Lipase

Lipases are a family of enzymes that catalyze the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. They are essential for digestion, absorption, transport, and metabolism of dietary fats. Multiple types exist with tissue-specific functions—pancreatic lipases digest dietary fats in the small intestine; hepatic and hormone-sensitive forms regulate lipid stores in liver and adipose tissue; while endothelial/lipoprotein variants act on circulating triglyceride-rich particles. Structurally, most mammalian lipases share an alpha/beta-hydrolase fold with a catalytic triad typically composed of serine, histidine, and aspartic acid residues. Their activity is tightly regulated by conformational changes involving a lid domain that controls access to their active site. Clinically relevant both as biomarkers for diseases like pancreatitis and as therapeutic targets—most notably by drugs such as orlistat—they play key roles in metabolic health but can also be implicated in disorders ranging from cardiovascular disease to lysosomal storage syndromes.[1][3][5]

Other names

Triacylglycerol lipaseTriglyceride lipasePancreatic lipase (for the digestive isoform)Lipoprotein lipase (for the vascular isoform)Hepatic lipase (for the liver isoform)Hormone-sensitive lipase (for adipocyte isoform)

Inhibition of enzymatic hydrolysis of dietary triglycerides, reducing fat absorption in the intestine[1]