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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35E277H substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 3%, D-mannose 11%, D-allose 67%, 3-O-methyl-D-glucose 45%, D-galactose 12%, D-xylose 9%, D-lactose 57%, D-maltose 39%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35E277K substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 7%, D-mannose 18%, D-allose 116%, 3-O-methyl-D-glucose 84%, D-galactose 28%, D-xylose 18%, D-lactose 79%, D-maltose 74%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35E277N substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 8%, D-mannose 29%, D-allose 148%, 3-O-methyl-D-glucose 91%, D-galactose 43%, D-xylose 18%, D-lactose 86%, D-maltose 59%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35E277Q substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 10%, D-mannose 31%, D-allose 134%, 3-O-methyl-D-glucose 80%, D-galactose 35%, D-xylose 25%, D-lactose 68%, D-maltose 54%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35E277V substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 8%, D-mannose 29%, D-allose 150%, 3-O-methyl-D-glucose 101%, D-galactose 25%, D-xylose 19%, D-lactose 114%, D-maltose 65%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35I278F substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 4%, D-mannose 14%, D-allose 54%, 3-O-methyl-D-glucose 47%, D-galactose 15%, D-xylose 12%, D-lactose 64%, D-maltose 49%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35more constructed of heterodimeric PQQGDH-B composed of native wild-type and inactive mutant H168Q subunits. The heterodimeric wild-type/H168Q shows slightly decreased GDH activity and almost identical substrate specificity profile to the wild-type enzyme. The Hill coefficient of the heterodimer is calculated as 1.13, indicating positive cooperativity 655929
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35more expression in Pichia pastoris using the Saccharomyces cerevisiae alpha-factor signal sequence for secretion. The productivity of secreted PQQGDH-B achieves 218 kU/liter, i.e. 43 mg/liter. The secreted PQQGDH-B in Pichia pastoris is glycosylated but shows similar enzymatic properties as compared with those of recombinant PQQGDH-B produced in Escherichia coli 655363
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35N279H substrate specificity: D-glucose 100% activity, 2-deoxy-D-glucose 2%, D-mannose 6%, D-allose 49%, 3-O-methyl-D-glucose 50%, D-galactose 13%, D-xylose 8%, D-lactose 64%, D-maltose 61%, respectively 639216
Display the word mapDisplay the reaction diagram Show all sequences 1.1.99.35N428C the catalytic efficiency is increased by 47% compared to the wild type enzyme, the mutant shows increased affinity for pyrroloquinoline quinone and is twice more active toward D-glucose and more selective toward maltose than the wild type 724172
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