Enzymatic bases for the fatty acid positioning in phospholipids of Brevibacterium ammoniagenes.

Abstract

Positional distribution of fatty acids in phospholipids from Brevibacterium ammoniagenes was analyzed to find that phosphatidylethanolamine consisted mainly of 1-saturated acyl 2-unsaturated acyl species while phosphatidylglycerol consisted mainly of 1-unsaturated acyl 2-saturated acyl species. Three acyltransferase systems were characterized in a membrane preparation--the acylations of glycerophosphate, 1-acyl-glycerophosphate, and 2-acyl-glycerophosphate--which appeared to be catalyzed by different enzymes. The distribution of fatty acids in the phosphatidylethanolamine molecule was not correlated simply with the specificities of these enzymes, but the relatively high specificity for palmitoyl-CoA of the glycerophosphate acyltransferase system to form 2-acyl-glycerophosphate, followed the relatively high specificity for oleoyl-CoA of the 2-acyl-glycerophosphate acyltransferase system, provided a basis for producing the major molecular species of phosphatidylglycerol.

Cite this paper

@article{Ohhashi1986EnzymaticBF, title={Enzymatic bases for the fatty acid positioning in phospholipids of Brevibacterium ammoniagenes.}, author={Yoshio Oh-hashi and Masashi Inoue and Shigeki Murase and Masashi Mizuno and Akira Kawaguchi and Hiroaki Okuyama}, journal={Archives of biochemistry and biophysics}, year={1986}, volume={244 2}, pages={413-20} }