Proteases and Glycosidases: Specificity and Substrate Diversity?

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Proteases and glycosidases differ significantly in their substrate specificity and function. Glycosidases are primarily involved in the degradation of sugars and exhibit high specificity, often acting on one substrate. In contrast, proteases break down proteins and can have a broader spectrum of activity, potentially compensating for deficiencies in specific proteases. This distinction is particularly relevant in the context of lysosomal storage diseases, which are mainly caused by deficiencies in glycosidase enzymes rather than proteases. The discussion highlights the importance of enzyme specificity in the context of metabolic disorders.
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I guess proteases have a very broad spectrum of substrates while glycosidases are very specific? Is that correct?
 
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Well according to my sources, a glycosidase is active in the degredation of sugars, while proteases break down proteins.

http://cancerweb.ncl.ac.uk/cgi-bin/omd?query=glycosidase
http://cancerweb.ncl.ac.uk/cgi-bin/omd?query=protease
 
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You are right, but what I was getting at is that lysosomal storage disease are mainly caused by deficiencies in glycosidase enzymes and not proteases. I thought that the reason for that would be that glycosidases work 1 enzyme 1 substrate, while proteases are more generally active. If you are deficient in a proteases, other proteases would still be able to digest the accumulating substrate. I guess?
 
Sorry,

I totally misread your question there.:frown:
I am not familiar with the lysosomal storage disease or glycosidases so much either, but I do know that proteases contain the potential to be quite specific based on the amino acid side chains that are contained within the peptide. Don't know if that helps at all, but hopefully it does.:smile:
 
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