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Results 1 - 6 of 6
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2R70D the mutation does not show an effect on the nonspecific dsDNA binding affinity. The mutations would prevent the tetramerization of the enzyme on nonspecific dsDNA due to the electrostatic repression of their side chains 746460
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2Y68F the mutant enzyme possesses approximately the same base-specific DNA binding ability as the wild-type enzyme but has reduced DNA glycosylase activity. The mutations would prevent the tetramerization of the enzyme on nonspecific dsDNA due to the electrostatic repression of their side chains 746460
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2Y68F/D71R the wild-type enzyme forms a tetramer with nonspecific dsDNA and the tetramerization is prevented by the D71R mutation. The mutations would prevent the tetramerization of the enzyme on nonspecific dsDNA due to the electrostatic repression of their side chains. The Y68F/D71R mutant would also prevent the tetramerization of the enzyme on nonspecific dsDNA due to the steric hindrance of the long side chain of D71R. The DNA glycosylase activity with the 24 bp dsDNA substrate is 74% compared with the mutant enzyme Y68Y (a mutant enzyme that possesses approximately the same base-specific DNA binding ability as the wild-type enzyme but has reduced DNA glycosylase activity). The activity with the 500 bp dsDNA substrate is 34% compared with the mutant enzyme Y68Y. The activity with the 3000 bp dsDNA substrate is 19% compared with the mutant enzyme Y68Y 746460
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2Y68F/R26A the DNA glycosylase activity with the 24 bp dsDNA substrate is 65% compared with the mutant enzyme Y68Y (a mutant enzyme that possesses approximately the same base-specific DNA binding ability as the wild-type enzyme but has reduced DNA glycosylase activity). The activity with the 500 bp dsDNA substrate is 55% compared with the mutant enzyme Y68Y. The activity with the 3000 bp dsDNA substrate is 27% compared with the mutant enzyme Y68Y 746460
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2Y68F/R70D the DNA glycosylase activity with the 24 bp dsDNA substrate is 127% compared with the mutant enzyme Y68Y (a mutant enzyme that possesses approximately the same base-specific DNA binding ability as the wild-type enzyme but has reduced DNA glycosylase activity). The activity with the 500 bp dsDNA substrate is 76% compared with the mutant enzyme Y68Y. The activity with the 3000 bp dsDNA substrate is 19% compared with the mutant enzyme Y68Y 746460
Display the word mapDisplay the reaction diagram Show all sequences 3.1.21.B2Y68F/R70D/D71R the DNA glycosylase activity with the 24 bp dsDNA substrate is 105% compared with the mutant enzyme Y68Y (a mutant enzyme that possesses approximately the same base-specific DNA binding ability as the wild-type enzyme but has reduced DNA glycosylase activity). The activity with the 500 bp dsDNA substrate is 71% compared with the mutant enzyme Y68Y. The activity with the 3000 bp dsDNA substrate is 40% compared with the mutant enzyme Y68Y 746460
Results 1 - 6 of 6