The second most studied triad is the Cysteine-Histidine-Aspartate motif. Several families of cysteine proteases use this triad set, for example TEV protease and papain. The triad acts similarly to serine protease triads, with a few notable differences. Due to cysteines low pK, the importance of the Asp to catalysis varies and several cysteine proteases are effectively Cys-His dyads (e.g. hepatitis A virus protease), whilst in others the cysteine is already deprotonated before catalysis begins (e.g. papain). This triad is also used by some amidases, such as N'-glycanase to hydrolyse non-peptide C-N bonds.