Sandbox313: Difference between revisions

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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>, 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-structured enzyme.
+The molecule contains many <scene name='Sandbox313/1lpmhydrophobic/3'>hydrophobic</scene> 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 [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPM OCA].