Protein Variants | Comment | Organism |
---|---|---|
F261Y | mutation of the Omega loop, inactive mutant | Leuconostoc mesenteroides |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2 D-alanine | Leuconostoc mesenteroides | - |
ADP + phosphate + D-alanyl-D-alanine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leuconostoc mesenteroides | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2 D-alanine | - |
Leuconostoc mesenteroides | ADP + phosphate + D-alanyl-D-alanine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
D-alanine:D-alanine (D-lactate) ligase (ADP) | - |
Leuconostoc mesenteroides |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Leuconostoc mesenteroides |
General Information | Comment | Organism |
---|---|---|
additional information | 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 | Leuconostoc mesenteroides |