Sandbox313
From Proteopedia
(→Lipase (1lpm)) |
(→Lipase (1lpm)) |
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Lipases catalyze the hydrolysis of ester bonds in lipids by employing a chymotrypsin-like hydrolysis mechanism. The enzyme itself is made up of both <scene name='Sandbox313/1lpmalphahelicies/2'>alpha helicies</scene> and <scene name='Sandbox313/1lpmbetasheets/1'>beta sheets</scene> sheets, but the enzyme activity hinges upon an alpha-beta hydrolase fold [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold]. Characteristics of this fold lie in a <scene name='Sandbox313/1lpmligand/2'>catalytic triad</scene>, all the pieces of which are located on loops.These include the reactive <scene name='Sandbox313/1lpmphosphane/1'>phosphonate</scene> center, two <scene name='Sandbox313/1lpmcalcium/1'>calcium ions</scene>, and two <scene name='Sandbox313/1lpmsugars/1'>sugars</scene> on the outside of the folded molecule. | Lipases catalyze the hydrolysis of ester bonds in lipids by employing a chymotrypsin-like hydrolysis mechanism. The enzyme itself is made up of both <scene name='Sandbox313/1lpmalphahelicies/2'>alpha helicies</scene> and <scene name='Sandbox313/1lpmbetasheets/1'>beta sheets</scene> sheets, but the enzyme activity hinges upon an alpha-beta hydrolase fold [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold]. Characteristics of this fold lie in a <scene name='Sandbox313/1lpmligand/2'>catalytic triad</scene>, all the pieces of which are located on loops.These include the reactive <scene name='Sandbox313/1lpmphosphane/1'>phosphonate</scene> center, two <scene name='Sandbox313/1lpmcalcium/1'>calcium ions</scene>, and two <scene name='Sandbox313/1lpmsugars/1'>sugars</scene> on the outside of the folded molecule. | ||
| - | The molecule retains its <scene name='Sandbox313/1lpmhydrophobic/1'>hydrophobic</scene> aspects when folded, making this a well- | + | The molecule retains its <scene name='Sandbox313/1lpmhydrophobic/1'>hydrophobic</scene> aspects when folded, making this a well-structured enzyme. |
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPM OCA]. | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPM OCA]. | ||
Revision as of 15:47, 4 March 2009
Lipase (1lpm)
Mark Omobono, 03.02.09
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| 1lpm, resolution 2.18Å () | |||||||||
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| Ligands: | , , | ||||||||
| 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 | ||||||||
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 and sheets, but the enzyme activity hinges upon an alpha-beta hydrolase fold [2]. Characteristics of this fold lie in a , all the pieces of which are located on loops.These include the reactive center, two , and two on the outside of the folded molecule.
The molecule retains its aspects when folded, making this a well-structured enzyme.
Full crystallographic information is available from OCA.
