2.6.1.5	C151Y	missense mutation leading to defective folding and likely alteration of the enzymatic activity	676025	
2.6.1.5	I249A	reduced catalytic activity	673540	
2.6.1.5	L273P	missense mutation leading to defective folding and likely alteration of the enzymatic activity	676025	
2.6.1.5	additional information	switch of aspartate aminotransferase to use of tyrosine substrate by introduction of six mutations obtained by rational design and termed HEX plus mutation A293D or mutation I73V	660463	
2.6.1.5	N17S	increase in Km-values, substantial decrease in kcat-values	660454	
2.6.1.5	N54S	reduced enzymic activity	660454	
2.6.1.5	R20A	increase in Km-values, substantial decrease in kcat-values	660454	
2.6.1.5	R315K	retains enzymic activity	660454	
2.6.1.5	R417Q	no enzymic activity	660454	
2.6.1.5	R41A	mutant is inactive when tested with (S)-beta-phenylalanine as amino donor and 2-oxoglutarate	 as amino acceptor	721359