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Sandbox Reserved 191
From Proteopedia
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'''<scene name='43/436866/Overall-3-rainbow/1'>Palmitoyl-protein thioesterase 1 (PPT-1)</scene>''' is a small glycoprotein [[hydrolase]] that<ref>ref name= "Mutations" PMID:10781062</ref> breaks the thioester bond between cysteine [[amino acids]] and <scene name='43/436866/Palmitic_acid_self/1'>Palmitic Acid</scene> (Newest). It is a homodimer that is composed primarily of ''alpha helices and beta sheets''(Blue like to PDB) (PDB)and is found in the lysosmes of the cell's of the central nervous system. It has a hydrophobic groove that allows the Palmitic Acid to bind to the hydrolyase, exposing the thioester bond to the catalytic triad. PPT-1 is an important hydrolyae in that it removes Palmatic Acid from proteins. When PPT-1 is not functioning properly, the lipid modified proteins can build up in the cells and cause Infantile whatever (source) | '''<scene name='43/436866/Overall-3-rainbow/1'>Palmitoyl-protein thioesterase 1 (PPT-1)</scene>''' is a small glycoprotein [[hydrolase]] that<ref>ref name= "Mutations" PMID:10781062</ref> breaks the thioester bond between cysteine [[amino acids]] and <scene name='43/436866/Palmitic_acid_self/1'>Palmitic Acid</scene> (Newest). It is a homodimer that is composed primarily of ''alpha helices and beta sheets''(Blue like to PDB) (PDB)and is found in the lysosmes of the cell's of the central nervous system. It has a hydrophobic groove that allows the Palmitic Acid to bind to the hydrolyase, exposing the thioester bond to the catalytic triad. PPT-1 is an important hydrolyae in that it removes Palmatic Acid from proteins. When PPT-1 is not functioning properly, the lipid modified proteins can build up in the cells and cause Infantile whatever (source) | ||
[[Image:Protopedia surface.png|400px|left|thumb|Surface view of PPT-1 showing the hydrophobic groove]] | [[Image:Protopedia surface.png|400px|left|thumb|Surface view of PPT-1 showing the hydrophobic groove]] | ||
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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 tetrahedral collapses and kicks the palmatic acid off of the cysteine residue. | 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. | ||
| - | + | [[Image:Simple RXN.png|400px|left|thumb|Surface view of PPT-1 showing the hydrophobic groove]] | |
<scene name='43/436866/Overall-3-rainbow/1'>Palmitoyl-protein thioesterase 1 (PPT-1)</scene> | <scene name='43/436866/Overall-3-rainbow/1'>Palmitoyl-protein thioesterase 1 (PPT-1)</scene> | ||
Revision as of 01:33, 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
