Sandbox Reserved 1091: Difference between revisions
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The ASP protein is a serine protease of the subtilisin family and it will cut peptide bonds after specific amino acids. | The ASP protein is a serine protease of the subtilisin family and it will cut peptide bonds after specific amino acids. | ||
The kexin-like serine protease, belonging to the subtilisin family (subtilases) too. The overall structure of ASP is similar to that of Kex2, but it has a unique extra occluding region close to its active site. | |||
== Secondary structure == | == Secondary structure == | ||
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== Active site == | == Active site == | ||
The catalytic triad of ASP is composed of Asp78, His115 and Ser336. These amino acids are the base is the active site of the protein, where the mode of action of the serine protease takes place. | The catalytic triad of ASP is composed of <font color='red'>Asp78</font>, <font color='red'>His115</font> and <font color='red'>Ser336</font>. 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. | ||
