Substrate specificity of enzymes catalyzing the biosynthesis of ionic alkoxylipids from alcohols

An equimolar mixture of homologous saturated alcohols (13:0, 15:0, 17:0, 19:0) and an equimolar mixture of vinylogous alcohols (19:0, 19:1, 19:2) were fed to two groups of rats. All of the odd-numbered alcohols were incorporated into the ionic alkoxylipids of the rats' small intestine. Pronounced quantitative differences in the distribution of the various odd-numbered alkyl and alk-1-enyl moieties of choline phosphoglycerides and ethanolamine phosphoglycerides gave evidence to differences in the specificity of the enzyme system catalyzing the biosynthesis of alkoxylipids from long-chain alcohols.