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Lipase (1lpm)
Mark Omobono, 03.02.09
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| 1lpm, resolution 2.18Å (default scene) | |||||||||||||
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| Ligands: | CA, MPA, NAG | ||||||||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
About this enzyme
Lipase is a single-stranded enzyme that is responsible for breaking down the majority of the dietary lipids (triglycerides, fats, oils) digested by most living organisms. Lipases are located in the digestive juices and general digestive regions of an organism. They are also used in industry as yogurt and cheese fermentation vehicles, as well as more modern applications such as converting vegetable oil to usable fuel [1].
Lipases catalyze the hydrolysis of ester bonds in lipids by employing a chymotrypsin-like hydrolysis mechanism. The enzyme itself is made up of both alpha helicies and beta sheets, but the enzyme activity hinges upon an alpha-beta hydrolase fold [2]. Characteristics of this fold lie in a catalytic triad, all the pieces of which are located on loops.These include the reactive phosphonate center, two calcium ions, and two sugars on the outside of the folded molecule.
The molecule contains many hydrophobic residues, but note that around the active phosphanate site (gold) there is a multitude of hydrophobic residues. This makes sense because the lipase enzyme catalyzes the hydrolysis of hydrophobic molecules as mentioned above.
Full crystallographic information is available from OCA.
