Synthetic phospholipids as substrates for phospholipase C from Bacillus cereus.
The substrate requirement of phospholipids for hydrolysis with phospholipase C from Bacillus cereus was studied with synthetic lipids well-defined in structure and configuration. For optimal activity, the glycerol molecule must contain three substituents: phosphocholine in sn-3-, an ester bond in sn-2- and an ether- or ester bond in sn-1-position. The length of the ester or ether chains is of minor importance. Any deviation from these structural requirements results in a large decrease in the hydrolysis rate. These essential structural and configurational elements for optimal activity for the B. cereus enzyme are perfectly combined in the platelet activating factor, 1-O-hexadecyl-2-acetyl-sn-glycero-3- phosphocholine. This molecule is one of the best substrates for hydrolysis with the bacterial phospholipase C.
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Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Fleer
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Unger
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Eibl
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H
D001409:Bacillus cereus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D007536:Isomerism; D010743:Phospholipids / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D010767:Phosphorylcholine / Q000737:chemistry; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D010738:Type C Phospholipases / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D010743:Phospholipids; D010767:Phosphorylcholine; D010738:Type C Phospholipases