Document Detail

Kinetic behavior of the pancreatic lipase-colipase-lipid system.
MedLine Citation:
PMID:  11099795     Owner:  NLM     Status:  MEDLINE    
Pancreatic lipase is a surface-active protein that binds avidly to interfaces comprised of the substrates and products of lipolysis. However, both lipase binding to substrate-containing particles and subsequent interfacial catalysis are inhibited by a number of amphipathic molecules. The most thoroughly studied of these, phosphatidylcholine, is a common constituent of membranes and intestinal lipid contents. Colipase, a surface-active cofactor of lipase, relieves inhibition by phosphatidylcholine in several ways. Through protein-protein interactions, colipase helps anchor lipase to surfaces and stabilizes it in the open conformation. Within the interface, colipase packs more efficiently with substrates and products of lipolysis than with phosphatidylcholine, thereby concentrating these reactants in the vicinity of colipase. This enrichment of lipase substrates and products in the vicinity of colipase enhances lipase-lipid interactions. The result is that colipase facilitates the adsorption of lipase to the interface and, possibly, increases the availability of substrate to the enzyme. Thus, the functional unit in intestinal lipolysis appears to be a lipase-colipase-reactant complex.
H L Brockman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Biochimie     Volume:  82     ISSN:  0300-9084     ISO Abbreviation:  Biochimie     Publication Date:  2000 Nov 
Date Detail:
Created Date:  2000-12-26     Completed Date:  2001-01-11     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  1264604     Medline TA:  Biochimie     Country:  FRANCE    
Other Details:
Languages:  eng     Pagination:  987-95     Citation Subset:  IM    
The Hormel Institute, University of Minnesota, 801 NE 16th Avenue, MN 55912, Austin, USA.
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MeSH Terms
Lipase / metabolism*
Lipid Metabolism*
Pancreas / enzymology*
Grant Support
Reg. No./Substance:

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