EC Number   |
Protein Variants |
Reference |
|---|
   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 |
