The binding and hydrolysis of sphingomyelin by phospholipase C (Bacillus cereus) as shown by 31P NMR.
31P nuclear magnetic resonance studies showed that heavily inactivated phospholipase C (Bacillus cereus) initially caused line broadening in the 31P resonance from sphingomyelin thus indicating enzyme-lipid association. Using larger amounts of enzyme or longer preincubation caused a displacement of the 31P resonance to a position suggesting phosphorylcholine formation. Incubation of the heavily inactivated enzyme with a phosphonolipid caused a displacement of the 31P resonance suggesting hydrolysis.
D001409:Bacillus cereus / Q000201:enzymology*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010740:Phospholipases / Q000378:metabolism*; D011485:Protein Binding; D013109:Sphingomyelins / Q000378:metabolism*; D010738:Type C Phospholipases / Q000378:metabolism*
D013109:Sphingomyelins; D010740:Phospholipases; D010738:Type C Phospholipases