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EC Number Protein Variants Commentary Reference
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.B3C130A FAD binding site, FAD covalently attached 698829
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
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.B3Q353A the mutation decreases 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.B3Q353N the mutation decreases 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.B3Q384A the mutation decreases 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.B3Q384N the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme 740204
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