In other parasites, cysteine proteases can be trans-activated by their mature enzymes and asparaginyl endopeptidase, a clan CD cysteine protease that cleaves C-terminal to asparginyl (Asn) residues (Dalton and Brindley, 1996).

What do cysteine proteases cleave?

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. ... Cysteine proteases are used as an ingredient in meat tenderizers.

What role does cysteine play in catalysis?

Cysteine proteases (also known as thiol proteases) catalyze the breakdown of proteins by cleaving peptide bonds using a nucleophilic thiol from a cysteine (Figure 4.63). The cysteine is typically found in a catalytic dyad or triad also involving histidine and (sometimes) aspartic acid (very much like serine proteases).