Pancreatic lipase enzyme (PL)

Pancreatic lipase is a key digestive enzyme secreted by the pancreas into the small intestine, where it catalyzes the hydrolysis of dietary triglycerides into monoglycerides and free fatty acids—an essential step for efficient fat absorption. Structurally, it consists of two domains: an N-terminal catalytic domain containing an α/β-hydrolase fold with a catalytic triad (serine 152, aspartic acid 176, histidine 263), and a C-terminal domain important for binding cofactors such as colipase. The enzyme's activity depends on interfacial activation—a conformational change that exposes its active site upon contact with lipid-water interfaces. Pancreatic lipase belongs to a broader family that includes hepatic and gastric/lingual lipases but has unique substrate specificity crucial for human nutrition. It serves as an important therapeutic target in obesity management through pharmacological inhibition.

Other names

Pancreatic triacylglycerol lipaseTriacylglycerol acyl hydrolasePTLEC 3.1.1.3

Inhibition of enzymatic hydrolysis of dietary triglycerides, reducing absorption of fats from the gastrointestinal tract