Lipases
Lipases are a subclass of the enzymes known as esterases that catalyze the breakdown of lipids, due to the water addition (hydrolysis) to the ester linkages present in these compounds. They play a vital role in the digestion, transport, and processing of dietary lipids in most, if not all, living organisms.
Structure[edit | edit source]
Lipases are usually composed of a single polypeptide chain that folds into a globular conformation. They have a catalytic triad that consists of a serine residue, an aspartic acid or glutamic acid residue, and a histidine residue. The active site of lipases is usually buried inside the protein molecule, which is why they require a conformational change to expose the active site to their substrates.
Function[edit | edit source]
Lipases perform essential roles in the digestion, transport, and processing of dietary lipids (e.g., triglycerides, fats, oils) in most, if not all, living organisms. In the human digestive system, the main lipase enzymes are pancreatic lipase (PL) and pancreatic lipase related protein 2 (PLRP2), which are secreted by the pancreas. Human gastric lipase is also involved in the digestion of lipids.
Clinical significance[edit | edit source]
Lipases are also of significant interest in the medical field. They are used in the diagnosis and treatment of diseases such as pancreatitis, celiac disease, and cystic fibrosis. Elevated levels of lipase in the blood can indicate the presence of diseases such as acute pancreatitis, while decreased levels can suggest permanent damage to the lipase-producing cells in the pancreas.
See also[edit | edit source]
Lipases Resources | |
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Contributors: Prab R. Tumpati, MD