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The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides: [1] triacylglycerol + H 2 O ⇌ diacylglycerol + a carboxylate. These lipases are widely distributed in animals, plants and prokaryotes.
Lipoprotein lipase (LPL) (EC 3.1.1.34, systematic name triacylglycerol acylhydrolase (lipoprotein-dependent)) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase.
Hormone-sensitive lipase (EC 3.1.1.79, HSL), also previously known as cholesteryl ester hydrolase (CEH), [5] sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene, [6] and catalyzes the following reaction: (1) diacylglycerol + H 2 O = monoacylglycerol + a carboxylate
Pancreatic lipase, also known as pancreatic triacylglycerol lipase or steapsin, is an enzyme secreted from the pancreas.As the primary lipase enzyme that hydrolyzes (breaks down) dietary fat molecules in the human digestive system, it is one of the main digestive enzymes, converting triglyceride substrates like 1 found in ingested oils to monoglycerides 3 and free fatty acids 2a and 2b.
Example of a triacylglycerol. Lipolysis / l ɪ ˈ p ɒ l ɪ s ɪ s / is the metabolic pathway through which lipid triglycerides are hydrolyzed into a glycerol and free fatty acids. It is used to mobilize stored energy during fasting or exercise, and usually occurs in fat adipocytes.
This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
Hepatic lipase (HL), also called hepatic triglyceride lipase (HTGL) or LIPC (for "lipase, hepatic"), is a form of lipase, catalyzing the hydrolysis of triacylglyceride. Hepatic lipase is coded by chromosome 15 and its gene is also often referred to as HTGL or LIPC . [ 5 ]
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.