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 <scene name='58/580296/Meshligand/2'>active site</scene>. 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 allows the sulfonyl group of PMSF to <scene name='58/580296/Inhibitorinteraction/4'>covalently bond</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, lipases such as pancreatic lipase and lipolase will not be inhibited by PMSF.<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] of only one hour at neutral [http://en.wikipedia.org/wiki/PH pH] level. PMSF binding induces only a minor conformational change from the native protein.