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A phospholipase is an enzyme that hydrolyzes phospholipids [1] into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C, and D, which are distinguished by the type of reaction which they catalyze: Phospholipase A Phospholipase A 1 – cleaves the sn-1 acyl chain (where sn refers to stereospecific numbering).
Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...
This family consists of lysophospholipase / phospholipase B (EC 3.1.1.5) and cytosolic phospholipase A 2 which also has a C2 domain InterPro: IPR000008. Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells. [ 1 ]
Phospholipase C (PLC) is a class of membrane-associated enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which play an important role in eukaryotic cell physiology , in particular signal transduction pathways.
Phospholipase B, also known as lysophospholipase, is an enzyme with a combination of both PLA 1 and PLA 2 activities; that is, it can cleave acyl chains from both the sn-1 and sn-2 positions of a phospholipid. In general, it acts on lysolecithin (which is formed by the action of PLA 2 on lecithin).
Phospholipase D (EC 3.1.4.4, lipophosphodiesterase II, lecithinase D, choline phosphatase, PLD; systematic name phosphatidylcholine phosphatidohydrolase) is an anesthetic sensitive [1] and mechanosensitive [2] enzyme of the phospholipase superfamily that catalyses the following reaction a phosphatidylcholine + H 2 O = choline + a phosphatidate
A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases.
For example, a PLA 1 enzyme with a long lid domain (22-23 amino acids) and a long B9 domain (18-19 amino acids) constitute an extracellular PLA 1 exhibiting triacylglycerol hydrolase activity. [13] In contrast, a PLA 1 enzyme that is considered more selective will have a short lid and B9 domain that span 7-12 and 12-13 amino acids, respectively.