NMR spectrometric assay for determining enzymatic hydrolysis of β-lactam antibiotics with bacteria in aqueous solution [PDF]
FEMS Microbiology Letters, 1984 An application of a nuclear magnetic resonance (NMR) spectrometer for the measurement of β-lactamase activity in clinical material containing bacteria is presented. By means of proton (1H)-NMR, it was easy to measure quantitatively β-lactamase activity in human bacteriuria, without performing any such pretreatment as isolation of bacteria or extraction
Koji O'hara, Yoko Shiomi, Megumi Kono
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BMC Complementary Medicine and Therapies, 2021 Background β-lactam antibiotics are a class of broad-spectrum antibiotics consisting of all antibiotic agents that contain a β-lactam ring in their molecular structures. β-lactam antibiotics are only known to be isolated from fungi (e.g.
Tiffany Turner +3 more
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Non-Canonical Beta-Lactam Antibiotics [PDF]
, 2022 In canonical β-Lactam antibiotics, such as penicillin, the strained nature of the β-Lactam ring leads to acylation of the catalytic serine in the active site of transpeptidases.
Virgin-Downey, Brett Wesley
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Involvement of O8-antigen in altering β-lactam antibiotic susceptibilities inEscherichia coli [PDF]
FEMS Microbiology Letters, 2008 In spite of being dispensable, O-antigens are believed to facilitate various cellular processes and alter antibiotic sensitivities. Escherichia coli K-12 (CS109) strains are lacking in O-antigens and are reported to be sensitive to antibiotics. To our surprise, E. coli 2443 (expressing O8-antigen) manifested two- to fourfold higher sensitivities toward
Sujoy K, Sarkar, Anindya S, Ghosh
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The barrier function of the outer membrane ofPseudomonas maltophiliain the diffusion of saccharides and β-lactam antibiotics [PDF]
FEMS Microbiology Letters, 1989 This paper reports that the efficiency of solute diffusion through the outer membrane of Pseudomonas maltophilia is roughly 3 to 5% of that of Escherichia coli. This is despite the fact that the outer membrane pore(s) is only a little smaller than that of E. coli. These results suggest that P. maltophilia has a low copy number of porin(s).
E, Yamazaki, J, Ishii, K, Sato, T, Nakae
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Characterization of the membrane sensor PenJ for β-lactam antibodies fromBacillus licheniformisby amino acid substitution [PDF]
FEMS Microbiology Letters, 1993 The PenJ protein of the penicillinase gene (penP) expression system from Bacillus licheniformis is an antirepressor and membrane receptor for beta-lactam antibiotics. A putative beta-lactam antibiotic binding site including Ser402 and Lys405, which are homologous to the conserved sequence for the beta-lactam binding site (Ser-X-X-Lys) is present.
M, Takagi, T, Ohta, S, Johki, T, Imanaka
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Commonly prescribed β-lactam antibiotics induce C. trachomatis persistence/stress in culture at physiologically relevant concentrations [PDF]
Frontiers in Cellular and Infection Microbiology, 2014 Chlamydia trachomatis, the most common bacterial sexually transmitted disease agent worldwide, enters a viable, non-dividing and non-infectious state (historically termed persistence and more recently referred to as the chlamydial stress response) when exposed to penicillin G in culture.
Kintner, Jennifer +4 more
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The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]
, 2008 Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page +3 more
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Efficacy of Non-Beta-lactam Antibiotics for Prevention of Cesarean Delivery Surgical Site Infections
American Journal of Perinatology Reports, 2019 Objective To examine the association between perioperative Beta (β))-lactam versus non-β-lactam antibiotics and cesarean delivery surgical site infection (SSI).
Benjamin S. Harris +8 more
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Imide and isatin derivatives as β-lactam mimics of β-lactam antibiotics [PDF]
, 2002 Activated γ-lactams, which are derivatives of succinimide, phthalimide and isatin with suitable elements of molecular recognition, have been synthesised as mimics of the ß-lactam antibiotics and their chemical and biological reactivity ...
Ronald H.B. Galt +10 more
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