3.4.21.97	A133V	I-site mutant	95603	
3.4.21.97	A134Q	oligomerization at high protein concentration	95600	
3.4.21.97	A143Q	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	
3.4.21.97	A143Q/D217N	the ratio of turnover number to Km-value is 11% of that for mutant enzyme A143Q	653320	
3.4.21.97	A143Q/D227N	the ratio of turnover number to Km-value is 1273fold lower than that for mutant A143Q	653320	
3.4.21.97	A143Q/E31R	the ratio of turnover number to Km-value is 44.6fold lower than that for the wild-typelike mutant A143Q	650227	
3.4.21.97	A143Q/E31S	the ratio of turnover number to Km-value is 4.8fold lower than that for the wild-typelike mutant A143Q	650227	
3.4.21.97	A143Q/H157A	the ratio of turnover number to Km-value is 22fold lower than that of the wild-typelike mutant enzyme A143Q	650071	
3.4.21.97	A143Q/H157E	the ratio of turnover number to Km-value is 11.7fold lower than that of the wild-typelike mutant enzyme A143Q	650071	
3.4.21.97	A143Q/H157Q	the ratio of turnover number to Km-value is 19fold lower than that of the wild-typelike mutant enzyme A143Q	650071