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Sandbox Reserved 191
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==Cataylitic Triad== | ==Cataylitic Triad== | ||
| - | 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 | + | 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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References
- ↑ ref name= "Mutations" PMID:10781062
