| Abstract: | A phospholipase specific for cardiolipin (CL) was found in the membrane of Haemophilus parainfluenzae. The enzyme hydrolyzed CL to phosphatidic acid (PA) and phosphatidylglycerol (PG), indicating that it was a phospholipase D (an enzyme activity believed to be confined to higher plants). In addition to its substrate specificity, this enzyme was unusual in its requirement for Mg(2+) (K(m) of 1.3 mm) for maximal activity and its inhibition by chelating agents, heavy metals, some detergents, and organic solvents. When inhibitors of phospholipase activity were added to the growth medium, CL accumulated and PG disappeared in the membrane, suggesting that the phospholipase D was active in vivo. The activity of phospholipase D in cell-free homogenates was greater than expected from earlier studies of CL metabolism and greater than the other phospholipase activities detected in the homogenate. The high activity of the CL-specific phospholipase D suggests there might be a very active degradation of CL to PG and PA and an active resynthesis of CL from the hydrolysis products. |
