Protease Cleavage: N-terminal or C-terminal of S102?

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The discussion centers on the specificity of endoproteases and their cleavage mechanisms, particularly regarding whether cleavage occurs N-terminally or C-terminally of a specified residue, such as S102. The key question is whether the residue at which the enzyme cleaves is retained in the modified protein or lost with the cleaved portion. The provided links to NEB products and PubMed articles may offer insights into the cleavage patterns and mechanisms of specific endoproteases, but the original query highlights a lack of clarity in existing literature regarding this aspect of protease function. Understanding this cleavage specificity is crucial for applications in protein engineering and analysis.
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If an endoprotease is known to cleave "at" a particular residue - for instance "at" S102 - does it cleave N-terminally or C-terminally of S102? In other words, is the residue which the enzyme cleaves "at" retained in the modified protein or lost along with the 'waste'?

Thanks for any help.
 
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