Sandbox Reserved 1091: Difference between revisions

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The [http://en.wikipedia.org/wiki/Catalytic_triad '''catalytic triad'''] of ASP is composed of '''Asp78''', '''His115''' and '''Ser336'''. A peptide can be inserted in the space of the active site. The amino acids of <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> will interact together and the mechanism will lead to a cut in the polypeptide. This triad can be observed in a 2D representation of the protein : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F3/ '''catalytic triad of ASP''']

The '''mechanism''' of the reaction is that the histidine will react with the serine and deprotonate it. The deprotonated hydroxyl group of the serine will act as a nucleophilic species and attack the carbon from the carbonyl function on the peptide. This will lead to the formation of a tetrahedral intermediate. The regeneration of the carbonyl group will be followed by the release of one part of the peptide, with an amine group at its extremity. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. In the end, the regeneration of the active site will be done with the release of the part of the peptide with a carboxyl extremity. '''The polypeptide is also cut in two parts and the target protein isn't functional anymore'''. <ref>http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png</ref>A schematic representation of the mechanism with the involved amino acids can be found under the following link : [http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png '''mechanism of the reaction''' ]

Sandbox Reserved 1091: Difference between revisions

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Revision as of 14:06, 12 January 2022 view source Amélie Mailliot (talk \| contribs) 7 edits No edit summary ← Older edit		Revision as of 14:07, 12 January 2022 view source Amélie Mailliot (talk \| contribs) 7 edits No edit summary Newer edit →
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	The [http://en.wikipedia.org/wiki/Catalytic_triad '''catalytic triad'''] of ASP is composed of '''Asp78''', '''His115''' and '''Ser336'''. A peptide can be inserted in the space of the active site. The amino acids of <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> will interact together and the mechanism will lead to a cut in the polypeptide. This triad can be observed in a 2D representation of the protein : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F3/ '''catalytic triad of ASP''']		The [http://en.wikipedia.org/wiki/Catalytic_triad '''catalytic triad'''] of ASP is composed of '''Asp78''', '''His115''' and '''Ser336'''. A peptide can be inserted in the space of the active site. The amino acids of <scene name='82/829344/Catalytic_triad/2'>the catalytic triad</scene> will interact together and the mechanism will lead to a cut in the polypeptide. This triad can be observed in a 2D representation of the protein : [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785694/figure/F3/ '''catalytic triad of ASP''']


	The '''mechanism''' of the reaction is that the histidine will react with the serine and deprotonate it. The deprotonated hydroxyl group of the serine will act as a nucleophilic species and attack the carbon from the carbonyl function on the peptide. This will lead to the formation of a tetrahedral intermediate. The regeneration of the carbonyl group will be followed by the release of one part of the peptide, with an amine group at its extremity. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. In the end, the regeneration of the active site will be done with the release of the part of the peptide with a carboxyl extremity. '''The polypeptide is also cut in two parts and the target protein isn't functional anymore'''. <ref>http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png</ref>A schematic representation of the mechanism with the involved amino acids can be found under the following link : [http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png '''mechanism of the reaction''' ]		The '''mechanism''' of the reaction is that the histidine will react with the serine and deprotonate it. The deprotonated hydroxyl group of the serine will act as a nucleophilic species and attack the carbon from the carbonyl function on the peptide. This will lead to the formation of a tetrahedral intermediate. The regeneration of the carbonyl group will be followed by the release of one part of the peptide, with an amine group at its extremity. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. In the end, the regeneration of the active site will be done with the release of the part of the peptide with a carboxyl extremity. '''The polypeptide is also cut in two parts and the target protein isn't functional anymore'''. <ref>http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png</ref>A schematic representation of the mechanism with the involved amino acids can be found under the following link : [http://fr.wikipedia.org/wiki/Fichier:Serine_protease_mechanism_by_snellios.png '''mechanism of the reaction''' ]