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 3.4.22.B50 D1826A purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues -, 670084 3.4.22.B50 D1901A the mutant almost completely loses interferon antagonistic activity compared to that of the wild type enzyme 732257 3.4.22.B50 E168A site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 E168D site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 E168R site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 H1888A the mutant almost completely loses interferon antagonistic activity compared to that of the wild type enzyme 732257 3.4.22.B50 I353R the mutant exhibits about 40fold reduction in specificity toward ubiquitin compared to the wild type while the activity toward RLRGG-7-amido-4-methylcoumarin is essentially unaltered 732827 3.4.22.B50 I353W the mutant exhibits about 10fold reduction in specificity toward ubiquitin compared to the wild type while the activity toward RLRGG-7-amido-4-methylcoumarin is essentially unaltered 732827 3.4.22.B50 L163Q site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 S32T the mutation enhances the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged 732725 3.4.22.B50 S32T/A67Y the mutations enhance the catalytic efficiency of the enzyme about 8fold while the thermostability of the mutant enzyme remains unchanged 732725 3.4.22.B50 T312A/I313V/I353R mutant lacks deubiquitinase activity, amino acid numbering based on polyprotein -, 755638 3.4.22.B50 T312A/I313V/I353R the mutant shows the greatest decrease in inhibitory activity in the interferon-beta promoter activity assay 732827 3.4.22.B50 T39W mutation enhances hydrolysis of the SARS-CoV-derived peptidyl substrate Dabcyl-FRLKGGAPIKGV-Edans 752517 3.4.22.B50 Y265A site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 Y265F site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069 3.4.22.B50 Y274A site-directed mutagenesis, inactive mutant 731069