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Results 1 - 10 of 27 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50A67Y 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
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C106A inactive 718275
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C112S site-directed mutagenesis, active site cysteine mutant, forms a noncovalent complex with ubiquitin, crystal structure analysis 731149
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C112S site-directed mutagenesis, the C112S mutant is monomeric, ubiquitin binding crystal structure analysis, overview 731069
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C1651A Plpro active-site mutant -, 670085
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C1651A purified SARS-CoV PLpro protein containing an alanine substitution at putative catalytic residues -, 670084
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C1729A the mutant shows reduced interferon antagonistic activity compared to that of the wild type enzyme 732257
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C1732A encodes a substitution of a cysteine residue, predicted to be critical for zinc binding -, 670084
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50C270A/H332A active site mutant 732827
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B50D165A site-directed mutagenesis, the mutant shows reduced activity in deubiquitination compared to the wild-type enzyme 731069
Results 1 - 10 of 27 > >>