{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T18:41:44Z","timestamp":1791312104689,"version":"4.3.1"},"reference-count":175,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2015,4,29]],"date-time":"2015-04-29T00:00:00Z","timestamp":1430265600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the National Research Laboratory Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science, ICT and Future Planning","award":["2011-0027928"],"award-info":[{"award-number":["2011-0027928"]}]},{"name":"the Next Generation BioGreen 21 Program of Rural Development Administration in Republic of Korea","award":["PJ01103102"],"award-info":[{"award-number":["PJ01103102"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Carbapenems (imipenem, meropenem, biapenem, ertapenem, and doripenem)  are \u03b2-lactam antimicrobial agents. Because carbapenems have the broadest spectra among all \u03b2-lactams and are primarily used to treat infections by multi-resistant Gram-negative bacteria, the emergence and spread of carbapenemases became a major public health concern. Carbapenemases are the most versatile family of \u03b2-lactamases that are able to hydrolyze carbapenems and many other \u03b2-lactams. According to the dependency of divalent cations for enzyme activation, carbapenemases can be divided into metallo-carbapenemases  (zinc-dependent class B) and non-metallo-carbapenemases (zinc-independent classes  A, C, and D). Many studies have provided various carbapenemase structures. Here  we present a comprehensive and systematic review of three-dimensional structures of  carbapenemase-carbapenem complexes as well as those of carbapenemases. We update recent studies in understanding the enzymatic mechanism of each class of carbapenemase, and summarize structural insights about regions and residues that are important in acquiring the carbapenemase activity.<\/jats:p>","DOI":"10.3390\/ijms16059654","type":"journal-article","created":{"date-parts":[[2015,4,29]],"date-time":"2015-04-29T11:02:35Z","timestamp":1430305355000},"page":"9654-9692","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":162,"title":["Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance"],"prefix":"10.3390","volume":"16","author":[{"given":"Jeong","family":"Jeon","sequence":"first","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jung","family":"Lee","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jae","family":"Lee","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kwang","family":"Park","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asad","family":"Karim","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chang-Ro","family":"Lee","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byeong","family":"Jeong","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5660-7122","authenticated-orcid":false,"given":"Sang","family":"Lee","sequence":"additional","affiliation":[{"name":"National Leading Research Laboratory of Drug Resistance Proteomics,  Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin,  Gyeonggido 449-728, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2015,4,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The structure of \u03b2-lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Philos. 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