50604-68-7Relevant academic research and scientific papers
Total synthesis of n-acetylglucosamine-1,6-anhydro-n- acetylmuramylpentapeptide and evaluation of its turnover by ampd from escherichia coli
Hesek, Dusan,Lee, Mijoon,Zhang, Weilie,Noll, Bruce C.,Mobashery, Shahriar
supporting information; experimental part, p. 5187 - 5193 (2009/09/30)
The bacterial cell wall is recycled extensively during the course of cell growth. The first recycling event involves the catalytic action of thelytic transglycosylase enzymes, which produce an uncommon 1,6-anhydropy ranose moiety during separation of the muramyl residues from the peptidoglycan, the major constituent of the cell wall. This product, an N-acetyl-β-D-glucosamine- (1→4)-1,6-anhydro-N-acetyl-β-Dmuramylpeptide, is either internalized to initiate the recycling process or diffuses into the milieu to cause stimulation of the pro-inflammatory responses by the host. We report the total syntheses of N-acetyl-β-Dglucosamine-( 1→4)-1,6-anhydro-N-acetyl- β-D-muramyl-L-Ala-γ-D-Glu-meso-DAP-D-Ala-D-Ala (compound 1, the product of lytic transglycosylase action on the cell wall of Gram-negative bacteria) and N-acetyl-β-Dglucosamine-( 1→4)-1,6-anhydro-N-acetyl- β-D-muramyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala (compound 2, from lytic transglycosylase action on the cell wall of Gram-positive bacteria). The syntheses were accomplished in 15 linear steps. Compound 1 is shown to be a substrate of the AmpD enzyme of the Gram-negative bacterium Escherichia coli, anenzyme that removes the peptide from the disaccharide scaffold in the e arly cytoplasmic phase of cell wall turnover.
