title: beta-Lactamase induction and cell wall recycling in gram-negative bacteria.
abstract: beta-Lactams with the ability to induce beta-lactamase in gram-negative bacteria bind to essential penicillin-binding proteins (PBPs) after entering the periplasmic space. This leads to inactivation of transpeptidase activities and thereby a decrease in the number of peptide cross-links, allowing further degradation of murein by soluble lytic transglycosylases. If all DD-carboxypeptidases (PBP 4, 5, 6a and 6b) are inhibited as well, the degradation product aD-pentapeptide (N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic-acid-D-alanyl-D- alanine) accumulates, which is the case with inducing beta-lactams such as imipenem. These molecules in addition to tri- and tetrapeptides (N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic-acid-[D-alanine]) which are the usual degradation products of peptidoglycan, are released into the cytoplasm and displace the UDP-pentapeptide (UDP-N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic-acid-D-alanyl-D-alanine) from the DNA-binding protein AmpR, converting it into an activator of AmpC beta-lactamase expression.
authors.affiliation: Pharmazeutische Mikrobiologie, University of Bonn, Bonn, Germany. B.Wiedemann@uni-bonn.de
authors.forename: B
authors.initials: B
authors.lastname: Wiedemann
authors.forename: D
authors.initials: D
authors.lastname: Pfeifle
authors.forename: I
authors.initials: I
authors.lastname: Wiegand
authors.forename: E
authors.initials: E
authors.lastname: Janas