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Results 1 - 10 of 18 > >>
EC Number General Information Commentary Reference
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4evolution conserved DDL structures consist of three domains: the N-terminal, central and C-terminal domains 743944
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4evolution phylogenetic tree based on the amino acid sequences of D-alanyl-D-alanine ligases (Ddls) in the proteomes of Escherichia coli and ddlR-positive bacteria, overview. DdlR-mediated transcriptional regulation of ddlR and ddl may occur in multiple bacterial systems such as Actinobacteria and Bacillus species -, 744879
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4malfunction inhibition of Ddl prevents bacterial growth 728577
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4metabolism two different metabolic pathways, of DdlA and LysA, respectively, leading to peptidoglycan biosynthesis, overview -, 745827
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more catalytic role of mega-loop, which contains two residues, K259 and Y260, which are crucial in substrate binding 726822
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more comparative molecular modeling approach for SsDdl, enzyme structure homology modeling using the Ddl structure mdoel of Streptococcus mutans (SmDdl) as template, PDB ID 3K3P, overview -, 745681
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more homology structure modeling analyses of wild-type enzyme and mutants S293D and S293E. Both amino acids Arg268 and Ser293 play an important role in the synthesis of D-Ala-D-Ala, residue Ser293 recognizes the carboxylate group of D-Ala2, but is not involved in the ATP hydrolysis, while the Arg268 residue recognizes the carboxylate group of D-Ala1 and is involved in ATP hydrolysis to form the activated acyl-phosphate intermediate. Ligand docking simulations -, 745494
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more NMR ligand binding assay for D-alanine-D-alanine ligase, overview -, 728209
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more Phe261 is a key specificity determinant in the alpha-helical cap of the Omega-loop when folded into the closed conformation, molecular docking, overview. The hydroxyl of Tyr261 plays an instrumental role in determining non-productive docking orientations of dlactate, i.e. D-lactate-OH as an H-bond donor to the Tyr261-OH or D-lactate as an H-bond donor to the phosphoryl of the intermediate D-alanyl phosphate, and the D-lactate-COO- as an H-bond acceptor for the Tyr261-OH. Arg301 is required for the activation of the nucleophilic D-lactate for D-Ala-D-lactate formation. Ligand binding docking structure study, involving also the transition-state analogue, overview 728168
Show all pathways known for 6.3.2.4Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.4more substrate-binding mechanism of enzyme YpDDL involving conformational changes of the loops, structure-function relationship analysis of the enzyme, overview 743944
Results 1 - 10 of 18 > >>