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Results 1 - 10 of 79 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25A406L the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type -, 736255
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25A406V the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type -, 736255
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D214N the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme -, 489022
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D293A site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D293N site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D294S site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme 685153
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D395A site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme 685153
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25D395N site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25E123Q the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme 726933
Show all pathways known for 2.4.1.25Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.25E129Q the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme 726933
Results 1 - 10 of 79 > >>