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Results 1 - 10 of 10
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82D258A 9% of wild-type kcat for 3-phosphonopyruvate 659267
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82D260A 0.1% of wild-type kcat for 3-phosphonopyruvate 659267
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82D297E catalytic turnover rate is 1.5fold less and Km is increased about 13fold compared to the wild type enzyme 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82D297N catalytic turnover rate of D297N is 2fold lower and Km is increased 940fold compared to the wild type enzyme -, 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82E213A 5% of wild-type kcat for 3-phosphonopyruvate 659267
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82G94A compared to wild type PPDC, Km is increased only 2fold, while kcat is 4fold lower -, 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82H110A no detectable activity -, 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82H111A the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme -, 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82S25D catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme -, 705200
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.82S25N catalytic turnover rate is 1.5fold less and Km is increased 80fold compared to the wild type enzyme 705200
Results 1 - 10 of 10