188.8.131.52 - D-alanine--D-alanine ligase
- Alanine:alanine ligase (ADP-forming).
- Alanylalanine synthetase.
- D-alanylalanine synthetase.
- D-Ala-D-Ala synthetase.
- D-alanyl-D-alanine synthetase.
ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
There are no Cofactors for this Enzyme
D-alanine--D-alanine ligase (EC:184.108.40.206) is a bacterial enzyme involved in cell-wall biosynthesis. It participates in forming UDP-N-acetylmuramoyl pentapeptide, the peptidoglycan precursor.
This enzyme catalyses the transfer of a phosphate group from ATP to carboxyl oxygen of D-alanine, forming an intermediate, D-alanyl acylphosphate. Then the acyl group is transferred from D-alanyl acylphosphate to the amine group of the second D-alanine substrate, releasing inorganic phosphate.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
There are no kinetic parameters information for this Enzyme
- Structure-guided design and synthesis of ATP-competitive N-acyl-substituted sulfamide d-alanine-d-alanine ligase inhibitors.
- Comparative functional and structural analysis of Pseudomonas aeruginosa d-alanine-d-alanine ligase isoforms as prospective antibiotic targets.
- d-Alanine-d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations.
- Integron gene cassettes harboring novel variants of D-alanine-D-alanine ligase confer high-level resistance to D-cycloserine.
- Insights into the Inhibition of Aeromonas hydrophila d-Alanine-d-Alanine Ligase by Integration of Kinetics and Structural Analysis.
- Integron Gene Cassettes Harboring Novel Variants of D-Alanine-D-Alanine Ligase Confer High-level Resistance to D-Cycloserine
- Digging Deeper to Save the Old Anti-tuberculosis Target: D-Alanine-D-Alanine Ligase With a Novel Inhibitor, IMB-0283.
- Burkholderia pseudomallei d-alanine-d-alanine ligase; detailed characterisation and assessment of a potential antibiotic drug target.
- 1-(2-Hydroxybenzoyl)-thiosemicarbazides are promising antimicrobial agents targeting d-alanine-d-alanine ligase in bacterio.
- Structure of D-alanine-D-alanine ligase from Yersinia pestis: nucleotide phosphate recognition by the serine loop.
- Metabolomics analysis identifies d-Alanine-d-Alanine ligase as the primary lethal target of d-Cycloserine in mycobacteria.