Sandbox Reserved 1091: Difference between revisions

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== Generalities ==

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 ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). 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.

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 ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>[[1R64]], a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.

This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal septic shock. [http://www.mdsmanuals.com Septic Shock] is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multivisceral failure, including the lungs, kidneys and liver, can be observed.

Sandbox Reserved 1091: Difference between revisions

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@@ Line 6: / Line 6: @@
 == Generalities ==
-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 ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). 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.
+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 ([http://en.m.wikipedia.org/wiki/Subtilase Subtilase]). The structure of ASP is similar to that of Kex2 <ref>PMID:2646633</ref>[[1R64]], a protease of the subtilisin family, but ASP has a unique extra occluding region close to its active site.
 This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal septic shock. [http://www.mdsmanuals.com Septic Shock] is a clinical syndrome of potentially fatal organ dysfunction caused by a disorder in the response to infection. In septic shock, there is a critical reduction in tissue perfusion; acute multivisceral failure, including the lungs, kidneys and liver, can be observed.