Sandbox Reserved 1091: Difference between revisions

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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 ([[1r64]]), a protease of the subtilisin family from Saccharomyces cerevisiae. <ref>PMID:2646633</ref>

This belonging to the '''subtilisin serine proteases family''' is hypothetical. Furthermore the predicted amino acid sequence reinforces this speculation. However, the size of the ASP (MW 65 kDa) is unlike other subtilisin proteases (MW 30 kDa). Also, the amino acid residues composition is different from the family’s characteristics because ASP shows unique cysteine residues that other family members don't show. Therefore we can state that it is likely that ASP belongs to the subtilisin serine proteases family, however it remains unclear.

This belonging to the '''subtilisin serine proteases family''' is hypothetical. Furthermore the predicted amino acid sequence reinforces this speculation. However, the size of the ASP (MW 65 kDa) is unlike other subtilisin proteases (MW 30 kDa). Also, the amino acid residues composition is different from the family’s characteristics because ASP shows unique cysteine residues that other family members don't show. Therefore we can state that it is likely that ASP belongs to the subtilisin serine proteases family, however it remains unclear. Moreover, ASP is the only prokaryotic member of the kexin-subtilisin family that is composed almost exclusively of eukaryotic proteases like Furin.<ref>Siezen RJ & Leunissen JAM (1997) Subtilase: the superfamily of subtilisin-like serine proteases. Protein Sci 6: 501–523.</ref>. ASP was shown not to be a metalloprotease because its activity is not affected by metal chelators ([http://en.wikipedia.org/wiki/Ethylenediaminetetraacetic_acid EDTA], [http://en.wikipedia.org/wiki/EGTA_(chemical) EGTA], [http://en.wikipedia.org/wiki/Phenanthroline o-phenanthroline]) or metalloprotease inhibitors ([http://en.wikipedia.org/wiki/Phosphoramidon phosphoramidon]). <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al. (2017)</ref>

Moreover, ASP is the only prokaryotic member of the kexin-subtilisin family that is composed almost exclusively of eukaryotic proteases like Furin.<ref>Siezen RJ & Leunissen JAM (1997) Subtilase: the superfamily of subtilisin-like serine proteases. Protein Sci 6: 501–523.</ref>

ASP was shown not to be a metalloprotease because its activity is not affected by metal chelators ([http://en.wikipedia.org/wiki/Ethylenediaminetetraacetic_acid EDTA], [http://en.wikipedia.org/wiki/EGTA_(chemical) EGTA], [http://en.wikipedia.org/wiki/Phenanthroline o-phenanthroline]) or metalloprotease inhibitors ([http://en.wikipedia.org/wiki/Phosphoramidon phosphoramidon]). <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al. (2017)</ref>

This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [http://en.m.wikipedia.org/wiki/Septic_shock septic shock]. It 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 multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>

This protein is secreted by the '''Anaerobic bacterium''' [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [http://en.m.wikipedia.org/wiki/Septic_shock septic shock]. It 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 multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>

ASP is a '''[http://en.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunctions like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally, it can cause the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''.

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 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 ([[1r64]]), a protease of the subtilisin family from Saccharomyces cerevisiae. <ref>PMID:2646633</ref>
-This belonging to the '''subtilisin serine proteases family''' is hypothetical. Furthermore the predicted amino acid sequence reinforces this speculation. However, the size of the ASP (MW 65 kDa) is unlike other subtilisin proteases (MW 30 kDa). Also, the amino acid residues composition is different from the family’s characteristics because ASP shows unique cysteine residues that other family members don't show. Therefore we can state that it is likely that ASP belongs to the subtilisin serine proteases family, however it remains unclear.
+This belonging to the '''subtilisin serine proteases family''' is hypothetical. Furthermore the predicted amino acid sequence reinforces this speculation. However, the size of the ASP (MW 65 kDa) is unlike other subtilisin proteases (MW 30 kDa). Also, the amino acid residues composition is different from the family’s characteristics because ASP shows unique cysteine residues that other family members don't show. Therefore we can state that it is likely that ASP belongs to the subtilisin serine proteases family, however it remains unclear. Moreover, ASP is the only prokaryotic member of the kexin-subtilisin family that is composed almost exclusively of eukaryotic proteases like Furin.<ref>Siezen RJ & Leunissen JAM (1997) Subtilase: the superfamily of subtilisin-like serine proteases. Protein Sci 6: 501–523.</ref>. ASP was shown not to be a metalloprotease because its activity is not affected by metal chelators ([http://en.wikipedia.org/wiki/Ethylenediaminetetraacetic_acid EDTA], [http://en.wikipedia.org/wiki/EGTA_(chemical) EGTA], [http://en.wikipedia.org/wiki/Phenanthroline o-phenanthroline]) or metalloprotease inhibitors ([http://en.wikipedia.org/wiki/Phosphoramidon phosphoramidon]). <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al. (2017)</ref>
-Moreover, ASP is the only prokaryotic member of the kexin-subtilisin family that is composed almost exclusively of eukaryotic proteases like Furin.<ref>Siezen RJ & Leunissen JAM (1997) Subtilase: the superfamily of subtilisin-like serine proteases. Protein Sci 6: 501–523.</ref>
-ASP was shown not to be a metalloprotease because its activity is not affected by metal chelators ([http://en.wikipedia.org/wiki/Ethylenediaminetetraacetic_acid EDTA], [http://en.wikipedia.org/wiki/EGTA_(chemical) EGTA], [http://en.wikipedia.org/wiki/Phenanthroline o-phenanthroline]) or metalloprotease inhibitors ([http://en.wikipedia.org/wiki/Phosphoramidon phosphoramidon]). <ref>Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al. (2017)</ref>
-This protein is secreted by the Anaerobic bacterium [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [http://en.m.wikipedia.org/wiki/Septic_shock septic shock]. It 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 multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>
+This protein is secreted by the '''Anaerobic bacterium''' [http://en.m.wikipedia.org/wiki/Aeromonas Aeromonas Sobria], which can cause potentially lethal [http://en.m.wikipedia.org/wiki/Septic_shock septic shock]. It 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 multi visceral failure, including the lungs, kidneys and liver, can be observed. <ref>http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock</ref>
 ASP is a '''[http://en.wikipedia.org/wiki/Sepsis sepsis]-related factor'''. It can cause several dysfunctions like by inducing vascular leakage, reducing blood pressure via the activation of the [http://en.wikipedia.org/wiki/Kinin-kallikreinsystem kinin system] or promoting human plasma coagulation through the activation of [http://fr.m.wikipedia.org/wiki/Prothrombine prothrombin]. Finally, it can cause the formation of pus and edema through the action of anaphylatoxin C5a ([[4p3a]]). Gastroenteritis, and in extreme cases deuteropathy, are the main syndrome caused by infection with ''A.sobria''.