{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T05:28:35Z","timestamp":1790659715251,"version":"4.1.0"},"reference-count":65,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,7]],"date-time":"2020-12-07T00:00:00Z","timestamp":1607299200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 AI32956"],"award-info":[{"award-number":["R01 AI32956"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R21 AI147654"],"award-info":[{"award-number":["R21 AI147654"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32AI055449"],"award-info":[{"award-number":["T32AI055449"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32GM008280"],"award-info":[{"award-number":["T32GM008280"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2021,1]]},"DOI":"10.1074\/jbc.ra120.015050","type":"journal-article","created":{"date-parts":[[2020,12,4]],"date-time":"2020-12-04T00:45:42Z","timestamp":1607042742000},"page":"100155","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":46,"special_numbering":"C","title":["KPC-2 \u03b2-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate"],"prefix":"10.1016","volume":"296","author":[{"given":"Shrenik C.","family":"Mehta","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian M.","family":"Furey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Orville A.","family":"Pemberton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David M.","family":"Boragine","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5267-0001","authenticated-orcid":false,"given":"Timothy","family":"Palzkill","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.015050_bib1","doi-asserted-by":"crossref","first-page":"4943","DOI":"10.1128\/AAC.00296-11","article-title":"Carbapenems: past, present, and future","volume":"55","author":"Papp-Wallace","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib2","doi-asserted-by":"crossref","first-page":"2410","DOI":"10.1093\/jac\/dkx181","article-title":"Sparing carbapenem usage","volume":"72","author":"Wilson","year":"2017","journal-title":"J.\u00a0Antimicrob. Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib3","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.coph.2014.09.012","article-title":"Penicillin-binding proteins: evergreen drug targets","volume":"18","author":"Fr\u00e8re","year":"2014","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1074\/jbc.RA120.015050_bib4","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/0002-9343(85)90097-X","article-title":"Carbapenems, a new class of beta-lactam antibiotics. Discovery and development of imipenem\/cilastatin","volume":"78","author":"Birnbaum","year":"1985","journal-title":"Am. J. Med."},{"key":"10.1074\/jbc.RA120.015050_bib5","doi-asserted-by":"crossref","first-page":"9748","DOI":"10.1021\/ja9818001","article-title":"Structural basis for clinical longevity of carbapenem antibiotics in the face of challenge by the common class A \u03b2-lactamases from the antibiotic-resistant bacteria","volume":"120","author":"Maveyraud","year":"1998","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib6","doi-asserted-by":"crossref","first-page":"12656","DOI":"10.1021\/ja7111146","article-title":"Inhibition of class A \u03b2-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1","volume":"130","author":"Nukaga","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib7","doi-asserted-by":"crossref","first-page":"18275","DOI":"10.1021\/ja304460j","article-title":"The basis for carbapenem hydrolysis by class A \u03b2-lactamases: a combined investigation using crystallography and simulations","volume":"134","author":"Fonseca","year":"2012","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib8","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The structure of beta-lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Phil. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"10.1074\/jbc.RA120.015050_bib9","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1749-6632.2012.06796.x","article-title":"Metallo-beta-lactamase structure and function","volume":"1277","author":"Palzkill","year":"2013","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1074\/jbc.RA120.015050_bib10","doi-asserted-by":"crossref","first-page":"3766","DOI":"10.1021\/bi100232q","article-title":"Biochemical and structural characterization of Mycobacterium tuberculosis \u03b2-lactamase with the carbapenems ertapenem and doripenem","volume":"49","author":"Tremblay","year":"2010","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib11","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1021\/bi00541a008","article-title":"Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acid","volume":"21","author":"Easton","year":"1982","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib12","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1128\/AAC.38.6.1262","article-title":"Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing class A beta-lactamase, Sme-1, from Serratia marcescens S6","volume":"38","author":"Naas","year":"1994","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib13","doi-asserted-by":"crossref","first-page":"3421","DOI":"10.1128\/AAC.49.8.3421-3427.2005","article-title":"Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1","volume":"49","author":"Majiduddin","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib14","first-page":"29","article-title":"A\u00a0kinetic study of NMC-A beta-lactamase, an ambler class A carbapenemase also hydrolyzing cephamycins","volume":"143","author":"Mariotte-Boyer","year":"1996","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1074\/jbc.RA120.015050_bib15","doi-asserted-by":"crossref","first-page":"9382","DOI":"10.1021\/ja9817996","article-title":"Inhibition of the NMC-A beta-lactamase by a penicillanic acid derivative and the structural bases for the increase in substrate profile of this antibiotic resistance enzyme","volume":"120","author":"Mourey","year":"1998","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib16","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1128\/AAC.45.4.1151-1161.2001","article-title":"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem- resistant strain of Klebsiella pneumoniae","volume":"45","author":"Yigit","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib17","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1128\/AAC.48.6.2321-2324.2004","article-title":"Molecular characterization of a carbapenem-hydrolyzing class A beta-lactamase, SFC-1, from Serratia fonticola UTAD54","volume":"48","author":"Henriques","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib18","doi-asserted-by":"crossref","first-page":"4512","DOI":"10.1128\/AAC.00491-07","article-title":"Biochemical characterization of SFC-1, a class A carbapenem-hydrolyzing beta-lactamase","volume":"51","author":"Fonseca","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib19","doi-asserted-by":"crossref","first-page":"6057","DOI":"10.1128\/AAC.01156-12","article-title":"KPC-9, a novel carbapenemase from clinical specimens in Israel","volume":"56","author":"Hidalgo-Grass","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib20","doi-asserted-by":"crossref","first-page":"6006","DOI":"10.1128\/AAC.01338-12","article-title":"Antibiotic resistance and substrate profiles of the class A carbapenemase KPC-6","volume":"56","author":"Lamoureaux","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib21","doi-asserted-by":"crossref","first-page":"1632","DOI":"10.1128\/JCM.06115-11","article-title":"Using nucleic acid microarrays to perform molecular epidemiology and detect novel \u03b2-lactamases: a snapshot of extended-spectrum \u03b2-lactamases throughout the world","volume":"50","author":"Lascols","year":"2012","journal-title":"J.\u00a0Clin. Microbiol."},{"key":"10.1074\/jbc.RA120.015050_bib22","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1128\/AAC.00899-09","article-title":"Detection of KPC in Acinetobacter spp. in Puerto Rico","volume":"54","author":"Robledo","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib23","doi-asserted-by":"crossref","first-page":"4793","DOI":"10.1128\/AAC.48.12.4793-4799.2004","article-title":"Outbreak of Klebsiella pneumoniae producing a new carbapenem-hydrolyzing class A beta-lactamase, KPC-3, in a New York Medical Center","volume":"48","author":"Woodford","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib24","doi-asserted-by":"crossref","first-page":"401","DOI":"10.2174\/138920309789351967","article-title":"Three decades of the class A beta-lactamase acyl-enzyme","volume":"10","author":"Fisher","year":"2009","journal-title":"Curr. Prot. Pept. Sci."},{"key":"10.1074\/jbc.RA120.015050_bib25","doi-asserted-by":"crossref","first-page":"11830","DOI":"10.1021\/bi800833u","article-title":"Carbapenems and SHV-1 beta-lactamase form different acyl-enzyme populations in crystals and solution","volume":"47","author":"Kalp","year":"2008","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib26","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.1021\/acscatal.7b03832","article-title":"Conformational intermediate that controls KPC-2 catalysis and beta-lactam drug resistance","volume":"8","author":"Cortina","year":"2018","journal-title":"ACS Catal."},{"key":"10.1074\/jbc.RA120.015050_bib27","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/bj2530323","article-title":"Imipenem as substrate and inhibitor of beta-lactamases","volume":"253","author":"Monks","year":"1988","journal-title":"Biochem. J."},{"key":"10.1074\/jbc.RA120.015050_bib28","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1128\/AAC.47.3.1062-1067.2003","article-title":"Amino acid sequence requirements at residues 69 and 238 for SME-1 \u03b2\u2212lactamase to confer resistance to \u03b2-lactam antibiotics","volume":"47","author":"Majiduddin","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.RA120.015050_bib29","doi-asserted-by":"crossref","first-page":"5732","DOI":"10.1021\/bi700300u","article-title":"Crystal structure of KPC-2: insights into carbapenemase activity in class A \u03b2-lactamases","volume":"46","author":"Ke","year":"2007","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib30","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1021\/acs.jmedchem.7b00158","article-title":"Molecular basis of substrate recognition and product release by the Klebsiella pneumoniae carbapenemase (KPC-2)","volume":"60","author":"Pemberton","year":"2017","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1074\/jbc.RA120.015050_bib31","doi-asserted-by":"crossref","first-page":"7600","DOI":"10.1021\/ja00134a003","article-title":"Mechanism of turnover of imipenem by the TEM \u03b2-lactamase revisted","volume":"117","author":"Taibi","year":"1995","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib32","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1021\/bi501052t","article-title":"Kinetic and structural requirements for carbapenemase activity in GES-type \u03b2-lactamases","volume":"54","author":"Stewart","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib33","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1021\/ja00030a070","article-title":"Facilitation of the D2 \u00c6 D1 pyrroline tautomerization of carbapenam antibiotics by the highly conserved arginine-244 of class A \u03b2-lactamases during the course of turnover","volume":"114","author":"Zafaralla","year":"1992","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib34","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3389\/fmolb.2018.00016","article-title":"Structural and mechanistic basis for extended-spectrum drug-resistance mutations in altering the specificity of TEM, CTX-M, and KPC \u03b2-lactamases","volume":"5","author":"Palzkill","year":"2018","journal-title":"Front. Mol. Biosci."},{"key":"10.1074\/jbc.RA120.015050_bib35","series-title":"Enzyme-Mediated Resistance to Antibiotics: Mechanisms, Dissemination, and Prospects for Inhibition","first-page":"67","article-title":"Kinetics of \u03b2-lactamases and penicillin-binding proteins","author":"Galleni","year":"2007"},{"key":"10.1074\/jbc.RA120.015050_bib36","doi-asserted-by":"crossref","first-page":"29509","DOI":"10.1074\/jbc.M109.011262","article-title":"Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of beta-lactamases","volume":"284","author":"Frase","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015050_bib37","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1042\/bj2310083","article-title":"Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus","volume":"231","author":"Bicknell","year":"1985","journal-title":"Biochem. J."},{"key":"10.1074\/jbc.RA120.015050_bib38","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/0014-5793(69)80261-9","article-title":"The ficin-catalysed hydrolysis of p-nitrophenyl hippurate. Detailed kinetics including the measurement of the apparent dissociation constant for the enzyme-substrate complex","volume":"4","author":"Hollaway","year":"1969","journal-title":"FEBS Lett."},{"key":"10.1074\/jbc.RA120.015050_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1001599","article-title":"Ground state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymes","volume":"11","author":"Andrews","year":"2013","journal-title":"PLoS Biol."},{"key":"10.1074\/jbc.RA120.015050_bib40","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/359700a0","article-title":"Molecular structure of the acyl-enzyme intermediate in \u03b2-lactam hydrolysis at 1.7 A resolution","volume":"359","author":"Strynadka","year":"1992","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.015050_bib41","doi-asserted-by":"crossref","first-page":"1747","DOI":"10.1073\/pnas.93.5.1747","article-title":"The catalytic mechanism of \u03b2-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme","volume":"93","author":"Damblon","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015050_bib42","doi-asserted-by":"crossref","first-page":"5333","DOI":"10.1021\/ja0259640","article-title":"An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation","volume":"124","author":"Minasov","year":"2002","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1074\/jbc.RA120.015050_bib43","doi-asserted-by":"crossref","first-page":"3443","DOI":"10.1021\/acs.biochem.7b00176","article-title":"The drug-resistant variant P167S expands the substrate profile of CTX-M \u03b2-lactamases for oxyimino-cephalosporin antibiotics by enlarging the active site upon acylation","volume":"56","author":"Patel","year":"2017","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib44","doi-asserted-by":"crossref","first-page":"33703","DOI":"10.1074\/jbc.M109.053819","article-title":"Structural and biochemical evidence that a TEM-1 \u03b2-lactamase Asn170Gly active site mutant acts via substrate assisted catalysis","volume":"284","author":"Brown","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015050_bib45","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0003-2697(87)90203-X","article-title":"The analysis of enzyme progress curves by numerical differentiation, including competitive product inhibition and enzyme reactivation","volume":"165","author":"Koerber","year":"1987","journal-title":"Anal. Biochem."},{"key":"10.1074\/jbc.RA120.015050_bib46","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1021\/acsinfecdis.9b00304","article-title":"Structural basis for substrate specificity and carbapenemase activity of OXA-48 class D \u03b2-lactamase","volume":"6","author":"Akhtar","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"10.1074\/jbc.RA120.015050_bib47","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.jmb.2005.02.010","article-title":"Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability","volume":"348","author":"Chen","year":"2005","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1074\/jbc.RA120.015050_bib48","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.jmb.2010.04.062","article-title":"Structural insights into substrate recognition and product expulsion in CTX-M enzymes","volume":"400","author":"Delmas","year":"2010","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1074\/jbc.RA120.015050_bib49","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1021\/bi501195g","article-title":"Molecular basis for the catalytic specificity of the CTX-M extended spectrum \u03b2-lactamases","volume":"54","author":"Adamski","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015050_bib50","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/0378-1119(83)90222-6","article-title":"Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli","volume":"25","author":"Amann","year":"1983","journal-title":"Gene"},{"key":"10.1074\/jbc.RA120.015050_bib51","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004949","article-title":"Natural variants of the KPC-2 carbapenemase have evolved increased catalytic efficiency for ceftazidime hydrolysis at the cost of enzyme stability","volume":"11","author":"Mehta","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1074\/jbc.RA120.015050_bib52","doi-asserted-by":"crossref","first-page":"2394","DOI":"10.1074\/jbc.274.4.2394","article-title":"Contributions of aspartate 49 and phenylalanine 142 residues of a tight binding inhibitory protein of beta-lactamases","volume":"274","author":"Petrosino","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015050_bib53","doi-asserted-by":"crossref","first-page":"W597","DOI":"10.1093\/nar\/gks400","article-title":"ExPASy: SIB bioinformatics resource portal","volume":"40","author":"Artimo","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.RA120.015050_bib54","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib55","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib56","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib57","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Cryst."},{"key":"10.1074\/jbc.RA120.015050_bib58","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1074\/jbc.RA120.015050_bib59","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib60","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib61","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1107\/S0907444908004319","article-title":"Iterative-build OMIT maps: map improvement by iterative model building and refinement without model bias","volume":"64","author":"Terwilliger","year":"2008","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib62","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1107\/S0907444909029436","article-title":"Electronic ligand builder and optimization workbench (eLBOW): a tool for ligand coordinate and restraint generation","volume":"65","author":"Moriarty","year":"2009","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.RA120.015050_bib63","doi-asserted-by":"crossref","first-page":"W615","DOI":"10.1093\/nar\/gkh398","article-title":"MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes","volume":"32","author":"Davis","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.RA120.015050_bib64","series-title":"Kinetic Analysis for the New Enzymology","author":"Johnson","year":"2019"},{"key":"10.1074\/jbc.RA120.015050_bib65","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1021\/bi00912a021","article-title":"The kinetics of the alpha-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate","volume":"1","author":"Kezdy","year":"1962","journal-title":"Biochemistry"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820001489?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820001489?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.015050","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,17]],"date-time":"2021-10-17T02:13:40Z","timestamp":1634436820000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820001489"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1]]},"references-count":65,"alternative-id":["S0021925820001489"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.015050","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2021,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"KPC-2 \u03b2-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.015050","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"100155"}}