Having grasped the enzymology expertise, Creative Enzymes has presented the ability to perform advanced activity measurement for hydrolases. With the most up-to-date instrument and specialized technical support, Creative Enzymes carries out enzymatic activity testing in a reliable and efficient way. Therefore, we provide the most accurate assay results for acylglycerol lipase.

Lipases catalyze the hydrolysis of ester bonds in long chain acylglycerols releasing fatty acids and glycerol. Acylglycerol lipase (MG, EC 3.1.1.23) is unique because it selectively catalyzes the hydrolysis of monoacylglycerol to free fatty acid and glycerol, with no activity toward triacylglycerol or diacylglycerol.

Acylglycerol lipase was first identified in rat adipose tissue. It is found to play an important role in lipid catabolism across all kingdoms of life. In humans, MG (hMG) is the enzyme mainly responsible for hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, which is an important signal molecule in the endocannabinoid metabolism of the central nervous system. Moreover, a role of MG in the progression of melanoma, human breast, ovarian and colorectal cancer has been identified. Inhibition of MG activity in these cancers shows a marked suppression of cell proliferation. Therefore, MG becomes a promising novel target for both cancer treatment and pharmacological research. In bacteria, some MGs show inhibitory effects on the growth of some microorganisms. The antimicrobial activities of MGs depend on the number of carbon atoms and double bonds present in the MGs. Consequently, the antimicrobial agents are developed and used in the food industry, therapeutic, and pharmaceutical applications. The huge potentials in clinical research and industry use trigger fast-growing studies on this enzyme. The characterized crystal structure of human acylglycerol lipase greatly facilitates the screening of the effective inhibitors. In addition of these available knowledge, Creative Enzymes provides precise quantification for acylglycerol lipase activity, which is a powerful tool in search of further evidence in inhibitory effect and applications.

Figure: The crystal structure of human acylglycerol lipase.
Reference: Labar, G. et al. Chembiochem 2010 11: 218-227.

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