Sandbox Reserved 1091: Difference between revisions
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== Active site == | == Active site == | ||
'''The catalytic triad:''' The | '''The catalytic triad:''' The 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 <scene name='82/829344/Catalytic_triad/1'>the catalytic triad</scene> will interact together and the mechanism will lead to a cut in the polypeptide. | ||
'''Mechanism:''' 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. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | '''Mechanism:''' 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. Then, a second tetrahedral intermediate will be formed, but with the attack of a deprotonated water molecule. At the end, the regeneration of the active site will be done with the release of the peptide cut in two parts. | ||
