Sandbox Reserved 1091: Difference between revisions
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== Active site == | == Active site == | ||
<b> The catalytic triade: </b> The catalytic triad of ASP is composed of <b>Asp78</b>, <b>His115</b> and <b>Ser336</b>. These amino acids are the base is the active site of the protein, where the mode of action of the serine protease takes place. | <b> The catalytic triade: </b> The [https://en.wikipedia.org/wiki/catalytic triad] of ASP is composed of <b>Asp78</b>, <b>His115</b> and <b>Ser336</b>. These amino acids are the base is the active site of the protein, where the mode of action of the serine protease takes place. | ||
A peptide can be inserted in the space of the active site. There, the amino acids of the catalytic triad will interact together and the mechanism will lead to a cut in the polypeptide. | A peptide can be inserted in the space of the active site. There, the amino acids of the catalytic triad will interact together and the mechanism will lead to a cut in the polypeptide. | ||
<b> Mechanism: </b>The mechanism is the following: 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. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | <b> Mechanism: </b>The mechanism is the following: 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. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | ||
https://upload.wikimedia.org/wikipedia/commons/1/17/Serine_protease_mechanism_by_snellios.png | |||
== Disease == | == Disease == | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
