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OXA-48 is a class D \u03b2-lactamase that hydrolyzes carbapenems through a catalytic mechanism involving a nucleophilic serine and a carboxylated lysine general base. To define the contributions of conserved active-site residues to catalysis and substrate turnover, alanine substitutions were introduced at key active site positions, followed by steady-state and presteady-state kinetic analysis of mutant enzymes for imipenem and cephalothin hydrolysis. Mutations produced distinct effects, revealing roles in substrate acylation and deacylation reactions. Substitutions at Val120, Trp157, and Leu158 cause the largest decreases in kcat for both imipenem and cephalothin hydrolysis. It is known that deacylation is the rate-limiting step in carbapenem hydrolysis by OXA-48 and presteady-state kinetics analysis shows that the V120A and L158A substitutions further slow the deacylation reaction for imipenem, reducing kcat and kcat\/KM values. Our data are also consistent with acylation being rate-limiting for cephalothin hydrolysis, with the V120A and L158A substitutions reducing substrate binding affinity and\/or the acylation rate. Structural analysis indicates that the V120A enzyme has open water channel to the noncarboxylated Lys73 while the L158A enzyme is also open to water but has a carboxylated Lys73. Together, these results support a model in which conserved hydrophobic active-site residues optimize the geometric and electrostatic environment required for efficient carbapenem deacylation and turnover. These findings provide mechanistic insight into OXA-48 catalysis that may be exploited to design inhibitors targeting the enzyme.<\/jats:p>","DOI":"10.1021\/acsinfecdis.6c00562","type":"journal-article","created":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T13:10:05Z","timestamp":1789132205000},"page":"3241-3252","source":"Crossref","is-referenced-by-count":0,"title":["Mechanistic\nRoles of Conserved Active-Site Residues\nin OXA-48 Carbapenem Hydrolysis"],"prefix":"10.1021","volume":"12","author":[{"given":"Doris M.","family":"Taylor","sequence":"first","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-3455-3338","authenticated-orcid":true,"given":"Dignite\u0301 Fabrice","family":"Ngango","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7354-4306","authenticated-orcid":true,"given":"Jiayi","family":"Fan","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suhyeorn","family":"Park","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Banumathi","family":"Sankaran","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B. V. Venkataram","family":"Prasad","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5267-0001","authenticated-orcid":true,"given":"Timothy","family":"Palzkill","sequence":"additional","affiliation":[{"name":"Baylor College of Medicine , , , ,","place":["Houston, Texas, United States, 77030"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,24]]},"reference":[{"issue":"2","key":"2026091109095967900_cit1","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00047-19","article-title":"Epidemiology\nof \u03b2-Lactamase-Producing Pathogens","volume":"33","author":"Bush","year":"2020","journal-title":"Clin.\nMicrobiol. Rev."},{"key":"2026091109095967900_cit2","doi-asserted-by":"publisher","first-page":"a025239","DOI":"10.1101\/cshperspect.a025239","article-title":"\u03b2-Lactamases:\nA Focus on Current Challenges","volume":"7","author":"Bonomo","year":"2017","journal-title":"Cold Spring Harb.\nPerspect. Med."},{"issue":"8","key":"2026091109095967900_cit3","doi-asserted-by":"publisher","first-page":"1290","DOI":"10.1093\/cid\/cix893","article-title":"Carbapenemase-Producing\nOrganisms:\nA Global Scourge","volume":"66","author":"Bonomo","year":"2018","journal-title":"Clin. Infect. Dis."},{"issue":"10","key":"2026091109095967900_cit4","doi-asserted-by":"publisher","first-page":"1623","DOI":"10.1039\/D1MD00200G","article-title":"\u03b2-Lactam Antibiotic\nTargets and Resistance Mechanisms:\nFrom Covalent Inhibitors to Substrates","volume":"12","author":"Mora-Ochomogo","year":"2021","journal-title":"RSC\nMed. Chem."},{"issue":"1","key":"2026091109095967900_cit5","doi-asserted-by":"publisher","first-page":"106","DOI":"10.3390\/pharmaceutics18010106","article-title":"Targeting Bacterial Cell Wall Synthesis:\nStructural Insights and Emerging Therapeutic Strategies","volume":"18","author":"Sanapalli","year":"2026","journal-title":"Pharmaceutics"},{"key":"2026091109095967900_cit6","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1038\/146837a0","article-title":"An Enzyme from Bacteria\nAble to Destroy Penicillin","volume":"146","author":"Abraham","year":"1940","journal-title":"Nature (London)"},{"key":"2026091109095967900_cit7","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The Structure\nof Beta-Lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Philos. Trans. R. Soc. Lond.\nSer. 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Res."},{"key":"2026091109095967900_cit11","doi-asserted-by":"publisher","first-page":"401","DOI":"10.2174\/138920309789351967","article-title":"Three Decades\nof the Class A Beta-Lactamase Acyl-Enzyme","volume":"10","author":"Fisher","year":"2009","journal-title":"Curr.\nProtein Pept. Sci."},{"issue":"25","key":"2026091109095967900_cit12","doi-asserted-by":"publisher","first-page":"14280","DOI":"10.1073\/pnas.241442898","article-title":"Critical Involvement\nof a Carbamylated Lysine in Catalytic Function of Class D Beta-Lactamases","volume":"98","author":"Golemi","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026091109095967900_cit13","doi-asserted-by":"publisher","first-page":"6132","DOI":"10.1021\/ja0013881","article-title":"The First\nStructural and Mechanistic Insights for Class D B-Lactamases: Evidence\nfor a Novel Catalytic Process for Turnover of \u03b2-Lactam Antibiotics","volume":"122","author":"Golemi","year":"2000","journal-title":"J. Am. Chem. 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Dis."},{"issue":"5","key":"2026091109095967900_cit23","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.02329-19","article-title":"Role of Arginine\n214 in the Substrate Specificity of OXA-48","volume":"64","author":"Oueslati","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"issue":"4","key":"2026091109095967900_cit24","doi-asserted-by":"publisher","first-page":"1059","DOI":"10.1093\/jac\/dku524","article-title":"Heterogeneous Hydrolytic Features\nfor OXA-48-like \u03b2-Lactamases","volume":"70","author":"Oueslati","year":"2015","journal-title":"J. Antimicrob.\nChemother."},{"issue":"17","key":"2026091109095967900_cit25","doi-asserted-by":"publisher","first-page":"2479","DOI":"10.1021\/acs.biochem.6b00056","article-title":"Removal of the Side\nChain at the Active-Site Serine by a Glycine Substitution Increases\nthe Stability of a Wide Range of Serine \u03b2-Lactamases by Relieving\nSteric Strain","volume":"55","author":"Stojanoski","year":"2016","journal-title":"Biochemistry"},{"issue":"21","key":"2026091109095967900_cit26","doi-asserted-by":"publisher","first-page":"3370","DOI":"10.1021\/acs.biochem.5b00298","article-title":"Structural\nBasis for Different Substrate Profiles of Two Closely Related Class\nD \u03b2-Lactamases and Their Inhibition by Halogens","volume":"54","author":"Stojanoski","year":"2015","journal-title":"Biochemistry"},{"key":"2026091109095967900_cit27","doi-asserted-by":"publisher","first-page":"16","DOI":"10.3389\/fmolb.2018.00016","article-title":"Structural\nand Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations\nin Altering the Specificity of TEM, CTX-M, and KPC \u03b2-Lactamases","volume":"5","author":"Palzkill","year":"2018","journal-title":"Front. Mol. Biosci."},{"key":"2026091109095967900_cit28","first-page":"67","article-title":"Kinetics of \u03b2-Lactamases\nand Penicillin-Binding Proteins","volume-title":"Enzyme-Mediated\nResistance to Antibiotics: Mechanisms, Dissemination, and Prospects\nfor Inhibition","author":"Galleni","year":"2007"},{"issue":"14","key":"2026091109095967900_cit29","doi-asserted-by":"publisher","first-page":"3220","DOI":"10.1021\/bi00685a029","article-title":"Partition\nAnalysis and the Concept of Net Rate Constants as Tools in Enzyme\nKinetics","volume":"14","author":"Cleland","year":"1975","journal-title":"Biochemistry"},{"key":"2026091109095967900_cit30","volume-title":"Kinetic Analysis for\nthe New Enzymology","author":"Johnson","year":"2019","edition":"1"},{"issue":"8","key":"2026091109095967900_cit31","doi-asserted-by":"publisher","first-page":"692","DOI":"10.1107\/S2059798317008671","article-title":"The Role\nof Conserved Surface Hydrophobic Residues\nin the Carbapenemase Activity of the Class D \u03b2-Lactamases","volume":"73","author":"Toth","year":"2017","journal-title":"Acta Crystallogr., Sect. D: Struct. Biol."},{"issue":"2","key":"2026091109095967900_cit32","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1021\/acsinfecdis.0c00798","article-title":"Mechanistic\nBasis of OXA-48-like \u03b2-Lactamases\u2019\nHydrolysis of Carbapenems","volume":"7","author":"Stojanoski","year":"2021","journal-title":"ACS Infect. Dis."},{"issue":"2","key":"2026091109095967900_cit33","doi-asserted-by":"publisher","DOI":"10.1128\/mSphere.00024-19","article-title":"OXA-48-Mediated\nCeftazidime-Avibactam\nResistance Is Associated with Evolutionary Trade-Offs","volume":"4","author":"Fro\u0308hlich","year":"2019","journal-title":"mSphere"},{"key":"2026091109095967900_cit34","doi-asserted-by":"publisher","first-page":"6188","DOI":"10.1021\/acscatal.0c00596","article-title":"Small Changes in Hydration Determine Cephalosporinase\nActivity of OXA-48 \u03b2-Lactamases","volume":"10","author":"Hirvonen","year":"2020","journal-title":"ACS Catal."},{"issue":"9","key":"2026091109095967900_cit35","doi-asserted-by":"publisher","first-page":"5416","DOI":"10.1021\/acs.jcim.6c00223","article-title":"Hydrogen-Bonding\nChanges Cause Differences in Imipenem Breakdown Activity in OXA-48\nVariants","volume":"66","author":"Wang","year":"2026","journal-title":"J. Chem. Inf. Model."},{"issue":"8","key":"2026091109095967900_cit36","doi-asserted-by":"publisher","first-page":"4534","DOI":"10.1021\/acscatal.1c05694","article-title":"Multiscale Simulations Identify Origins of Differential\nCarbapenem Hydrolysis by the OXA-48 \u03b2-Lactamase","volume":"12","author":"Hirvonen","year":"2022","journal-title":"ACS Catal."},{"issue":"12","key":"2026091109095967900_cit37","doi-asserted-by":"publisher","first-page":"2339","DOI":"10.1021\/acscentsci.3c00609","article-title":"An Ion-Pair\nInduced Intermediate Complex Captured in Class D Carbapenemase Reveals\nChloride Ion as a Janus Effector Modulating Activity","volume":"9","author":"Zhou","year":"2023","journal-title":"ACS Cent. Sci."},{"issue":"1","key":"2026091109095967900_cit38","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00102-19","article-title":"The Global\nAscendency of OXA-48-Type Carbapenemases","volume":"33","author":"Pitout","year":"2019","journal-title":"Clin.\nMicrobiol. 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Infect."},{"key":"2026091109095967900_cit42","volume-title":"Enzyme Structure and\nMechanism","author":"Fersht","year":"1985"},{"issue":"5","key":"2026091109095967900_cit43","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1021\/acsinfecdis.0c00015","article-title":"Identifying Oxacillinase-48 Carbapenemase Inhibitors\nUsing DNA-Encoded Chemical Libraries","volume":"6","author":"Taylor","year":"2020","journal-title":"ACS Infect.\nDis."},{"key":"2026091109095967900_cit44","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/j.jbiotec.2016.06.012","article-title":"Tobacco Etch\nVirus Protease: A Shortcut\nacross Biotechnologies","volume":"231","author":"Cesaratto","year":"2016","journal-title":"J. Biotechnol."},{"issue":"2","key":"2026091109095967900_cit45","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gku1189","article-title":"New Insights into the QuikChangeTM Process Guide the Use\nof Phusion DNA Polymerase for Site-Directed\nMutagenesis","volume":"43","author":"Xia","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"2026091109095967900_cit46","doi-asserted-by":"publisher","first-page":"100155","DOI":"10.1074\/jbc.RA120.015050","article-title":"KPC-2 \u03b2-Lactamase\nEnables Carbapenem Antibiotic\nResistance through Fast Deacylation of the Covalent Intermediate","volume":"296","author":"Mehta","year":"2021","journal-title":"J. Biol. Chem."},{"issue":"4","key":"2026091109095967900_cit47","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview\nof the CCP4 Suite and Current Developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. Sect. D Biol. 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