923-16-0

White to off-white powder

D-Ala-D-Ala is a bacterial endogenous metabolite. D-Ala-D-Ala constitutes the terminus of the peptide part of the peptidoglycan monomer unit and is involved in the transpeptidation reaction as the substrate. D-Ala-D-Ala is catalyzed by D-Alanine-D-Alanine ligase[1][2][3].

ChEBI: D-alanyl-D-alanine is a dipeptide comprising D-alanine with a D-alanyl residue attached to the alpha-nitrogen. It is a component of bacterial peptidoglycan and forms an important target for development of antibacterial drugs. It has a role as an Escherichia coli metabolite. It is a tautomer of a D-alanyl-D-alanine zwitterion.

D-Ala-D-Ala is found in the stem termini of peptidoglycan side-chain pentapeptide found in the cell walls of gram positive bacteria. The D-ala-d-ala stem termini is the site of interaction of glycopeptide antibiotics such as vancomycin and teicoplanin. D-ala-D-ala is a substrate used to study kinetics of UDPMurNAc-tripeptide D-alanyl-D-alanine-adding (ligase) enzyme.''D-Ala-D-Alaa terminus moiety of bacterial peptidoglycansis used for affinity chromatography and binding mechanism studies of antibiotics such as teicoplaninristocetinvancomycin.

Microbial Metabolite

[1] Kitamura Y, et al. Structure of D-alanine-D-alanine ligase from Thermus thermophilus HB8: cumulative conformational change and enzyme-ligand interactions. Acta Crystallogr D Biol Crystallogr. 2009 Oct;65(Pt 10):1098-106. DOI:10.1107/S0907444909029710
[2] Tytgat I, et al. DD-ligases as a potential target for antibiotics: past, present and future. Curr Med Chem. 2009;16(20):2566-80. DOI:10.2174/092986709788682029
[3] Trivedi RR, et al. Mechanical Genomic Studies Reveal the Role of d-Alanine Metabolism in Pseudomonas aeruginosa Cell Stiffness. mBio. 2018 Sep 11;9(5):e01340-18. DOI:10.1128/mBio.01340-18