Could an enzyme be sensitive to sulfhydryl specific inhibitors on account of cysteine(s) away from the catalytic pocket?
Certainly yes! Catalytic cysteines are those involved in the active sites of cysteine proteases. Most of the cysteine residues in proteins maintain protein conformation or structure, coordinate metals regulate protein function. Only a few are involved in direct catalysis. Please see the attached documents.
The enzymes are also sensitive to sulfhydryl specific inhibitors if the cysteine residue in the vicinity of the active site is effected.
Nitin Kulhar
What is the importance of your question? I would appreciate if you elaborate it bit more !!
Amino acid Cysteine is attached with sulfhydryl group which provide the catalytic activity for an enzymatic action.
Cysteine is used in human body to produce glutathione and taurine, also glucose sometimes as source of energy. It plays important role in the communication between immune system cells.
Please check the links below:
Article The Role of Thiols and Disulfides on Protein Stability
https://academic.oup.com/toxsci/article/94/2/240/1644737
If the inhibitor interacts with Cys residues away from the active site, it may cause a conformational change that affects substrate binding, and in this case you will observe inhibition.
Stephanie Misquitta
As per your answer ......
so that means the appropriate signals on the immune cells stop to transfer to the other one. Hence, it can cause immune system impairment !!
Anju, I didn't quite understand your comment. Let me clarify that we are discussing the cysteine residues present in enzymes, and not free cysteine (which is used in glutathione).
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