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URB754
URB754 was originally reported by Piomelli ''et al.'' to be a potent, noncompetitive inhibitor of monoacylglycerol lipase Monoacylglycerol lipase (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase, also known as MAG lipase, acylglycerol lipase, MAGL, MGL or MGLL) is an enzyme that, in humans, is encoded by the ''MGLL'' gene. MAGL is a 33-kDa, membrane-associ ... (MGL). However, recent studies have shown that URB754 failed to inhibit recombinant MGL, and brain FAAH activity was also resistant to URB754. In a later study by Piomelli ''et al.'', the MGL-inhibitory activity attributed to URB754 is in fact due to a chemical impurity present in the commercial sample, identified as bis(methylthio)mercurane. References Benzoxazines Lactones {{organic-compound-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monoacylglycerol Lipase
Monoacylglycerol lipase (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase, also known as MAG lipase, acylglycerol lipase, MAGL, MGL or MGLL) is an enzyme that, in humans, is encoded by the ''MGLL'' gene. MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239. Function Monoacylglycerol lipase catalyzes a reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids: : hydrolyses glycerol monoesters of long-chain fatty acids It functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides. Monoacylglycerol lipa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Inhibitor
An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity. Enzymes are proteins that speed up chemical reactions necessary for life, in which substrate molecules are converted into products. An enzyme facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult step of the reaction. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. Enzyme inhibitors may bind reversibly or irreversibly. Irreversible inhibitors form a chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By contrast, reversible inhibitors bind non-covalently and may spontaneously leave the enzyme, allowing the enzyme to resume its function. Reve ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FAAH
Fatty acid amide hydrolase or FAAH (, oleamide hydrolase, anandamide amidohydrolase) is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide in 1993. In humans, it is encoded by the gene ''FAAH''.; Function FAAH is an integral membrane hydrolase with a single ''N''-terminal transmembrane domain. ''In vitro'', FAAH has esterase and amidase activity. ''In vivo'', FAAH is the principal catabolic enzyme for a class of bioactive lipids called the fatty acid amides (FAAs). Members of the FAAs include: * Anandamide (''N''-arachidonoylethanolamine), an endocannabinoid *2-arachidonoylglycerol (2-AG), an endocannabinoid. * Other ''N''-acylethanolamines, such as ''N''-oleoylethanolamine and ''N''-palmitoylethanolamine * The sleep-inducing lipid oleamide * The ''N''-acyltaurines, which are agonists of the transient receptor potential (TRP) family of calcium channels. ''FAAH'' knockout mice display highly elevated (>15-fold) levels of ''N''-a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Benzoxazines
Benzoxazines are a group of isomeric bicyclic heterocyclic chemical compounds that consist of a benzene ring fused to an oxazine ring. The different isomers depend on the relative positions of the oxygen and nitrogen atoms in the oxazine ring, on the location of ring fusion, and on the position of the double bond in the oxazine ring. They have the molecular formula C8H7NO. Preparation 1,3-Benzoxazines can be synthesized by the Mannich reaction using a phenol, an amine, and formaldehyde. Uses Pharmaceutical drugs Benzoxazine rings form the central chemical structure of a number of pharmaceutical drugs including, for example, apararenone, elbasvir, and etifoxine. Polymers Polybenzoxazines, also called benzoxazine resins, are a class of polymers that are produced from the ring-opening polymerization of 3-phenyl-2,4-dihydro-1,3-benzoxazine monomers and its chemical derivatives The derivative of a function is the rate of change of the function's output relative to its input value. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
