Characterization of phosphatidate phosphohydrolase activity associated with isolated lamellar bodies.
It has been demonstrated that lamellar bodies isolated from porcine lung have L-alpha-phosphatidate phosphohydrolase (EC 3.1.3.4) activity which cannot be accounted for by microsomal or mitochondrial contamination. Phosphatidate phosphohydrolase activity associated with the lamellar bodies is relatively insensitive to Mg2+ and more heat labile than the activity associated with whole lung microsomes. The enzyme was found to be the most active phosphohydrolase present in isolated lamellar bodies and is inhibited by 5 mM Be2+. Lamellar bodies isolated from human and rat lung tissue were also found to have this activity, and the functional role of the enzyme in lamellar bodies is proposed in relation to glycerophospholipid metabolism.
D000818:Animals; D001608:Beryllium / Q000494:pharmacology; D006801:Humans; D007425:Intracellular Membranes / Q000201:enzymology; D008168:Lung / Q000201:enzymology* / Q000648:ultrastructure; D008274:Magnesium / Q000494:pharmacology; D008861:Microsomes / Q000201:enzymology; D010711:Phosphatidate Phosphatase / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D013552:Swine
D010744:Phosphoric Monoester Hydrolases; D010711:Phosphatidate Phosphatase; D008274:Magnesium; D001608:Beryllium