Abstract
Our understanding of the enzyme Coenzyme A-independent transacylase (CoA-IT) has increased dramatically over the last 10 years. The enzyme catalyses the removal of the fatty acyl group from the sn-2 position of glycerophospholipids (GPL) and transfers it into 1-radyl-2-lyso GPL.1 The enzyme shows striking selectivity for transfer of arachidonate and other long-chain, unsaturated fatty acyl groups. It also shows strong preference for phosphocholine-and phosphoethanolamine-containing GPL, along with a preference for using 1-ether GPL as acceptors for the transferred arachidonate.2 The mechanism of action of CoA-IT has yet to be defined at the molecular level, but CoA-IT is hypothesized to be a member of the family of tranferases typified by lecithin-cholesterol acyl transferase.3 Based on these characteristics, CoA-IT has been presumed to play a role in the movement of arachidonate between GPL that occurs in inflammatory cells.4–7
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References
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Winkler, J.D., Sung, CM., Marshall, L.A., Chilton, F.H. (1996). Inhibitors of Arachidonate Metabolism and Effects on PAF Production. In: Nigam, S., Kunkel, G., Prescott, S.M. (eds) Platelet-Activating Factor and Related Lipid Mediators 2. Advances in Experimental Medicine and Biology, vol 416. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0179-8_3
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