Octadecatrienoic acids as the substrates for the key enzymes in glycerolipid biosynthesis and fatty acid oxidation in rat liver

The activities of key enzymes in glycerolipid biosynthesis and fatty acid oxidation were compared using CoA esters of naturally occurring positional isomers of octadecatrienoic acids (18∶3) as the substrates. The trienoic acids employed were 9,12,15–18∶3 (α‐18∶3), 6,9,12–18∶3 (γ‐18∶3), and 5,9,12–18∶3 (pinolenic acid which is a fatty acid contained in pine seed oil, po‐18∶3). The activities of microsomal glycerol 3‐phosphate acyltransferase obtained with various 18∶3 were only slightly lower than or comparable with those obtained with palmitic (16∶0), oleic (18∶1), and linoleic (18∶2) acids. Mitochondrial glycerol 3‐phosphate acyltransferase was exclusively specific for saturated fatty acyl‐CoA. The activities of microsomal diacylglycerol acyltransferase measured with various polyunsaturated fatty acyl‐CoAs were significantly lower than those obtained with 16∶0‐ and 18∶1‐CoAs. Among the polyunsaturated fatty acids, γ‐18∶3 gave the distinctly low activity. The V max values of the mitochondrial carnitine palmitoyltransferase I were significantly higher with α‐18∶3 and po‐18∶3 but not γ‐18∶3, than with 16∶0 and 18∶2, while the apparent K m values were the same irrespective of the types of acyl‐CoA used except for the distinctly low value obtained with γ‐18∶3. The response to an inhibitor of the acyltransferase reaction, malonyl‐CoA, was appreciably exaggerated with 18∶2, α‐18∶3, and po‐18∶3 more than with 16∶0 and 18∶1. However, the response with γ‐18∶3 was the same as with 16∶0. Thus, some of glycerolipid biosynthesis and fatty acid oxidation enzymes could discriminate not only the differences in the degree of unsaturation of fatty acids but also the positional distribution of double bond among the naturally occurring 18∶3 acids.