Acyl esters of polyprenols: specificity of microsomal transacylase for polyprenols of different chain length and saturation.
Transfer of fatty acids from phospholipids to polyprenols, catalysed by the transacylase from rat liver microsomes, was investigated. The specificity of the enzyme for polyprenols of different chain length and different degree of saturation was studied using individual isoprenologues, the preparation of which in highly tritiated form is described. It was found that short-chain polyprenols are better substrates for the enzyme than long-chain polyprenols, and alpha-saturated better than unsaturated or multiply saturated polyprenols. Short-chain, alpha-saturated single isoprenologues were several-fold more active as acyl acceptors than natural dolichol.
D000214:Acyl Coenzyme A / Q000378:metabolism; D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002070:Butadienes / Q000378:metabolism; D002855:Chromatography, Thin Layer; D005227:Fatty Acids / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology*; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity; D013729:Terpenes / Q000378:metabolism
D000214:Acyl Coenzyme A; D002070:Butadienes; D005227:Fatty Acids; D010743:Phospholipids; D013729:Terpenes; D000217:Acyltransferases