{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,4,20]],"date-time":"2025-04-20T07:01:30Z","timestamp":1745132490091},"reference-count":30,"publisher":"Springer Science and Business Media LLC","issue":"12","license":[{"start":{"date-parts":[[2016,5,11]],"date-time":"2016-05-11T00:00:00Z","timestamp":1462924800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2016,5,11]],"date-time":"2016-05-11T00:00:00Z","timestamp":1462924800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Antibiot"],"published-print":{"date-parts":[[2016,12]]},"DOI":"10.1038\/ja.2016.48","type":"journal-article","created":{"date-parts":[[2016,5,11]],"date-time":"2016-05-11T06:23:11Z","timestamp":1462947791000},"page":"858-862","update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Kinetic characterization of GES-22 \u03b2-lactamase harboring the M169L clinical mutation"],"prefix":"10.1038","volume":"69","author":[{"given":"Aysegul","family":"Saral","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David A","family":"Leonard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Azer Ozad","family":"Duzgun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aysegul Copur","family":"Cicek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cynthia M","family":"June","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cemal","family":"Sandalli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2016,5,11]]},"reference":[{"key":"BFja201648_CR1","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1016\/S1473-3099(08)70041-0","volume":"8","author":"JD Pitout","year":"2008","unstructured":"Pitout, J. D. & Laupland, K. B. Extended-spectrum \u03b2-lactamase-producing Enterobacteriaceae: an emerging public-health concern. Lancet. Infect. Dis. 8, 159\u2013166 (2008).","journal-title":"Lancet. Infect. Dis."},{"key":"BFja201648_CR2","doi-asserted-by":"publisher","first-page":"5423","DOI":"10.1021\/ja042850a","volume":"127","author":"Y Chen","year":"2005","unstructured":"Chen, Y., Shoichet, B. & Bonnet, R. Structure, function, and inhibition along the reaction coordinate of CTX-M \u03b2-lactamases. J. Am. Chem. Soc. 127, 5423\u20135434 (2005).","journal-title":"J. Am. Chem. Soc."},{"key":"BFja201648_CR3","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1128\/CMR.18.4.657-686.2005","volume":"18","author":"DL Paterson","year":"2005","unstructured":"Paterson, D. L. & Bonomo, R. A. Extended-spectrum \u03b2-lactamases: a clinical update. Clin. Microbiol. Rev. 18, 657\u2013686 (2005).","journal-title":"Clin. Microbiol. Rev."},{"key":"BFja201648_CR4","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1128\/AAC.48.1.1-14.2004","volume":"48","author":"R Bonnet","year":"2004","unstructured":"Bonnet, R. Growing group of extended-spectrum \u03b2-lactamases: the CTX-M enzymes. Antimicrob. Agents Chemother. 48, 1\u201314 (2004).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR5","doi-asserted-by":"publisher","first-page":"410","DOI":"10.1111\/1469-0691.12338","volume":"20","author":"AC Cicek","year":"2014","unstructured":"Cicek, A. C. et al. OXA- and GES-type \u03b2-lactamases predominate in extensively drug-resistant Acinetobacter baumannii isolates from a Turkish University Hospital. Clin. Microbiol. Infect. 20, 410\u2013405 (2014).","journal-title":"Clin. Microbiol. Infect."},{"key":"BFja201648_CR6","doi-asserted-by":"publisher","first-page":"538","DOI":"10.1128\/CMR.00058-07","volume":"21","author":"AY Peleg","year":"2008","unstructured":"Peleg, A. Y., Seifert, H. & Paterson, D. L. Acinetobacter baumannii: emergence of a successful pathogen. Clin. Microbiol. Rev. 21, 538\u2013582 (2008).","journal-title":"Clin. Microbiol. Rev."},{"key":"BFja201648_CR7","doi-asserted-by":"publisher","first-page":"4864","DOI":"10.1128\/AAC.00771-10","volume":"54","author":"SD Kotsakis","year":"2010","unstructured":"Kotsakis, S. D., Miriagou, V., Tzelepi, E. & Tzouvelekis, L. S. Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES \u03b2-lactamases. Antimicrob. Agents Chemother. 54, 4864\u20134871 (2010).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR8","doi-asserted-by":"publisher","first-page":"2598","DOI":"10.1128\/AAC.45.9.2598-2603.2001","volume":"45","author":"L Poirel","year":"2001","unstructured":"Poirel, L., Weldhagen, G. F., Naas, T., De Champs, C., Dove, M. G. & Nordmann, P. GES-2, a class A \u03b2-lactamase from Pseudomonas aeruginosa with increased hydrolysis of imipenem. Antimicrob. Agents Chemother. 45, 2598\u20132603 (2001).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR9","doi-asserted-by":"publisher","first-page":"5618","DOI":"10.1128\/AAC.01272-12","volume":"56","author":"H Delbr\u00fcck","year":"2012","unstructured":"Delbr\u00fcck, H. et al. Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 \u03b2-lactamases. Antimicrob. Agents Chemother. 56, 5618\u20135625 (2012).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR10","doi-asserted-by":"publisher","first-page":"1960","DOI":"10.1128\/AAC.48.6.1960-1967.2004","volume":"48","author":"J Wachino","year":"2004","unstructured":"Wachino, J. et al. Nosocomial spread of ceftazidime-resistant Klebsiella pneumoniae strains producing a novel class a \u03b2-lactamase, GES-3, in a neonatal intensive care unit in Japan. Antimicrob. Agents Chemother. 48, 1960\u20131967 (2004).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR11","doi-asserted-by":"publisher","first-page":"396","DOI":"10.1128\/AAC.01784-12","volume":"57","author":"C Bebrone","year":"2013","unstructured":"Bebrone, C. et al. GES-18, a new carbapenem-hydrolyzing GES-Type \u03b2-lactamase from Pseudomonas aeruginosa that contains Ile80 and Ser170 residues. Antimicrob. Agents Chemother. 57, 396\u2013401 (2013).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR12","doi-asserted-by":"publisher","first-page":"7358","DOI":"10.1128\/AAC.03930-14","volume":"58","author":"M Castanheira","year":"2014","unstructured":"Castanheira, M., Costello, S. E., Woosley, L. N., Deshpande, L. M., Davies, T. A. & Jones, R.N. Evaluation of clonality and carbapenem resistance mechanisms among Acinetobacter baumannii-Acinetobacter calcoaceticus complex and Enterobacteriaceae isolates collected in European and Mediterranean countries and detection of two novel \u03b2-lactamases, GES-22 and VIM-35. Antimicrob. Agents Chemother. 58, 7358\u20137366 (2014).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR13","doi-asserted-by":"publisher","first-page":"1145","DOI":"10.1093\/jac\/dkt465","volume":"69","author":"AN Zeka","year":"2014","unstructured":"Zeka, A. N. et al. GES-type and OXA-23 carbapenemase-producing Acinetobacter baumannii in Turkey. J. Antimicrob. Chemother. 69, 1145\u20131146 (2014).","journal-title":"J. Antimicrob. Chemother."},{"key":"BFja201648_CR14","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1128\/AAC.01384-12","volume":"57","author":"RA Bonnin","year":"2013","unstructured":"Bonnin, R. A. et al. Wide dissemination of GES-type carbapenemases in Acinetobacter baumannii isolates in Kuwait. Antimicrob. Agents Chemother. 57, 183\u2013188 (2013).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR15","doi-asserted-by":"publisher","first-page":"600","DOI":"10.1128\/AAC.49.2.600-605.2005","volume":"49","author":"L Ma","year":"2005","unstructured":"Ma, L. et al. Novel SHV-derived extended-spectrum \u03b2-lactamase, SHV-57, that confers resistance to ceftazidime but not cefazolin. Antimicrob. Agents Chemother. 49, 600\u2013605 (2005).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR16","doi-asserted-by":"publisher","first-page":"1861","DOI":"10.1128\/AAC.01656-10","volume":"55","author":"L Djamdjian","year":"2011","unstructured":"Djamdjian, L., Naas, T., Tand\u00e9, D., Cuzon, G., Hanrotel-Saliou, C. & Nordmann, P. CTX-M-93, a CTX-M variant lacking penicillin hydrolytic activity. Antimicrob. Agents Chemother. 55, 1861\u20131866 (2011).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR17","doi-asserted-by":"publisher","first-page":"646","DOI":"10.1128\/AAC.46.3.646-653.2002","volume":"46","author":"S Vakulenko","year":"2002","unstructured":"Vakulenko, S. & Golemi, D. Mutant TEM \u03b2-lactamase producing resistance to ceftazidime, ampicillins, and \u03b2-lactamase inhibitors. Antimicrob. Agents Chemother. 46, 646\u2013653 (2002).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR18","doi-asserted-by":"publisher","first-page":"731","DOI":"10.1128\/AAC.50.2.731-738.2006","volume":"50","author":"J Delmas","year":"2006","unstructured":"Delmas, J., Robin, F., Carvalho, F., Mongaret, C. & Bonnet, R. Prediction of the evolution of ceftazidime resistance in extended-spectrum \u03b2-lactamase CTX-M-9. Antimicrob. Agents Chemother. 50, 731\u2013738 (2006).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR19","doi-asserted-by":"publisher","first-page":"19512","DOI":"10.1021\/ja308197j","volume":"134","author":"CA Smith","year":"2012","unstructured":"Smith, C. A. et al. Structural basis for progression toward the carbapenemase activity in the GES family of \u03b2-lactamases. J. Am. Chem. Soc. 134, 19512\u201319515 (2012).","journal-title":"J. Am. Chem. Soc."},{"key":"BFja201648_CR20","doi-asserted-by":"publisher","first-page":"3579","DOI":"10.1128\/AAC.00072-09","volume":"53","author":"C Moubareck","year":"2009","unstructured":"Moubareck, C., Br\u00e9mont, S., Conroy, M. C., Courvalin, P. & Lambert, T. GES-11, a novel integron-associated GES variant in Acinetobacter baumannii. Antimicrob. Agents Chemother. 53, 3579\u20133581 (2009).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR21","doi-asserted-by":"publisher","first-page":"4848","DOI":"10.1128\/AAC.00762-13","volume":"57","author":"KC Kaitany","year":"2013","unstructured":"Kaitany, K. C. et al. Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam. Antimicrob. Agents Chemother. 57, 4848\u20134855 (2013).","journal-title":"Antimicrob. Agents Chemother."},{"key":"BFja201648_CR22","doi-asserted-by":"publisher","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","volume":"22","author":"Y Cheng","year":"1973","unstructured":"Cheng, Y. & Prusoff, W. H. Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 22, 3099\u20133108 (1973).","journal-title":"Biochem. Pharmacol."},{"key":"BFja201648_CR23","unstructured":"Naas, T., Iorga, B., Djamdjian, L., Maros, M. & Nordmann, P. Insights in penicillin hydrolysis activity of class A extended-spectrum \u03b2-lactamases (ESBL) TLA-2. Abstracts of Papers of 23rd European Congress of Clinical Microbiology and Infectious Diseases, No. 1179, Berlin, Germany (2013)."},{"key":"BFja201648_CR24","doi-asserted-by":"publisher","first-page":"1429","DOI":"10.1093\/jac\/dkv002","volume":"70","author":"RH Nijhuis","year":"2015","unstructured":"Nijhuis, R. H., Oueslati, S., Zhou, K., Bosboom, R. W., Rossen, J. W. & Naas, T. OXY-2-15, a novel variant showing increased ceftazidime hydrolytic activity. J. Antimicrob. Chemother. 70, 1429\u20131433 (2015).","journal-title":"J. Antimicrob. Chemother."},{"key":"BFja201648_CR25","doi-asserted-by":"publisher","first-page":"1976","DOI":"10.1021\/bi501547k","volume":"54","author":"JM Mitchell","year":"2015","unstructured":"Mitchell, J. M. et al. Structural basis of activity against aztreonam and extended spectrum cephalosporins for two carbapenem-hydrolyzing class D \u03b2-lactamases from Acinetobacter baumannii. Biochemistry 54, 1976\u20131987 (2015).","journal-title":"Biochemistry"},{"key":"BFja201648_CR26","doi-asserted-by":"publisher","first-page":"46601","DOI":"10.1074\/jbc.M207884200","volume":"277","author":"T Shimamura","year":"2002","unstructured":"Shimamura, T. et al. Acyl-intermediate structures of the extended-spectrum class A \u03b2-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin. J. Biol. Chem. 277, 46601\u201346608 (2002).","journal-title":"J. Biol. Chem."},{"key":"BFja201648_CR27","unstructured":"PyMOL The PyMOL Molecular Graphics System, version 1.3, New York, NY, USA: Schr\u00f6dinger, LLC, (2014)"},{"key":"BFja201648_CR28","doi-asserted-by":"publisher","first-page":"540","DOI":"10.1016\/j.chembiol.2009.04.010","volume":"16","author":"JD Docquier","year":"2009","unstructured":"Docquier, J. D. et al. Crystal structure of the OXA-48 \u03b2-lactamase reveals mechanistic diversity among class D carbapenemases. Chem. Biol. 16, 540\u2013547 (2009).","journal-title":"Chem. Biol."},{"key":"BFja201648_CR29","doi-asserted-by":"publisher","first-page":"7600","DOI":"10.1021\/ja00134a003","volume":"117","author":"P Taibi","year":"2002","unstructured":"Taibi, P. & Mobashery, S. Mechanism of turnover of imipenem by the TEM \u03b2-lactamase revisited. J. Am. Chem. Soc. 117, 7600\u20137605 (2002).","journal-title":"J. Am. Chem. Soc."},{"key":"BFja201648_CR30","doi-asserted-by":"publisher","first-page":"2546","DOI":"10.1128\/AAC.00022-11","volume":"55","author":"L Poirel","year":"2011","unstructured":"Poirel, L. et al. OXA-163, an OXA-48-related class D \u03b2-lactamase with extended activity toward expanded-spectrum cephalosporins. Antimicrob. Agents Chemother. 55, 2546\u20132551 (2011).","journal-title":"Antimicrob. Agents Chemother."}],"container-title":["The Journal of Antibiotics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/ja201648.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ja201648","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ja201648.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T17:23:36Z","timestamp":1684430616000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ja201648"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5,11]]},"references-count":30,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2016,12]]}},"alternative-id":["BFja201648"],"URL":"https:\/\/doi.org\/10.1038\/ja.2016.48","relation":{},"ISSN":["0021-8820","1881-1469"],"issn-type":[{"value":"0021-8820","type":"print"},{"value":"1881-1469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,5,11]]},"assertion":[{"value":"13 December 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 March 2016","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 March 2016","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 May 2016","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"conflict of interest.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"This content has been made available to all.","name":"free","label":"Free to read"}]}}