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> | 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 | 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. | ||
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> | 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> | ||
