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.
D000438:Alcohols / Q000008:administration & dosage / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D002849:Chromatography, Gas; D005997:Glycerylphosphorylcholine / Q000031:analogs & derivatives / Q000378:metabolism; D007413:Intestinal Mucosa / Q000201:enzymology*; D007421:Intestine, Small / Q000201:enzymology*; D007477:Ions; D008055:Lipids / Q000096:biosynthesis* / Q000302:isolation & purification; D051381:Rats
D000438:Alcohols; D007477:Ions; D008055:Lipids; D005997:Glycerylphosphorylcholine