title: Selectivities of 1-acylglycerophosphorylcholine acyltransferase and acyl-CoA synthetase for n-3 polyunsaturated fatty acids in platelets and liver microsomes.
abstract: 1- Acylglycerophosphorylcholine acyltransferase in platelets and liver microsomes showed a selectivity for polyunsaturated fatty acids. The acyl-donor specificity of the enzyme for 1- acylglycerophosphorylcholine and also 1- acylglycerophosphorylethanolamine was high for n-3 eicosapentaenoyl -CoA and docosahexaenoyl -CoA, and highest for arachidonyl-CoA. Further, the enzyme activity was higher for n-6 eicosatrienoyl -CoA than for n-3 and n-9 eicosatrienoyl -CoAs. It appears that the acyltransferase has a predominant selectivity for n-6 series, but the selectivity is not limited to this series. Acyl-CoA synthetase of liver microsomes and platelets also exhibited a high selectivity for n-3 polyunsaturated fatty acids as well as n-6. In platelets, the acyl-CoA synthetase activity preferential to polyunsaturated fatty acids (n-3 and n-6) was found by competitive aspects of incorporation, in addition to the activity preferential to palmitic acid. In any case, it is suggested that n-3 polyunsaturated fatty acids are easily incorporated into platelet and liver phospholipids.
mesh_terms: D008243:1-Acylglycerophosphocholine O-Acyltransferase; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D001792:Blood Platelets / Q000201:enzymology*; D003066:Coenzyme A Ligases / Q000378:metabolism*; D005231:Fatty Acids, Unsaturated / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008861:Microsomes / Q000201:enzymology; D051381:Rats; D013379:Substrate Specificity
chemical_list: D005231:Fatty Acids, Unsaturated; D000217:Acyltransferases; D008243:1-Acylglycerophosphocholine O-Acyltransferase; D003066:Coenzyme A Ligases