5.1.1.5	A165K/N174L/T391Y	site-directed mutagenesis, the mutant shows no activity towards L-Ala, L-Lys, or L-Arg	-, 728587	
5.1.1.5	additional information	for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. L-lysine is rapidly racemized to give DL-lysine, and L-lysine is selectively catabolized to generate cadaverine by lysine decarboxylase. In order to obtain enantiopure D-lysine, chiral selective degradation of L-lysine from the reaction mixture of DL-lysine is necessary. Under optimal conditions, 750.7 mmol/l D-lysine is finally obtained from 1710 mmol/l L-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. D-lysine yield can reach 48.8% with enantiomeric excess of 99% or more	-, 747470	
5.1.1.5	additional information	in an attempt to limit extracellular Lyr (while retaining the catalytic activity), amino acids 1-36 are removed from the enzyme (LyrM37) and a C-terminal KDEL ER retention motif (LyrM37-KDEL) is added	748654	
5.1.1.5	N174L	site-directed mutagenesis, inactive mutant	-, 728587	
5.1.1.5	R173A	site-directed mutagenesis, inactive mutant	-, 728587	
5.1.1.5	R173K	site-directed mutagenesis, inactive mutant	-, 728587	
5.1.1.5	S394C	site-directed mutagenesis, the mutant shows 1.5fold increased activity with L-arginine compared to the wild-type enzyme	-, 728711	
5.1.1.5	S394N	site-directed mutagenesis, the mutant shows about 2.2fold increased activity with L-arginine compared to the wild-type enzyme	-, 728711	
5.1.1.5	S394T	site-directed mutagenesis, the mutant shows 1.8fold increased activity with L-arginine compared to the wild-type enzyme	-, 728711	
5.1.1.5	S394Y	site-directed mutagenesis, the mutant shows 2.1fold increased activity with L-arginine compared to the wild-type enzyme	-, 728711	
5.1.1.5	T224I	site-directed mutagenesis, the mutant shows significantly decreased activity compared to the wild-type enzyme	727795	
5.1.1.5	T224I/W355Y	site-directed mutagenesis, the double mutant shows significantly decreased activity compared to the wild-type enzyme	727795	
5.1.1.5	T391Y	site-directed mutagenesis, the mutant shows 47% reduced activity with L-lysine compared to the wild-type enzyme	-, 728587	
5.1.1.5	T391Y/S394Y	site-directed mutagenesis,the mutant exhibits significantly reduced specific activity towards L-Lys (6% residual activity) and toward L-Arg (0.9% residual activity)	728587	
5.1.1.5	W355Y	site-directed mutagenesis, the mutant shows significantly decreased activity compared to the wild-type enzyme	727795