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Sandbox Reserved 191

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==Cataylitic Triad==
==Cataylitic Triad==
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PPT-1's structure creates an external hydrophobic groove that binds the palmitate acid. The catalytic <scene name='43/436866/Triad_all_marked/1'>triad</scene> is composed of Serine 115, Aspartate 233, and Histidine 289 (source). The Serine is "deprotonated" by the HIstidine and attacks the carbonyl carbon of the palmitic acid. The negative charge is pushed onto the oxygen and is possible stabilized by a water molecule. The tethedral collapses and kicks the palmatic acid off of the cystine residue.
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PPT-1's structure creates an external hydrophobic groove that binds the palmitate acid. The catalytic <scene name='43/436866/Triad_all_marked/1'>triad</scene> is composed of Serine 115, Aspartate 233, and Histidine 289 (source). The Serine is "deprotonated" by the HIstidine and attacks the carbonyl carbon of the palmitic acid. The negative charge is pushed onto the oxygen and is possible stabilized by a water molecule. The tetrahedral collapses and kicks the palmatic acid off of the cysteine residue.

Revision as of 00:03, 2 April 2014

This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200.
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  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert a 3D applet Jmol scene window.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

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Palmitoyl-protein thioesterase 1 (PPT-1)

Drag the structure with the mouse to rotate


References

  1. ref name= "Mutations" PMID:10781062
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