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Results 1 - 10 of 65 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23A288V naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1, activity, substrate specificity and kinetics compared to the wild-type enzyme, overview 708484
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23D322N naturally occuring polymorphism, the mutant is 2.3fold more specific for the correct opposite base than the wild-type enzyme, activity, substrate specificity and kinetics compared to the wild-type enzyme 708484
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E131R loss of activity 750392
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E173Q no enzymic activity, E173 may play a crucial role in forming the active site pocket 667594
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E2Q no enzymic activity, interactions with G167 and Y170 are interupted 667594
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E3Q crystallization data 680361
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E3Q inactive. Mutant binds DNA duplexes containing spiroiminodihydantoin or guanidinohydantoin about 1000fold more tightly over corresponding duplexes containing 8-oxoguanine 678318
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23E77S in wild-type, 8-oxoguanine is bound via E77 in syn conformation. In mutant E77S, which reflects the sequence of the Escherichia coli enzyme, 8-oxoguanine is preferentially bound in the anti conformation 678139
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23F110A the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps 710030
Display the word mapDisplay the reaction diagram Show all sequences 3.2.2.23F110W the mutation affects the enzyme activity, especially in the case of oxoG/C substrate, in the second and third reaction steps 710030
Results 1 - 10 of 65 > >>