Exton, John H. Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, Tennessee.
- Phospholipase A1
- Phospholipase A2
- Phospholipase C
- Phospholipase D
- Related Primary Literature
- Additional Reading
Enzymes that hydrolyze membrane phospholipids to generate products that are involved in the regulation of many cellular processes. The activity of phospholipases is controlled by a wide variety of agonists, including hormones, neurotransmitters, growth factors, and cytokines. The principal phospholipases are designated PLA1, PLA2, PLC, and PLD, and they cleave phospholipids at different sites (Fig. 1). PLA1 releases fatty acids from the first position (F1) of phospholipids, whereas PLA2 cleaves them from the second position (F2). PLC hydrolyzes phospholipids at the phosphodiester bond to produce diacylglycerol (DAG) and a phosphorylated head group, as found in phosphocholine or phosphoinositol. PLD hydrolyzes the phosphodiester bond at a different site to yield phosphatidic acid and a free head group, as found in choline or ethanolamine. Phospholipases are widely distributed in nature and are found in almost all mammalian cells. In mammals, the principal substrates of PLA1, PLA2, and PLD are phosphatidylcholine and phosphatidylethanolamine, whereas PLC acts on phosphatidylinositol (PI) and its mono- and bis-phosphates (PIP and PIP2). In plants and bacteria, the phospholipases are less selective toward their substrates. See also: Enzyme; Phospholipid
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