On the relation between a stearoyl-specific transacylase from bovine testis membranes and a copurifying acyltransferase

Biochemistry
David Hollenback, J A Glomset

Abstract

Bovine testis membranes contain a coenzyme A-dependent transacylase that can catalyze the preferential transfer of stearoyl groups from phosphoglycerides to sn-2-acyl molecular species of lysophosphatidic acid and lysophosphatidylinositol [Itabe et al., (1992) J. Biol. Chem. 267, 15319-15325]. We have now purified this enzyme 1000-fold and shown that it copurifies with an acyltransferase. The purified transacylase can use phosphatidic acid, phosphatidylinositol, or phosphatidylinositol-4-phosphate as an acyl donor and catalyzes the transfer of stearoyl groups in preference to palmitoyl groups or oleoyl groups. In contrast, the purified acyltransferase uses acyl-coenzyme A as an acyl donor and shows no such preference for stearoyl group transfer. Furthermore, phosphatidylinositol-4, 5-bisphosphate inhibits the two enzymes to different extents and by different mechanisms. Nevertheless, the enzymes are similar in several respects: they use the same acyl acceptors and, when assayed together, compete for the acyl acceptor, sn-2-oleoyl lysophosphatidic acid; they lose activity in parallel unless stabilized by the addition of an anionic phosphoglyceride or stearoyl-coenzyme A; and they show similar sensitivities to heat and pH. One wa...Continue Reading

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