Phospholipase A and acyltransferase 5 (PLAAT5)

Phospholipase A and acyltransferase 5 (PLAAT5) is a large cytosolic enzyme that catalyzes both the calcium-independent hydrolysis of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PL A1/A2 activity) and acyltransfer, transferring the fatty acyl group to the primary amine of phosphatidylethanolamine to form N-acylphosphatidylethanolamine (NAPE), an important precursor for bioactive lipid mediators such as N-acylethanolamines[1][3][4]. Unlike other PLAATs, PLAAT5 is not membrane-anchored, is highly expressed in testicular tissue, and is structurally part of the NlpC/P60 superfamily. The HRASLS family, which includes PLAAT5, was historically linked to HRAS-like tumor suppressor activity and cell death modulation. Mutations or disproportional activity of PLAAT5 is associated with genetic syndromes and may play a role in cancer and neurodegenerative diseases due to its biochemical function in phospholipid metabolism and signaling[1][4].

Other names

HRASLS5HRLP5HRSL5iNATRLP1Phospholipase A/acyltransferase-5Calcium-independent phosphatidylethanolamine N-acyltransferaseLecithin-retinol acyltransferase (LRAT)-like protein-1Testicular tissue protein Li 90H-rev107-like protein 5

Drugs targeting PLAAT5 (hypothetically): would inhibit or modulate the enzyme’s phospholipase or acyltransferase activities, affecting NAPE and NAE synthesis and downstream bioactive lipid pathways. Modulation could alter cell death, proliferation, or inflammation associated with altered lipid signaling.