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Methods for inhibition of residual lipase activity in colorimetric assay: a comparative study.
The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads
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Hormone-sensitive lipase can be inhibited by phenylmethylsufonyl flouride (PMSF) entering into the active site. PMSF inhibits enzymes by binding to the serine residue of the serine protease active sites so that the normal catalytic activity cannot be carried out. This inhibitor will only bind to the active site serine because of its increased activity from being in the catalytic triad. This hyper activity allows the PMSF to covalently bond to the serine residue to disrupt its activity. Because of this serine residue specificity, PMSF does not inhibit all kinds of lipases, just those dependent on serine residues in the active site. PMSF is highly degradable in aqueous solutions so it does not inhibit for very long periods of time in its natural environment.
