Sandbox Reserved 918: Difference between revisions

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===Active Site===
===Active Site===
These substrates, along with many others, are cleaved by DPP IV at its active site containing a [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708</scene>. This Serine-Histadine-Asparatate motif, best known in the enzyme [http://en.wikipedia.org/wiki/Chymotrypsin chymotrypsin], uses acid-base chemistry to facilitate the binding, cleaving, and release of the given substrate. The mechanism of the reaction is as follows:  
These substrates, along with many others, are cleaved by DPP IV at its active site containing a [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad] composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708</scene>. The substrate shown is a DPP IV inhibitorThis Serine-Histadine-Asparatate motif, best known in the enzyme [http://en.wikipedia.org/wiki/Chymotrypsin chymotrypsin], uses acid-base chemistry to facilitate the binding, cleaving, and release of the given substrate. The mechanism of the reaction is as follows:  


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# The negative oxygen on serine readily accepts the hydrogen from histadine and in doing so regenerates the active site of the enzyme.
# The negative oxygen on serine readily accepts the hydrogen from histadine and in doing so regenerates the active site of the enzyme.
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  </div>
In addition to the glutamates holding the substrate in close proximity, and the catalytic triad using acid base chemistry to cleave the peptide bond, there is a tyrosine, <scene name='57/573132/1x70_activesitetyr/2'>Tyr547</scene>, which is depicted in orange and notably only 4.08 [http://en.wikipedia.org/wiki/Angstrom angstroms] away from the substrate, [http://en.wikipedia.org/wiki/Sitagliptin Sitagliptin].


</StructureSection>
</StructureSection>