Characterization of a β-N-acetylglucosaminidase ofEscherichia coli and Elucidation of Its Role in Muropeptide Recycling and β-Lactamase Induction*

By W. Vötsch, M. Templin. Journal of Biological Chemistry, 2000

128 citations recorded by the source corpus.

Using the known mapping position the gene encoding a β-1,4-N-acetylglucosaminidase needed for the degradation of muropeptides could be identified. nagZencodes a cytosolic enzyme active onN-actylglucosamyl-β-1,4-(1,6)-anhydromuramic acid containing muropeptides. These degradation products of the peptidoglycan are formed during the enlargement of the murein sacculus as a consequence of a growth mechanism, which couples the controlled degradation of the cell wall polymer with the insertion of new material. NagZ is needed for the formation of monosaccharides from the released disaccharides during the cytosolic steps of the muropeptide-recycling pathway. The formation of intracellular 1,6-anhydro-N-acetylmuramyl-peptides is important for the expression control of the inducible β-lactamases of the AmpC type. A mutant lacking active NagZ cannot establish AmpC mediated β-lactam resistance. The biochemical characterization of the enzyme showed its activity on different muropeptides and inhibitors of enzyme activity could be identified. This observation might be important for designing inhibitors of NagZ that could prevent the establishment of β-lactam resistance of Enterobacteria possessing inducible β-lactamases.

Subfields: Biotechnology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/b60fc6f6d0b57e7be79085779ef098505f3dd1eb

Citations in the corpus

• Peptidoglycan Hydrolases of Escherichia coli (2011, unknown): “Later, the encoding nagZ gene was identified (37), and an overproduced recombinant form was purified (298).”