Fosfolipaz

Fosfolipaz, also known as phospholipases, are a family of enzymes that catalyze the hydrolysis of phospholipids, the major components of cell membranes. They regulate membrane remodeling and lipid signaling, releasing fatty acids or generating lipid second messengers. Phospholipases are classified by the bond they cleave: A, C, and D types, with phospholipase B as a combined activity in some organisms. The A family includes A1 and A2; PLA1 removes the fatty acid at the sn-1 position of glycerophospholipids to form a lysophospholipid and a free fatty acid; PLA2 cleaves at the sn-2 position to yield a lysophospholipid and a free fatty acid, often liberating arachidonic acid as a precursor for eicosanoids. Phospholipase C enzymes cleave the glycerophosphodiester bond to produce diacylglycerol (DAG) and a phosphorylated head group, such as inositol trisphosphate (IP3). Phospholipase D enzymes split after the phosphate to form phosphatidic acid (PA) and an alcohol (for example choline). Phospholipase B combines A1 and A2 activities in some species and can fully hydrolyze the two fatty acyl chains.

Fosfolipaz exist as secreted and cytosolic forms in animals and as secreted toxins in bacteria and venom. In cellular signaling, PLC-derived DAG and IP3 act as key second messengers controlling calcium release and protein kinase activation; PLA2 activity provides arachidonic acid for inflammatory mediators. Dysregulation of phospholipases is linked to inflammatory diseases, pancreatitis, and neurodegenerative conditions. Industrial and research applications include lipid remodeling, lipidomics workflows, and the modification of phospholipids in food, pharmaceutical, and biotechnology contexts.