Phospholipase

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Phospholipase cleavage sites. An enzyme that displays both PLA1 and PLA2 activities is called a Phospholipase B.

A phospholipase is an enzyme that hydrolyzes phospholipids[1] into fatty acids and other lipophilic substances. Acids trigger the release of bound calcium from cellular stores and the consequent increase in free cytosolic Ca2+, an essential step in calcium signaling to regulate intracellular processes.[2] There are four major classes, termed A, B, C and D, which are distinguished by the type of reaction which they catalyze:

Types C and D are considered phosphodiesterases.

Endothelial lipase is primarily a phospholipase.[3]

Phospholipase A2 acts on the intact lecithin molecule and hydrolyses the fatty acid esterified to the second carbon atom. The resulting products are lysolecithin and a fatty acid. Phospholipase A2 is an enzyme present in the venom of bees and viper snakes.[4]

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References[edit]

  1. ^ "phospholipase" at Dorland's Medical Dictionary
  2. ^ Molinari, Giuliano; Nervo, Elsa (2021-02-26). "Role of protons in calcium signaling". The Biochemical Journal. 478 (4): 895–910. doi:10.1042/BCJ20200971. ISSN 1470-8728. PMID 33635336.
  3. ^ Yu JE, Han SY, Wolfson B, Zhou Q (2018). "The role of endothelial lipase in lipid metabolism, inflammation, and cancer". Histology and Histopathology. 33 (1): 1–10. doi:10.14670/HH-11-905. PMC 5858721. PMID 28540715.
  4. ^ D. M. Vasudevan & S. Sreekumari, Textbook of Biochemistry (5th ed.)

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