Sandbox 50: Difference between revisions
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[[Image:Lipase mech.gif|200px|left|thumb| lipase-catalyzed hydrolysis of esters<ref>http://www.pnas.org/content/101/16/5716/F6.expansion.html</ref> ]]In the first step, His263 deprotonates Ser152. Ser152 is then free to attack the carboxy carbon of triacylglycerol through a nucleophilic addition reaction. Next, the diacylglycerol product is eliminated when the oxyaninion collapses. This deprotonates His263. In the third step, His263 deprotonates water, which can then attack the carboxyl carbon of Ser152 through a nucleophilic addition reaction. Finally, the carboxylate product and Ser152 are eliminated with the collapse of the oxyanion, and His263 is deprotonated.<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/MACiE/entry/getPage.pl?id=M0218</ref> | [[Image:Lipase mech.gif|200px|left|thumb| lipase-catalyzed hydrolysis of esters<ref>http://www.pnas.org/content/101/16/5716/F6.expansion.html</ref> ]]In the first step, His263 deprotonates Ser152. Ser152 is then free to attack the carboxy carbon of triacylglycerol through a nucleophilic addition reaction. Next, the diacylglycerol product is eliminated when the oxyaninion collapses. This deprotonates His263. In the third step, His263 deprotonates water, which can then attack the carboxyl carbon of Ser152 through a nucleophilic addition reaction. Finally, the carboxylate product and Ser152 are eliminated with the collapse of the oxyanion, and His263 is deprotonated.<ref>http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/MACiE/entry/getPage.pl?id=M0218</ref> | ||