Enzyme affinity in the acylation of lysophosphatidylcholine.
Analogues of 1-palmitoyl-sn-glycero-3-phosphorylcholine were used to ascertain the respective roles of the 1-palmitoyl-sn-glycero and choline groups in binding this substrate to the transferase catalyzing the acylation reaction. 1-Palmitoyl-sn-glycero-3-phosphorylhomocholine proved to be an effective competitive inhibitor whereas 1-palmitoyl-2-deoxyglycero-3-phosphorylcholine was totally ineffective. The data support the view that the 1-palmitoyl-sn-glycero group plays the major role in determining enzyme affinity whereas the choline group functions primarily in the subsequent steps of the acylation reaction.
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000378:metabolism*; D000214:Acyl Coenzyme A / Q000378:metabolism; D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D008244:Lysophosphatidylcholines / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism; D051381:Rats; D013329:Structure-Activity Relationship
D000214:Acyl Coenzyme A; D008244:Lysophosphatidylcholines; D000217:Acyltransferases; D008243:1-Acylglycerophosphocholine O-Acyltransferase