The Activation Method for Phospholipase

Phospholipase B is a term used to define those that catalyze the hydrolysis of phospholipids and lysophopholipids; these enzymes have been isolated from bacterial and mammalian sources, however little is know regarding their action mechanisms. Phospholipase B liberates sebaceous acids and produces glycerophosphorylcholine. Most preparations of phospholipase B are found to yield a mixture of both A1 and A2 phospholipases.

In 1974, Brockerhoff and Jensen described phospholipase 1, 2, 3, 4. Phospholipase 1 was not recognized before 1960, and the author reported that at that place was little information regarding its chemistry or action mechanism. A phospholipase 1 was concluded to hydrolyze the 1-acyl bond of a 1,2-diacyl-sn-glycerol orthophosphate and its esters. The enzyme from E. coli is considered steriotypic; microbial and lysosomal type 1 enzymes have besides been identified. Phospholipases 1 of mammalian intracellular organelles include the microsomal type and the lysosomal type. The lysosomal enzyme of the flair is considered to be competitively inhibited by fatty acids.

Phospholipase 2 is defined as an enzyme that hydrolyzes the ester linkage in position 2 of a phosphoglyceride. Before 1967, these enzymes were referred to as phospholipase A or lecithinase A. Phospholipase 2 was first found in snake venom; the reach report classifies the enzymes into venom enzymes, digestive enzymes, and intracellular enzymes in tis

Zheng, Zhihong, Barkai, Amiram I., & Hungund, Basalingappa L. "Effects of Ethanol on the incorporation of Free Fatty Acids into Cerebral Membrane Phospholipids." Neurochemistry International 28 (5/6, 1996): 551-555.

In 1963 studies showed that S. cerevisiae extracts could degrade phosphatidylcholine; one group showed the extract to block off a phospholipase A coupled with a lysophospholipase or a phospholipase B, which led to a complete deacylation of phosphatidylcholine.

Some enzymes are known to have triglyceride lipase bodily process and phospholipase A1 activity; a membrane-bound phospholipase A1 has been purified from Escherichia coli. A guileless study of the phospholipases A1 of E. coli outer membrane was done by Scandella and Kornberg in 1971.

A key success factor in the purgation of this enzyme was the note that it was stable to treatment with sodium dodecyl sulfate (SDS) and fundamental solvents. The purified phospholipase A1 was found to hydrolyze all the major phospholipids in E. coli; the fatty acid composition had only a slight effect on hydrolysis rates. A second major phospholipase of E. coli was inactivated by detergents and entire solvents and preferentially hydrolyzed phosphatidylglycerol. Functions of the enzyme presumed that it was important for bacterial membrane metabolism, particularly chthonian condition os stress, however, mutants of e. coli deficient in these enzymes have also been isolated.

Phospholipase C found in bovine platelets require Ca2+, are stimulated by amply arachidonate concentrations, and have a high molecular weight. Phospholipase C from lysosomes is found to be widely distributed, however, its activity has been difficult to assess since it competes with phospholipases A1 and A2, and lipases.

Plant phospholipase D catalyzes a transphosphatidylation playacting through a phosphatidate-enzyme intermediate; this is more commonly termed the humble exchange reaction. This enzyme may use a variety of hydroxyl groups to ac
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