Sandbox Reserved 1091: Difference between revisions

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== Generalities ==

The ASP protein is a serine protease that will cut peptide bonds after specific amino acids. The kexin-like serine protease belongs to the subtilisin family (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site. o

The ''Aeromonas Sobria Serine Protease'' ASP protein is a serine protease that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.

Thos protein is secreted by the Anaerobic bacterium Aeromonas Sobria, which can cause potentially lethal septic shock. Sepsis [http://www.mdsmanuals.com Septic Shock] is

The maturation of ASP is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain a propeptide (such as Kex2) that is involved in the proper folding of the protein.

Sandbox Reserved 1091: Difference between revisions

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@@ Line 6: / Line 6: @@
 == Generalities ==
-The ASP protein is a serine protease that will cut peptide bonds after specific amino acids. The kexin-like serine protease belongs to the subtilisin family (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site. o
+The ''Aeromonas Sobria Serine Protease'' ASP protein is a serine protease that will cut peptide bonds after specific amino acids of a target protein. It preferentially cleaves peptide bonds that follow dibasic amino-acid residues. The kexin-like serine protease belongs to the subtilisin family (subtilases). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>, a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.
+Thos protein is secreted by the Anaerobic bacterium Aeromonas Sobria, which can cause potentially lethal septic shock. Sepsis [http://www.mdsmanuals.com Septic Shock] is
 The maturation of ASP is achieved by ORF2. This protein plays the role of an external chaperone and is necessary for the construction of the stable ASP. Indeed, ASP doesn’t contain a propeptide (such as Kex2) that is involved in the proper folding of the protein.