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Journal ArticleDOI

Structure and function of pancreatic lipase and colipase

Mark E. Lowe
- 01 Jan 1997 - 
- Vol. 17, Iss: 1, pp 141-158
TLDR
This review discusses the advances made in protein structure and in understanding the relationships of structure to function of pancreatic triglyceride lipase and colipase.
Abstract
Dietary fats are essential for life and good health. Efficient absorption of dietary fats is dependent on the action of pancreatic triglyceride lipase. In the last few years, large advances have been made in describing the structure and lipolytic mechanism of human pancreatic triglyceride lipase and of colipase, another pancreatic protein that interacts with pancreatic triglyceride lipase and that is required for lipase activity in the duodenum. This review discusses the advances made in protein structure and in understanding the relationships of structure to function of pancreatic triglyceride lipase and colipase.

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Citations
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The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease

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References
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Journal ArticleDOI

Structure of human pancreatic lipase

TL;DR: The structural results are evidence that Ser 152 is the nucleophilic residue essential for catalysis, located in the larger N-terminal domain at the C- terminal edge of a doubly wound parallel β-sheet and part of an Asp-His-Ser triad, which is chemically analogous to, but structurally different from, that in the serine proteases.
Journal ArticleDOI

A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex

TL;DR: It is proposed that the structure of the enzyme in this complex of R. miehei lipase with n-hexylphosphonate ethyl ester is equivalent to the activated state generated by the oil–water interface.
Journal ArticleDOI

Action de la lipase pancréatique sur les esters en émulsion

TL;DR: De considerer la lipase pancreatique comme une esterase particuliere destinee a agir sur des esters insolubles au niveau of l'interface separant ces esters de l'eau, un calcul fait intervenir the “concentration molaire interfaciale” du substrat.
Journal ArticleDOI

Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography.

TL;DR: The three-dimensional structure of the lipase–-procolipase complex, co-crystallized with mixed micelles of phosphatidylcholine and bile salt, has been determined at 3 Å resolution by X-ray crystallography.
Journal ArticleDOI

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

TL;DR: An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
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