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Both compounds are very efficient inactivators of the<jats:italic>Enterobacter cloacae<\/jats:italic>908R \u03b2-lactamase, which is usually resistant to inhibition. Preliminary experiments indicate that various extended-spectrum class C \u03b2-lactamases (ACT-1, CMY-1, and MIR-1) are also inactivated. With the<jats:italic>E. cloacae<\/jats:italic>908R enzyme, complete inactivation occurs with a second-order rate constant,<jats:italic>k<\/jats:italic><jats:sub>2<\/jats:sub>\/<jats:italic>K<\/jats:italic>\u2032, of 2 \u00d7 10<jats:sup>4<\/jats:sup>to 4 \u00d7 10<jats:sup>4<\/jats:sup>M<jats:sup>\u22121<\/jats:sup>s<jats:sup>\u22121<\/jats:sup>, and reactivation is very slow, with a half-life of &gt;1 h. Accordingly, Lek 157 significantly decreases the MIC of ampicillin for<jats:italic>E. cloacae<\/jats:italic>P99, a constitutive class C \u03b2-lactamase overproducer. With the other serine \u03b2-lactamases tested, the covalent adducts exhibit a wide range of stabilities, with half-lives ranging from long (&gt;4 h with the TEM-1 class A enzyme), to medium (10 to 20 min with the OXA-10 class D enzyme), to short (0.2 to 0.4 s with the NmcA class A \u03b2-lactamase). By contrast, both carbapenems behave as good substrates of the<jats:italic>Bacillus cereus<\/jats:italic>metallo-\u03b2-lactamase (class B). The<jats:italic>Streptomyces<\/jats:italic>sp. strain R61 and K15 extracellular<jats:sc>dd<\/jats:sc>-peptidases exhibit low levels of sensitivity to both compounds.<\/jats:p>","DOI":"10.1128\/aac.45.8.2215-2223.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:06:42Z","timestamp":1027764402000},"page":"2215-2223","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["Kinetic Study of Two Novel Enantiomeric Tricyclic \u03b2-Lactams Which Efficiently Inactivate Class C \u03b2-Lactamases"],"prefix":"10.1128","volume":"45","author":[{"given":"Mateja","family":"Vilar","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Biochemistry and Molecular Biology, Institut Jozef Stefan, 1000 Ljubljana,1"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Moreno","family":"Galleni","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Laboratoire d'Enzymologie, Centre for Protein Engineering, University of Lie\u0300ge, Institut de Chimie, B6, B-4000 Liege (Sart Tilman), Belgium,4 and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tom","family":"Solmajer","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Department of Molecular Modelling and NMR Spectroscopy, National Institute of Chemistry, 1115 Ljubljana,2 and"},{"name":"<!--label omitted: 3-->Lek, d. d., Research and Development, 1526 Ljubljana,3 Slovenia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Boris","family":"Turk","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Biochemistry and Molecular Biology, Institut Jozef Stefan, 1000 Ljubljana,1"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Marie","family":"Fre\u0300re","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Laboratoire d'Enzymologie, Centre for Protein Engineering, University of Lie\u0300ge, Institut de Chimie, B6, B-4000 Liege (Sart Tilman), Belgium,4 and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andre\u0301","family":"Matagne","sequence":"additional","affiliation":[{"name":"<!--label omitted: 4-->Laboratoire d'Enzymologie, Centre for Protein Engineering, University of Lie\u0300ge, Institut de Chimie, B6, B-4000 Liege (Sart Tilman), Belgium,4 and"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1042\/bj2700525","article-title":"Chromogenic depsipeptide substrates for \u03b2-lactamases and penicillin-sensitive dd-peptidases.","volume":"270","author":"Adam M.","year":"1990","unstructured":"Adam M. 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