Cysteine proteases are remarkably similar to serine proteases (like chymotrypsin), except they have a cysteine in their active site rather than a serine. Using the mechanism that we discussed for serine proteases, draw a corresponding mechanism for a cysteine protease cleaving the bond between an alanine-glycine dipeptide. Note that cysteine proteases do not require an aspartate in their active site. Also note that the cysteine is usually in its thiolate form (deprotonated) and the histidine is in its imidazolium form (fully protonated) in the resting state of the enzyme.

Biochemistry
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Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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Cysteine proteases are enzymes that degrade proteins. You may have heard of some examples of these types of proteins before! Bromelain is an enzyme found in pineapple that is commonly used as a meat tenderizer and is the reason Jell-O with fresh pineapple will not solidify. Cysteine proteases are remarkably similar to serine proteases (like chymotrypsin), except they have a cysteine in their active site rather than a serine. Using the mechanism that we discussed for serine proteases, draw a corresponding mechanism for a cysteine protease cleaving the bond between an alanine-glycine dipeptide. Note that cysteine proteases do not require an aspartate in their active site. Also note that the cysteine is usually in its thiolate form (deprotonated) and the histidine is in its imidazolium form (fully protonated) in the resting state of the enzyme. 

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