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Results 1 - 10 of 30 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A133V I-site mutant 95603
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A134Q oligomerization at high protein concentration 95600
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q all enzyme samples used in this experiments contain an additional mutation, A143Q. The mutation disables one of the internal cleavage sites but has little effects on the kinetic properties of the enzyme 653320
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/D217N the ratio of turnover number to Km-value is 11% of that for mutant enzyme A143Q 653320
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/D227N the ratio of turnover number to Km-value is 1273fold lower than that for mutant A143Q 653320
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/E31R the ratio of turnover number to Km-value is 44.6fold lower than that for the wild-typelike mutant A143Q 650227
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/E31S the ratio of turnover number to Km-value is 4.8fold lower than that for the wild-typelike mutant A143Q 650227
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/H157A the ratio of turnover number to Km-value is 22fold lower than that of the wild-typelike mutant enzyme A143Q 650071
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/H157E the ratio of turnover number to Km-value is 11.7fold lower than that of the wild-typelike mutant enzyme A143Q 650071
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.97A143Q/H157Q the ratio of turnover number to Km-value is 19fold lower than that of the wild-typelike mutant enzyme A143Q 650071
Results 1 - 10 of 30 > >>