Colipase

Colipase is a protein is_associated_with::co-enzyme required for optimal is_associated_with::enzyme activity of is_associated_with::pancreatic lipase. It is secreted by the is_associated_with::pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by is_associated_with::trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain is_associated_with::triglycerides.

In humans, the colipase is_associated_with::protein is encoded by the CLPS is_associated_with::gene.

Protein domain
Colipase is also a family of evolutionarily related proteins.

Colipase is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. Efficient absorption of dietary fats is dependent on the action of pancreatic triglyceride lipase. Colipase binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising an active conformation and considerably increasing the hydrophobicity binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture.

Colipase is a small protein with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein (Dickkopf), the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. These non-catalytic domains in the latter enzymes are important for interaction with membrane. It has not been established if these domains are also involved in eventual protein cofactor binding as is the case for pancreatic lipase.