Oacyltransferases

O-acyltransferases are enzymes that catalyze the transfer of acyl groups to oxygen atoms on acceptor molecules, yielding esters. They participate in lipid metabolism and the modification of various biomolecules by attaching fatty acyl chains to hydroxyl-bearing substrates. The acyl donor is typically an acyl-CoA thioester, though other donors are used by specific enzymes.

The term encompasses multiple enzyme families rather than a single catalytic scaffold. A prominent subset consists of lysophospholipid acyltransferases (LPLATs), such as LPAAT/AGPAT and LPCAT enzymes, which acylate lysophospholipids to produce phospholipids. These reactions generally proceed via acyl transfer from acyl-CoA to an oxygen atom on a lysophospholipid, forming a diacyl phospholipid.

In plants and microbes, O-acyltransferases contribute to the biosynthesis of cuticular lipids, waxes, and other esterified lipids that affect membrane properties and surface traits. In animals, including humans, LPLAT family enzymes participate in phospholipid biosynthesis and remodeling, influencing membrane composition and signaling pathways. O-acyltransferases include enzymes with broad substrate ranges and, in some contexts, may exhibit acyltransferase activity alongside hydrolytic activities under certain conditions.

Due to their central role in lipid assembly and modification, O-acyltransferases are of interest in studies of metabolism, membrane biology, and biotechnological applications aimed at adjusting oil content, fatty acid composition, or surface lipid barriers in plants and microorganisms.