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Results 1 - 6 of 6
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63C219A/H157A/R228A inactive 717581
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63D84A the mutation in the lid does not abrogate pilus protein polymerization 717581
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63F86A the mutant shows decreased catalytic efficiency compared to the wild type -, 732709
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63more mutation or deletion of the positively charged domain flanking a transmembrane helix in SrtC abolishes both its retention at single foci and its function in efficient pilus assembly. This positively charged domain can act as a localization retention signal for the focal compartmentalization of membrane proteins 692899
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63Y86A the mutant show an increased Km value compared to the wild type enzyme, the mutation in the lid does not abrogate pilus protein polymerization 717581
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.B63Y92A the mutant shows increased catalytic efficiency compared to the wild type -, 732709
Results 1 - 6 of 6
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