Porcine pancreatic lipase (PPL)

Porcine pancreatic lipase is a single-chain, 449-amino-acid glycoprotein enzyme produced by the exocrine pancreas. It is the primary digestive lipase in mammals, catalyzing the hydrolysis of dietary triglycerides at the lipid–water interface of fat droplets formed in the intestine. The enzyme requires the presence of colipase and bile salts for optimal activity. Structurally, it possesses an α/β-hydrolase fold and a conserved catalytic triad (Ser–Asp–His), with a 'lid' domain that covers the active site and mediates interfacial activation. The porcine enzyme serves as the classic biochemical model for the study of mammalian lipases due to its structural and functional similarity to human pancreatic lipase. Inhibition of this enzyme is an approved mechanism for the treatment of obesity, most notably via drugs such as orlistat, which reduces fat absorption and caloric intake by irreversibly inhibiting the catalytic serine residue.

Other names

Triacylglycerol hydrolase (EC 3.1.1.3)Pancreatic triacylglycerol lipase

Competitive and covalent inhibition of the active site serine by drugs like orlistat, blocking triglyceride breakdown and reducing fat absorption