1.4.1.16	A69R	mutation to the correspondung residue of Symbiobacteium thermophilum DAPDH. Mutation improves the catalytic efficiencies toward 2-keto acids and does not affect the catalytic efficiency toward meso-DAP	-, 762982	
1.4.1.16	F146W	site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates	724026	
1.4.1.16	F146W/M152Q	site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates	724026	
1.4.1.16	H227C	site-directed saturation mutagenesis, the mutant shows 15.1fold increased activity with phenylpyruvate compared to the wild-type enzyme	724034	
1.4.1.16	H227I	mutant accepts substrates D-2-phenylglycine and D-homophenylalanine	762879	
1.4.1.16	H227V	mutant shows high activity toward phenylpyruvic acid and 2-oxo-4-phenylbutyric acid	762879	
1.4.1.16	H227V	site-directed saturation mutagenesis, the mutant shows 35.1fold increased activity with phenylpyruvate compared to the wild-type enzyme	724034	
1.4.1.16	K159R	mutation decreases the kcat/KM value with meso-DAP, the catalytic efficiency toward pyruvic acid increases by 24%	763313	
1.4.1.16	M152A	the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme	742276	
1.4.1.16	M152D	inactive	742276