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Results 1 - 10 of 27 > >>
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EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363D177N absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8 721583
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363D177N kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme 721580
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363D205C enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzyme shows changes in activity and the efficacy of immobilization. 722852
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363D374Q kcat/Km for D-glucose 6-phosphate is 7.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 7.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.2fold lower compared to kcat/KM of wild-type enzyme 721584
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363D453C enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited 722852
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363H178N kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme 721580
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363H250N kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme 721580
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363K182Q kcat/Km for D-glucose 6-phosphate is 127fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.4fold lower compared to kcat/KM of wild-type enzyme 721584
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363K182R kcat/Km for D-glucose 6-phosphate is 81fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme 721584
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363K21Q kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 76.2fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 28.5fold lower compared to wild-type value 723718
Results 1 - 10 of 27 > >>
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