A subclass of esterases, pancreatic lipase (EC 3.1.1.3) is an enzyme that catalyzes the hydrolysis and formation of lipids. While produced in the pancreas, it is also present in the stomach and mouth. Due to its effective ester bond hydrolysis of lipids, lipase is essential for fat digestion, breaking lipids into monoglycerides and single fatty acids. If one is lipase deficient, it is hard to obtain adequate nutrition from food. This results in diseases such as cystic fibrosis, Crohn's disease, and celiac disease.
Structure
The quaternary structure of horse pancreatic lipase (as featured right) contains two molecules which each contain 449 amino acid residues, 705 water molecules, and 1 calcium ion. These two identical molecules are connected by a two-fold symmetry axis. The include and salt bridges. The secondary structure of lipase is composed of 102 residues that constitute 13 (22% helical) and 139 residues that constitute 28 strands (30% beta sheets). Lipase is essentially composed of two domains, the , which contains the of lipase (consisting of three residues: Ser-152, Asp-176, and His-263). The N-terminal domain also contains the (residues 216-239) which serves to block the active site, which is nestled in the , from the solvent. Additionally, the is essential to the binding of lipase with colipase, an important cofactor for the catalysis of lipids. This forms the .
Calcium Ligand
The most prominent ligand involved in the structure of lipase is the . This ion has been shown to promote the folding of lipase into its active dimer state. As such, the calcium ion is extremely important in forming the lipase-fat complex, necessary for the breakdown of lipids. Studies have shown that an increase in calcium concentration in a lipase catalyzed reaction resulted in an increase in the rate of the reaction.
Colipase Cofactor
