{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,6,21]],"date-time":"2022-06-21T15:18:39Z","timestamp":1655824719129},"reference-count":12,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2014,10,1]],"date-time":"2014-10-01T00:00:00Z","timestamp":1412121600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2014,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149\n            <jats:sup>H240<\/jats:sup>\n            , and TEM-149\n            <jats:sup>H164-H240<\/jats:sup>\n            versus a large panel of inhibitors\/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149\n            <jats:sup>H240<\/jats:sup>\n            , and TEM-149\n            <jats:sup>H164-H240<\/jats:sup>\n            \u03b2-lactamases, and the\n            <jats:italic>\n              K\n              <jats:sub>i<\/jats:sub>\n            <\/jats:italic>\n            (inhibition constant),\n            <jats:italic>K<\/jats:italic>\n            (dissociation constant of the Henri-Michaelis complex),\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>+2<\/jats:sub>\n            and\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>+3<\/jats:sub>\n            (first-order acylation and deacylation constants, respectively), and\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>+2<\/jats:sub>\n            \/\n            <jats:italic>K<\/jats:italic>\n            values were calculated.\n          <\/jats:p>","DOI":"10.1128\/aac.02950-14","type":"journal-article","created":{"date-parts":[[2014,8,5]],"date-time":"2014-08-05T03:35:46Z","timestamp":1407209746000},"page":"6294-6296","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Kinetic Study of the Effect of Histidines 240 and 164 on TEM-149 Enzyme Probed by \u03b2-Lactam Inhibitors"],"prefix":"10.1128","volume":"58","author":[{"given":"Mariagrazia","family":"Perilli","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Universit\u00e0 degli Studi dell'Aquila, L'Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alisia","family":"Mancini","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Universit\u00e0 degli Studi dell'Aquila, L'Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giuseppe","family":"Celenza","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Universit\u00e0 degli Studi dell'Aquila, L'Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlo","family":"Bottoni","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Universit\u00e0 degli Studi dell'Aquila, L'Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pierangelo","family":"Bellio","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Universit\u00e0 degli Studi dell'Aquila, L'Aquila, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessia","family":"Sabatini","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, 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Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0966-842X(98)01317-1"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2010.10.008"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.01028-07"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.01268-12"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-2952(87)90609-5"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.38.7.1608"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.1.227"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.33.8.1160"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/0732-8893(90)90083-8"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2010.00222.x"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dkm275"},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1042\/bj3030825","article-title":"Kinetic 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