666728-52-5

Upstream product

• 129172-14-1 methyl 2-acetamido-4,6-O-benzylidene-3-O-((R)-1'-carboxyethyl)-2-deoxy-β-D-glucopyranoside 
• 3946-01-8 methyl N-acetyl-β-D-glucosaminide 
• 87038-18-4 methyl 2-acetylamido-4,6-O-benzylidene-2-deoxy-β-D-glucopyranoside 
• 666728-50-3 (R)-2-((2R,4aR,6R,7R,8R,8aS)-7-Acetylamino-6-methoxy-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-8-yloxy)-propionic acid 4-nitro-phenyl ester 
• 10378-06-0 2-methyl-(3,4,6-tri-O-acetyl-1,2-dideoxy-α-D-glucopyranoso)[1,2-d]-2-oxazoline 
• 2771-48-4 methyl 2-acetamido-3,4,6-O-triacetyl-2-deoxy-β-D-glucopyranoside 

Relevant academic research and scientific papers

Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria

The major constituent of the bacterial cell wall, peptidoglycan, is comprised of repeating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide. Penicillin-binding proteins (PBPs) are involved in the final stages of bacterial cell wall assembly. Two activities for PBPs are the cross-linking of the cell wall, carried out by DD-transpeptidases, and the DD-peptidase activity, that removes the terminal D-Ala residue from peptidoglycan. The DD-peptidase activity moderates the extent of the cell wall cross-linking. There exists a balance between the two activities that is critical for the well-being of bacterial cells. We have cloned and purified PBP5 of Escherichia coli. The membrane anchor of this protein was removed, and the enzyme was obtained as a soluble protein. Two fragments of the polymeric cell wall of Gram-negative bacteria (compounds 5 and 6) were synthesized. These molecules served as substrates for PBP5. The products of the reactions of PBP5 and compounds 5 and 6 were isolated and were shown to be D-Ala and the fragments of the substrates minus the terminal D-Ala. The kinetic parameters for these enzymic reactions were evaluated. PBP5 would appear to have the potential for turnover of as many as 1.4 million peptidoglycan strands within a single doubling time (i.e., generation) of E. coli.