4.3.1.2	Q73A	analysis carried out with mutant Q73A. The potential of the mutant Q73A enzyme is shown for application in the asymmetric synthesis of a large variety of valuable N-substituted l-aspartic acids	729599	
4.3.1.2	Q73A	kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 37% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 91:9 (89:11 wild-type)	729745	
4.3.1.2	Q73A	mutant displays significant decrease in ammonia addition and a large increase in methylamine addition compared to wild-type. Mutant displays a wide nucleophile scope including structurally diverse linear and cyclic allkylamines	730442	
4.3.1.2	Q73N	mutant shows very low-level amination activity preventing the measurement of kinetic parameters. Conversion 2h: 18% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)	729745	
4.3.1.2	T360A	kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 38% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 93:7 (89:11 wild-type)	729745	
4.3.1.2	T360S	kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 76% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 86:14 (89:11 wild-type)	729745	
4.3.1.2	Y356A	kcat (mesaconate) decreased compared to wild-type, Km (mesaconate) increased compared to wild-type. Conversion 2h: 24% (73% wild-type), diastereomeric product ratio (threo:erythro) after 2h: 95:5 (89:11 wild-type)	729745