Sandbox Reserved 1091: Difference between revisions

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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 65000) is unlike other subtilisin proteases (MW 30000). 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 (EDTA, EGTA, o-phenanthroline) or metalloprotease inhibitors (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>

Sandbox Reserved 1091: Difference between revisions

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Revision as of 10:18, 16 January 2020 view source Amandine Moreno (talk \| contribs) 76 edits No edit summary ← Older edit		Revision as of 10:27, 16 January 2020 view source Amandine Moreno (talk \| contribs) 76 edits No edit summary Newer edit →
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	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 65000) is unlike other subtilisin proteases (MW 30000). 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 65000) is unlike other subtilisin proteases (MW 30000). 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 (EDTA, EGTA, o-phenanthroline) or metalloprotease inhibitors (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>