative bacteria but was absent in preparations of gram positive bacteria, Saccharomyces cerevisiae, and rat liver mitochondria. In cell free extracts of Escherichia coli, Salmonella typhimurium, Proteus vulgaris, and Pseudomonas aeruginosa, this cardiolipin hydrolyzing enzyme has similar pH and Mg2+ requirements and displayed a specificity which excluded phosphatidyl glycerol and phosphatidyl ethanolamine as substrates.