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Literature summary for 6.3.2.4 extracted from

  • Neuhaus, F.C.
    Role of the omega loop in specificity determination in subsite 2 of the D-alanine:D-alanine (D-lactate) ligase from Leuconostoc mesenteroides: a molecular docking study (2011), J. Mol. Graph. Model., 30, 31-37.
    View publication on PubMed
Search for more literature for 6.3.2.4

Protein Variants

Protein Variants Comment Organism
F261Y mutation of the Omega loop, inactive mutant Leuconostoc mesenteroides

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2 D-alanine
-
 Leuconostoc mesenteroides ADP + phosphate + D-alanyl-D-alanine
-
 ?

Synonyms

Synonyms Comment Organism
D-alanine:D-alanine (D-lactate) ligase (ADP)
-
 Leuconostoc mesenteroides

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Leuconostoc mesenteroides

General Information

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