Proteases and Glycosidases: Specificity and Substrate Diversity?

  • Thread starter Monique
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In summary, glycosidases and proteases are enzymes that break down substances in the body. Glycosidases are specific to sugars while proteases are more general and can break down proteins. Lysosomal storage disease is mainly caused by deficiencies in glycosidase enzymes, not proteases. This is because glycosidases work on one enzyme-one substrate basis, while proteases can still function with the presence of other proteases. However, proteases can also be specific depending on the amino acid side chains in the peptide.
  • #1
Monique
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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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  • #2
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 [Broken]
http://cancerweb.ncl.ac.uk/cgi-bin/omd?query=protease [Broken]
 
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  • #3
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?
 
  • #4
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:
 

1. What are proteases and glycosidases?

Proteases and glycosidases are enzymes that are responsible for breaking down proteins and carbohydrates, respectively. They play an important role in digestion, as well as in various cellular processes.

2. How do proteases and glycosidases work?

Proteases and glycosidases work by breaking the chemical bonds between amino acids in proteins and between monosaccharides in carbohydrates, respectively. This process is known as hydrolysis, where water molecules are used to break the bonds.

3. What are the different types of proteases and glycosidases?

There are many different types of proteases and glycosidases, each with their own specific functions and targets. Some common types include serine proteases, cysteine proteases, and aspartic proteases. Glycosidases can be classified into different families based on their specific target carbohydrates, such as alpha-amylases and beta-glucosidases.

4. Where are proteases and glycosidases found?

Proteases and glycosidases are found in various organisms, including plants, animals, and microorganisms. They can be found in the digestive system, as well as in other tissues and organs. Some are also used in industrial processes, such as food production and pharmaceuticals.

5. What are the applications of proteases and glycosidases?

Proteases and glycosidases have a wide range of applications in various industries. They are commonly used in food production to improve digestion and enhance flavor. In medicine, they are used as therapeutic agents for diseases caused by protein or carbohydrate abnormalities. They are also important tools in biotechnology and research, allowing for the manipulation and study of proteins and carbohydrates.

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