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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228A202S Km/Vmax for tRNA is 2fold higher than wild-type value 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228A25S Km/Vmax for tRNA is 2.9fold higher than wild-type value 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228A70S Km/Vmax for tRNA is 4fold higher than wild-type value 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228C112A Km/Vmax for tRNA is 7.6fold higher than wild-type value 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228C20S the C20S mutant protein forms a dimer structure even though it is missing the Cys20–Cys20 disulfide bond between its two subunits. Incubation at 85°C for 20 min causes the precipitation of more than half of the C20S protein, while more than 70% of the wild-type enzyme is soluble at that temperature. Methyl-transfer activity of the C20S mutant protein is slightly less than that of the wild-type enzyme at 70°C. Comparison of the CD-spectra of wild-type and C20S proteins reveals that some of the alpha-helices in the C20S mutant protein are less tightly packed than the alpha-helices of the wild-type enzyme at 70°C 712103
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228C301S/C308S/C326S site-directed mutagenesis 758376
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228D119A inactive mutant enzyme 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228D128A inactive mutant enzyme 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228D135A inactive mutant enzyme 712737
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228D169A inactive mutant enzyme 712737
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