The role of acyl transferase in the biosynthesis of pulmonary microsomal phosphatidylglycerol.
Dog lung microsome contain an enzymatic system capable of catalyzing the transfer of radiolabel from [14C]-acyl CoA, palmitoyl or oleoyl, to 1-acyl-2-lysophosphatidylglycerol thereby forming phosphatidylglycerol. This synthetic activity is consistent with a 1-acyl-2-lyso-phosphatidylglycerol:acyl-CoA acyl transferase. Kinetic analysis suggests the enzyme is preferentially, but not exclusively, orientated to the production of 1-acyl-2-oleoyl-phosphatidylglycerol. When enzymatic activity was examined with palmitoyl-CoA as the donor substrate and either 2-lysophosphatidylglycerol or 2-lysophosphatidylcholine as the acceptor substrates, the preferred product seemed to be phosphatidylglycerol. When the activity was examined with both acceptor substrates present, phosphatidylglycerol formation decreased while phosphatidylcholine formation increased. This observation may represent an effective control mechanism for the differential synthesis of pulmonary phospholipids, according to metabolic or physiological requirements.
D000214:Acyl Coenzyme A / Q000378:metabolism; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D004285:Dogs; D005227:Fatty Acids / Q000378:metabolism; D008168:Lung / Q000201:enzymology*; D008861:Microsomes / Q000201:enzymology; D010713:Phosphatidylcholines / Q000096:biosynthesis; D010715:Phosphatidylglycerols / Q000378:metabolism*
D000214:Acyl Coenzyme A; D005227:Fatty Acids; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D000217:Acyltransferases