Monoacylglycerol lipase

Monoacylglycerol lipase (also known as MAGL or MGL) is an enzyme that plays a crucial role in lipid metabolism. It is primarily responsible for the hydrolysis of monoacylglycerols (MAGs) into glycerol and fatty acids, a process that is essential for the maintenance of lipid homeostasis in the body.

Function

MAGL is predominantly found in the adipose tissue, where it catalyzes the final step in the degradation of triacylglycerol (TAG), breaking down MAGs into glycerol and fatty acids. This process is vital for the body's energy metabolism, as the released fatty acids can be oxidized to produce adenosine triphosphate (ATP), the body's main energy currency.

In addition to its role in lipid metabolism, MAGL also contributes to the regulation of the endocannabinoid system. It is the primary enzyme responsible for the degradation of 2-arachidonoylglycerol (2-AG), one of the main endocannabinoids in the body. By controlling the levels of 2-AG, MAGL indirectly influences various physiological processes, including pain perception, inflammation, and neuroprotection.

Structure

MAGL is a serine hydrolase, a type of enzyme characterized by the presence of a serine residue in its active site. It is composed of two identical subunits, each containing a catalytic triad of serine, aspartate, and histidine residues. The enzyme's structure allows it to bind to its substrate, a monoacylglycerol molecule, and catalyze its hydrolysis.

Clinical significance

Given its role in lipid metabolism and the endocannabinoid system, MAGL has been implicated in various diseases, including obesity, type 2 diabetes, neurodegenerative diseases, and cancer. Inhibitors of MAGL are currently being investigated as potential therapeutic agents for these conditions.

File:Monoacylglycerol lipase 3D structure.png

3D structure of monoacylglycerol lipase

See also

• Lipase
• Endocannabinoid system
• 2-Arachidonoylglycerol

References

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