3.4.22.B50	A67Y	the mutation enhances the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged. The specific activity against azo-casein is almost 2.4 times higher than wild type	732725	
3.4.22.B50	C106A	inactive	718275	
3.4.22.B50	C112S	site-directed mutagenesis, active site cysteine mutant, forms a noncovalent complex with ubiquitin, crystal structure analysis	731149	
3.4.22.B50	C112S	site-directed mutagenesis, the C112S mutant is monomeric, ubiquitin binding crystal structure analysis, overview	731069	
3.4.22.B50	C1651A	Plpro active-site mutant	-, 670085	
3.4.22.B50	C1651A	purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues	-, 670084	
3.4.22.B50	C1729A	the mutant shows reduced interferon antagonistic activity compared to that of the wild type enzyme	732257	
3.4.22.B50	C1732A	encodes a substitution of a cysteine residue, predicted to be critical for zinc binding	-, 670084	
3.4.22.B50	C270A/H332A	active site mutant	732827	
3.4.22.B50	D165A	site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme	731069