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Results 1 - 9 of 9
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5G392F mutant does not display measurable activity 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5I427A mutant is significantly more efficient with 2,6-dimethoxy-4-allylphenol than wild-type 762539
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5I427T mutant does not display measurable activity 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5L381W mutant does not display measurable activity 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5L438C variant displays lowered activity towards all substrates as compared to wild-type 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5M282L substrate specificity profile is similar to wild-type 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5more exchange of a loop at the dimer-dimer interface in octameric vanillin oxidase that is not present in dimeric EUGO. A vanillin oxidase variant where the loop was deleted, loopless VAO, exclusively forms dimers. Introduction of the loop into EUGO is not sufficient to induce its octamerization. Neither variant displays major changes in its catalytic properties as compared to the wild-type enzyme 763012
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5Q425T display similar activity to the wild-type enzyme with vanillyl alcohol, but no measurable activity towards any other substrate 763480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.B5V436I variant displays lowered activity towards vanillyl alcohol and eugenol 763480
Results 1 - 9 of 9