{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T23:32:32Z","timestamp":1793057552133,"version":"4.5.0"},"reference-count":54,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"vor","delay-in-days":5,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["24K09366"],"award-info":[{"award-number":["24K09366"]}],"id":[{"id":"10.13039\/501100001691","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":[[2026,10]]},"DOI":"10.1016\/j.jbc.2026.113628","type":"journal-article","created":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T06:37:50Z","timestamp":1791527870000},"page":"113628","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural basis for oxidation-coupled isomerization by ApnO"],"prefix":"10.1016","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6530-9047","authenticated-orcid":false,"given":"Seiya","family":"Watanabe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuzuki","family":"Aono","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shin-ichi","family":"Terawaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Himika","family":"Sato","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taiyo","family":"Yokoi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113628_bib1","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.tibs.2024.04.007","article-title":"Double-duty isomerases: a case study of isomerization-coupled enzymatic catalysis","volume":"49","author":"Solano","year":"2024","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.jbc.2026.113628_bib2","doi-asserted-by":"crossref","first-page":"9437","DOI":"10.1002\/anie.201204138","article-title":"A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase","volume":"51","author":"Katsuyama","year":"2012","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1016\/j.jbc.2026.113628_bib3","doi-asserted-by":"crossref","first-page":"9879","DOI":"10.1073\/pnas.95.17.9879","article-title":"A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis","volume":"95","author":"Takahashi","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jbc.2026.113628_bib4","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1021\/bi00428a012","article-title":"Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement","volume":"28","author":"Chunduru","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113628_bib5","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1038\/s41589-018-0067-7","article-title":"Functional assignment of multiple catabolic pathways for D-apiose","volume":"14","author":"Carter","year":"2018","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib6","doi-asserted-by":"crossref","first-page":"7523","DOI":"10.1021\/cr200055g","article-title":"Semipinacol rearrangement in natural product synthesis","volume":"111","author":"Song","year":"2011","journal-title":"Chem Rev"},{"key":"10.1016\/j.jbc.2026.113628_bib7","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1093\/glycob\/cww012","article-title":"Apiose: one of nature's witty games","volume":"26","author":"Pi\u010dmanov\u00e1","year":"2016","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2026.113628_bib8","doi-asserted-by":"crossref","first-page":"21434","DOI":"10.1074\/jbc.M116.749069","article-title":"Functional characterization of UDP-apiose synthases from bryophytes and green algae provides insight into the appearance of apiose-containing glycans during plant evolution","volume":"291","author":"Smith","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib9","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/s41598-018-36774-6","article-title":"Novel non-phosphorylating pathway of pentose metabolism from bacteria","volume":"9","author":"Watanabe","year":"2019","journal-title":"Sci Rep"},{"key":"10.1016\/j.jbc.2026.113628_bib10","first-page":"E4161","article-title":"Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars","volume":"113","author":"Zhang","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jbc.2026.113628_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2026.111280","article-title":"Identification, functional characterization, and structural analysis of an atypical L-threonate 3-dehydrogenase","volume":"302","author":"Watanabe","year":"2026","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib12","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/j.bbrc.2018.10.033","article-title":"Discovering a new catabolic pathway of D-ribonate in Mycobacterium smegmatis","volume":"505","author":"Luo","year":"2018","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.jbc.2026.113628_bib13","doi-asserted-by":"crossref","first-page":"2583","DOI":"10.1099\/ijs.0.64397-0","article-title":"Aurantimonas altamirensis sp. nov., a member of the order Rhizobiales isolated from Altamira Cave","volume":"56","author":"Jurado","year":"2006","journal-title":"Int J Syst Evol Microbiol"},{"key":"10.1016\/j.jbc.2026.113628_bib14","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1016\/S0021-9258(18)51644-6","article-title":"L-Threonic acid dehydrogenase: Purification and properties","volume":"239","author":"Aspen","year":"1964","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib15","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113628_bib16","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.jmb.2012.09.018","article-title":"Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle","volume":"424","author":"Wong","year":"2012","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib17","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/s41557-022-01005-z","article-title":"Pathogenic bacteria remodel central metabolic enzyme to build a cyclopropanol warhead","volume":"14","author":"Trottmann","year":"2022","journal-title":"Nat Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib18","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1038\/nchembio.2414","article-title":"Molecular basis of the evolution of alternative tyrosine biosynthetic routes in plants","volume":"13","author":"Schenck","year":"2017","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib19","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.jmb.2005.08.036","article-title":"Crystal structures of \u03941-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes","volume":"354","author":"Nocek","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib20","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1042\/BJ20150183","article-title":"Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases","volume":"468","author":"Cahn","year":"2015","journal-title":"Biochem J"},{"key":"10.1016\/j.jbc.2026.113628_bib21","doi-asserted-by":"crossref","first-page":"3405","DOI":"10.1093\/emboj\/16.12.3405","article-title":"The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 \u00c5 resolution","volume":"16","author":"Biou","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/j.jbc.2026.113628_bib22","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1107\/S0907444900001694","article-title":"Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose","volume":"56","author":"Thomazeau","year":"2000","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jbc.2026.113628_bib23","doi-asserted-by":"crossref","first-page":"3089","DOI":"10.1110\/ps.051791305","article-title":"The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution","volume":"14","author":"Tyagi","year":"2005","journal-title":"Protein Sci"},{"key":"10.1016\/j.jbc.2026.113628_bib24","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.jmb.2012.09.018","article-title":"Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle","volume":"424","author":"Wong","year":"2012","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib25","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0022-2836(03)00264-X","article-title":"Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa","volume":"328","author":"Ahn","year":"2003","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib26","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.jmb.2009.04.012","article-title":"Conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding as revealed by two crystal structures","volume":"389","author":"Leung","year":"2009","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib27","doi-asserted-by":"crossref","first-page":"18289","DOI":"10.1002\/chem.201704481","article-title":"Crystal structures of Staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state analogues that have biocidal activity","volume":"23","author":"Patel","year":"2017","journal-title":"Chemistry"},{"key":"10.1016\/j.jbc.2026.113628_bib28","doi-asserted-by":"crossref","first-page":"7176","DOI":"10.1038\/s41598-018-25361-4","article-title":"NADH\/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius","volume":"8","author":"Chen","year":"2018","journal-title":"Sci Rep"},{"key":"10.1016\/j.jbc.2026.113628_bib29","article-title":"A Ketol-Acid reductoisomerase inhibitor that has antituberculosis and herbicidal activity","volume":"31","author":"Lin","year":"2025","journal-title":"Chemistry"},{"key":"10.1016\/j.jbc.2026.113628_bib30","doi-asserted-by":"crossref","first-page":"8527","DOI":"10.1021\/acs.jafc.9b03262","article-title":"Crystal structure and biochemical characterization of ketol-acid reductoisomerase from Corynebacterium glutamicum","volume":"67","author":"Lee","year":"2019","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib31","doi-asserted-by":"crossref","first-page":"6827","DOI":"10.1021\/acscatal.4c00958","article-title":"Mapping of the reaction trajectory catalyzed by class I ketol-acid reductoisomerase","volume":"14","author":"Lin","year":"2024","journal-title":"ACS Catalysis"},{"key":"10.1016\/j.jbc.2026.113628_bib32","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1107\/S0907444901012823","article-title":"Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase by the MAD method using Mn atoms","volume":"57","author":"Yasutake","year":"2001","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jbc.2026.113628_bib33","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/S0969-2126(02)00904-8","article-title":"Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication","volume":"10","author":"Yasutake","year":"2002","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.113628_bib34","first-page":"381","article-title":"The biochemical properties of manganese in plants","volume":"8","author":"Schmidt","year":"2019","journal-title":"Plants (Basel)"},{"key":"10.1016\/j.jbc.2026.113628_bib35","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1126\/science.279.5347.98","article-title":"Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis","volume":"279","author":"Rozwarski","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113628_bib36","doi-asserted-by":"crossref","first-page":"5749","DOI":"10.1038\/s41598-018-24063-1","article-title":"Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex","volume":"8","author":"Ogata","year":"2018","journal-title":"Sci Rep"},{"key":"10.1016\/j.jbc.2026.113628_bib37","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1042\/BCJ20240685","article-title":"Metal sensing properties of the disordered loop from the Arabidopsis metal transceptor IRT1","volume":"482","author":"Cointry","year":"2025","journal-title":"Biochem J"},{"key":"10.1016\/j.jbc.2026.113628_bib38","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1515\/pac-2024-0276","article-title":"Acid dissociation constants in selected dipolar non-hydrogen-bond-donor solvents (IUPAC Technical Report)","volume":"97","author":"Leito","year":"2025","journal-title":"Pure Appl Chem"},{"key":"10.1016\/j.jbc.2026.113628_bib39","doi-asserted-by":"crossref","first-page":"29625","DOI":"10.1039\/C8CP04776F","article-title":"Factors governing when a metal-bound water is deprotonated in proteins","volume":"20","author":"Grauffel","year":"2018","journal-title":"Phys Chem Chem Phys"},{"key":"10.1016\/j.jbc.2026.113628_bib40","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1021\/bi00428a012","article-title":"Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement","volume":"28","author":"Chunduru","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113628_bib41","doi-asserted-by":"crossref","first-page":"14570","DOI":"10.1021\/jacs.5b08968","article-title":"A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis","volume":"137","author":"Huang","year":"2015","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.jbc.2026.113628_bib42","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1107\/S2059798318017795","article-title":"ZOO: an automatic data-collection system for high-throughput structure analysis in protein microcrystallography","volume":"75","author":"Hirata","year":"2019","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib43","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1107\/S2059798318004576","article-title":"KAMO: towards automated data processing for microcrystals","volume":"74","author":"Yamashita","year":"2018","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"10.1016\/j.jbc.2026.113628_bib44","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jbc.2026.113628_bib45","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444907050172","article-title":"BALBES: a molecular-replacement pipeline","volume":"64","author":"Long","year":"2008","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jbc.2026.113628_bib46","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":"10.1016\/j.jbc.2026.113628_bib47","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":"10.1016\/j.jbc.2026.113628_bib48","unstructured":"OEDocking 4.3.2.1. OpenEye, Cadence Molecular Sciences, Inc., Santa Fe, NM."},{"key":"10.1016\/j.jbc.2026.113628_bib49","unstructured":"OMEGA 6.1.0.1. OpenEye, Cadence Molecular Sciences, Santa Fe, NM."},{"key":"10.1016\/j.jbc.2026.113628_bib50","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1021\/ci100031x","article-title":"Conformer Generation with OMEGA: Algorithm and Validation Using High Quality Structures from the Protein Databank and Cambridge Structural Database","volume":"50","author":"Hawkins","year":"2010","journal-title":"J Chem Inf Model"},{"key":"10.1016\/j.jbc.2026.113628_bib51","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1021\/ci100436p","article-title":"FRED Pose Prediction and Virtual Screening Accuracy","volume":"51","author":"McGann","year":"2011","journal-title":"J Chem Inf Model"},{"key":"10.1016\/j.jbc.2026.113628_bib52","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1007\/s10822-012-9584-8","article-title":"FRED and HYBRID Docking Performance on Standardized Datasets","volume":"26","author":"McGann","year":"2012","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/j.jbc.2026.113628_bib53","doi-asserted-by":"crossref","first-page":"D457","DOI":"10.1093\/nar\/gkv1070","article-title":"KEGG as a reference resource for gene and protein annotation","volume":"44","author":"Kanehisa","year":"2016","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113628_bib54","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1016\/S0021-9258(18)64096-7","article-title":"The metabolism of hydroxypyruvate: I. The nonenzymatic decarboxylation and autoxidation of hydroxypyruvate","volume":"239","author":"Hedrick","year":"1961","journal-title":"J Biol Chem"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826025007?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826025007?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T22:43:48Z","timestamp":1793054628000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826025007"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":54,"alternative-id":["S0021925826025007"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113628","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural basis for oxidation-coupled isomerization by ApnO","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113628","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113628"}}