Introduction

Lipases is a part of the lipase family. Lipases are enzymes that is capable of catalyzing the hydrolysis of fats/lipids which are consumed through oils. It is encoded by the p22 region in chromosome 8. Once synthesized, it is secreted into the inter interstitial space in several tissues. The main site of action for LPL is in the capillary lumen within muscle and adipose tissue. LPL Wiki

Function

The function of this lipase is to hydrolyze triglycerides of very low density lipoproteins (VLDL) and to aid in the delivery of lipid nutrients to vital tissues.

Mechanism

Serine hydrolase mechanism utilized by LPL to catalyze the breakdown of one ester bond of a triglyceride

The transition state of the catalytic triad is stabilized by the .

Relevance & Disease

LPL is an extremely important enzyme, in that it breaks down triglycerides carried on VLDL, which leads to the reduction of cholesterol buildup. Cholesterol build up is a very serious issue with regards to obesity in the United States. In addition to this, increased plasma triglyceride levels (hypertriglyceridemia) is very unhealthy and is the leading cause of Coronary Artery Disease in America. LPL is an enzyme that helps combat this disease by breaking down the excess triglycerides that block the arteries of your heart. Very similarly, Chylomicronemia, a high level of triglycerides in the blood, causes buildup of chylomicrons (ultra-low-density lipoproteins) and leads to similar diseases. Without LPL in the body, developing coronary & metabolic (liver & pancreas) based diseases are at a higher likelihood

Structural highlights

Image of N terminal with active site Image of C terminal domain

References

Arora R, Nimonkar AV, Baird D, Wang C, Chiu CH, Horton PA, Hanrahan S, Cubbon R, Weldon S, Tschantz WR, Mueller S, Brunner R, Lehr P, Meier P, Ottl J, Voznesensky A, Pandey P, Smith TM, Stojanovic A, Flyer A, Benson TE, Romanowski MJ, Trauger JW. Structure of lipoprotein lipase in complex with GPIHBP1. Proc Natl Acad Sci U S A. 2019 May 21;116(21):10360-10365. doi:, 10.1073/pnas.1820171116. Epub 2019 May 9. PMID:31072929doi:http://dx.doi.org/10.1073/pnas.1820171116

Student Contributors

• Giselle Flores
• Dustin Soe
• Maggie Stopa