Glycerophospholipid arachidonoyl-transferase (CoA-independent)

Glycerophospholipid arachidonoyl-transferase (CoA-independent), also sometimes referred to as CoA-independent transacylase, represents a class of enzymes that catalyze the transfer of arachidonic acid (20:4, ω-6) from one glycerophospholipid molecule to another, without the requirement of coenzyme A (CoA) as an intermediate. These enzymes are involved in the remodeling of glycerophospholipids, specifically focusing on the introduction or redistribution of arachidonic acid within cellular membranes. This process plays a significant role in regulating membrane fluidity, cell signaling, and the production of eicosanoids, which are potent lipid mediators involved in inflammation, pain, and other physiological processes.

The CoA-independence distinguishes these transacylases from other acyltransferases that utilize CoA as a carrier molecule for the acyl group being transferred. The exact mechanism of action can vary depending on the specific enzyme and its cellular location, but it generally involves a direct transfer of arachidonic acid from the sn-2 position of a donor glycerophospholipid to the sn-2 position of an acceptor glycerophospholipid.

These enzymes are found in various tissues and cell types, and their activity is often regulated by a variety of factors, including calcium ions, other lipids, and specific cellular signals. Disregulation of these transacylases has been implicated in various pathological conditions, including inflammatory diseases, cardiovascular disease, and cancer. Research into these enzymes aims to elucidate their specific roles in health and disease, potentially leading to the development of novel therapeutic strategies.