The suitability of different acyl acceptors as substrates for the acyl-Coa : 2-acyl-sn-glycero-3-phosphorylcholine acyltransferase in rat liver microsomes.

The fatty acid selectivity of the acyl-CoA : 2-acyl-sn-glycero-3-phosphorylcholine acyltransferase towards different acyl acceptors was studied in rat liver microsomes. The individual molecular species of 2-acylglycerylphosphorylcholine tested as enzyme substrates contained either palmitate, stearate, oleate, linoleate, linolenate or arachidonate with an equimolar mixture of [14C]palmitoyl-CoA plus [3H]stearoyl-CoA serving as the acyl donor. At 2-acyl-sn-glycero-3-phosphorylcholine concentrations of 16 or 64 microM, the various acyl acceptors gave generally similar reactivities, although reaction velocities with the linoleoyl, linolenoyl or arachidonoyl species were moderately greater than those with 2-stearoyl-sn-glycero-3-phosphorylcholine. Regardless of the acyl acceptor tested, little preference towards either palmitoyl-CoA or stearoyl-CoA was indicated at 64 microM 2-acyl-sn-glycero-3-phosphorylcholine whereas a distinct preference for stearate over palmitate (by 1.9--2.6-fold) was exhibited when a lower concentration (16 microM) of the acceptor was employed. The results support the potential importance of the acyl-CoA : 2-acyl-sn-glycero-3-phosphorylcholine acyltransferase for the synthesis of 1-stearoyl 2-unsaturated species of phosphatidylcholine. However, it cannot independently account for the varying palmitate : stearate ratios in the 1-position of this phospholipid when different unsaturated fatty acids reside in the 2-position.