Sandbox reserved 919: Difference between revisions

Hormone-sensitive lipase can be inhibited by phenylmethylsufonyl flouride ([http://en.wikipedia.org/wiki/PMSF PMSF]) covalently bound to the active site. The experiments performed to test this inhibition used different lipases obtained from [http://en.wikipedia.org/wiki/Bacillus_coagulans ''Bacillus coagulans''] as well as lipases from different areas of the human body. PMSF inhibits hydrolase by binding to the catalytic serine residue of the [http://proteopedia.org/wiki/index.php/Serine_Proteases serine protease] active site which disrupts the nucleophilic activity of the catalytic serine.<ref name="Kim">PMID: 19715665 </ref> The sulfur of PMSF binds to the oxygen of the hydroxyl group on the serine residue to form this covalent bond. This inhibitor will only bind to the active site of the catalytic serine because of its participation in the charge relay of the <scene name='58/580296/Meshligandinteraction/1'>catalytic triad</scene>. This hyper activity, indicated by increased temperature around the active site <scene name='58/580296/Meshligand/3'>here</scene>, allows the sulfonyl group of PMSF to <scene name='58/580296/Inhibitorinteraction/4'>covalently bind</scene> to the catalytic serine residue to disrupt its activity. Because of this catalytic serine residue specificity, PMSF does not inhibit all kinds of lipases, such as [http://en.wikipedia.org/wiki/Pancreatic_lipase pancreatic lipase] and lipolase.<ref name="Kanwar">PMID:23923547</ref> PMSF is highly degradable in aqueous solutions as it has a [http://en.wikipedia.org/wiki/Half-life half-life] range of 35-110 minutes at  [http://en.wikipedia.org/wiki/PH pH] levels of 7.0-8.0 <ref name="Gordon">PMID:26289</ref>. PMSF binding induces only a minor conformational change from the <scene name='58/580297/3dnm_ligandsite_triad_chains/7'>native protein</scene>.