The presence of phospholipase A and lysophospholipase activities in culture supernatant fluid from Alteromonas espejiana.
Culture supernatants from late Log phase cultures of Alteromonas espejiana hydrolyzed phosphatidylinositol to glycerylphosphorylinositol and free fatty acid. No lysophosphatidylimositol was detected. The phospholipase activity degraded up to 50% of the substrate and displayed a broad pH optimum from 6.5-8.5. The activity was slightly stimulated in the presence of either Mg2+ or Ca2+, but was not inhibited by EDTA. The apparent Km for phosphatidylinositol was 1.5 mM. Culture supernatants also contained deacylating activity which released fatty acid from phosphatidylcholine and erythrocyte ghosts.
D001419:Bacteria / Q000201:enzymology*; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008245:Lysophospholipase / Q000378:metabolism*; D010716:Phosphatidylinositols / Q000378:metabolism; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*
D003470:Culture Media; D010716:Phosphatidylinositols; D010740:Phospholipases; D010741:Phospholipases A; D008245:Lysophospholipase