6.1.2.1	F261Y	the mutant shows a complete loss of the ability to make D-alanyl-(R)-lactate	728168	
6.1.2.1	additional information	construction of several mutant strains, generating a Bacillus subtilis strain BP341A expressing a depsipeptide-containing (D-Ala-D-Lac) lipid II, phenotype, overview. Strains BP341A-E, that require expression of the VanB-type operon for growth, have mutations in the endogenous Ddl ligase	-, 716269	
6.1.2.1	additional information	structure-based modification of D-alanine-D-alanine ligase from strain ATCC 43589 for depsipeptide synthesis, overview	714541	
6.1.2.1	Q260K/A283E	the two amino acid substitutions result from point mutations at nucleotide positions 778 and 848, respectively. The mutant enzyme VRSA-9 synthesizes precursors ending in D-Ala-D-Lac (72%) and D-Ala-D-Ala (21%) in the absence of vancomycin. VRSA-9 Ddl shows a 200fold loss of activity and the importance of conformational changes in the dimer interface which can indirectly affect the topology of the active site	-, 715371	
6.1.2.1	S137A	site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate	714541	
6.1.2.1	S137A/Y207F	site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate	714541	
6.1.2.1	S137F/Y207F	site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate	714541	
6.1.2.1	S137G/Y207F	site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate	714541	
6.1.2.1	S137T/Y207F	site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate	714541	
6.1.2.1	S150A	mutant of D-Ala-D-Ala ligase Ddl, mutant has gained depsipeptide ligase activity, i.e. formation of D-Ala-D-Lac, D-Ala-D-hydroxybutyrate, with dipeptide/depsipeptide partition ratios that mimic the pH behaviour of D-Ala-D-lactate ligase VanA. Mutant displays a clear pH-dependent partitioning between the preferred depsipeptide product at low pH and the dipeptide product at high pH	707464