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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3C130A FAD binding site, FAD covalently attached 698829
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3H70A FAD binding site, FAD covalently attached 698829
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3H70A/C130A no activity, lack of essential FAD cofactor 698829
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3Y310A larger amount of carbohydrates 698829
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3W351F the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates -, 724616
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3Y300A the mutation doubles kcat values for monosaccharide and oligosaccharide substrates -, 724616
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3Y300N the mutation doubles kcat values for monosaccharide and oligosaccharide substrates -, 724616
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3A38V the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme -, 740204
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3A38V/S388N the mutation increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme 740204
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.B3E247A the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme -, 740204
Results 1 - 10 of 20 > >>