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		<title>Sandbox Reserved 443 - Revision history</title>
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		<updated>2026-04-12T16:00:55Z</updated>
		<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_443&amp;diff=1895045&amp;oldid=prev</id>
		<title>OCA: New page: &lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt; {{Sandbox_Reserved_Taylor_1}} &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;  ==Trypsin:  an example of a serine protease== Trypsin is a serine pro...</title>
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				<updated>2014-02-09T06:41:23Z</updated>
		
		<summary type="html">&lt;p&gt;New page: &amp;lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&amp;gt; {{Sandbox_Reserved_Taylor_1}} &amp;lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&amp;gt;  ==Trypsin:  an example of a serine protease== Trypsin is a serine pro...&lt;/p&gt;
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==Trypsin:  an example of a serine protease==&lt;br /&gt;
Trypsin is a serine protease.  It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. This structure shows the binding of trypsin to a competitive inhibitor, leupeptin. There is a hydrophobic binding pocket to help align the substrate protein with the enzyme, and an oxyanion hole to stabilize the intermediate.  Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277 &lt;br /&gt;
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{{STRUCTURE_2agi |  PDB=2agi  |  SCENE=  }}&lt;/div&gt;</summary>
		<author><name>OCA</name></author>	</entry>

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