Phospholipase A activity in supernatants from cultures of Bacteroides melaninogenicus.
The phospholipase A activity in culture supernatants of two strains of Bacteroides melaninogenicus is described. The enzyme utilize phosphatidylcholine as substrate and produce mainly lysophosphatidylcholine and free fatty acids. The activities are Ca2+-independent, are not affected by the presence of a chelating agent, have a broad pH range (5-9) and an optimum temperature for activity of approx. 50 degrees C. The activity in a growing bacterial culture increases from the end of the lag phase to the late exponential phase of growth. Analysis of the products resulting from the actions of the enzymes on L-alpha-palmitoyl-beta-oleoyl[1-14C]phosphatidylcholine indicates that the enzymes are phospholipase A1 (EC 3.1.1.32).
D001439:Bacteroides / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D010713:Phosphatidylcholines; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054466:Phospholipases A1; D001443:Prevotella melaninogenica / Q000201:enzymology*; D012995:Solubility; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D010713:Phosphatidylcholines; D010740:Phospholipases; D010741:Phospholipases A; D054466:Phospholipases A1; D002118:Calcium