{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T12:06:44Z","timestamp":1778933204917,"version":"3.51.4"},"reference-count":54,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,10,3]],"date-time":"2024-10-03T00:00:00Z","timestamp":1727913600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000288","name":"The Royal Society","doi-asserted-by":"publisher","award":["RGS\\u2216R1\\u2216231514"],"award-info":[{"award-number":["RGS\\u2216R1\\u2216231514"]}],"id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004815","name":"Isaac Newton Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004815","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010663","name":"European Research Council","doi-asserted-by":"publisher","award":["695669"],"award-info":[{"award-number":["695669"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/T003545\/1"],"award-info":[{"award-number":["BB\/T003545\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018693","name":"Horizon Europe","doi-asserted-by":"publisher","award":["101082304"],"award-info":[{"award-number":["101082304"]}],"id":[{"id":"10.13039\/100018693","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014013","name":"UK Research and Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014013","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000275","name":"Leverhulme Trust","doi-asserted-by":"publisher","award":["ECF-2020-694"],"award-info":[{"award-number":["ECF-2020-694"]}],"id":[{"id":"10.13039\/501100000275","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chem Catalysis"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1016\/j.checat.2024.101160","type":"journal-article","created":{"date-parts":[[2024,10,24]],"date-time":"2024-10-24T10:52:13Z","timestamp":1729767133000},"page":"101160","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Expanding the repertoire of imine reductases by mining divergent biosynthetic pathways for promiscuous reactivity"],"prefix":"10.1016","volume":"4","author":[{"given":"Godwin A.","family":"Aleku","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1367-6312","authenticated-orcid":false,"given":"Florian","family":"Hollfelder","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.checat.2024.101160_bib1","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1038\/nchem.2782","article-title":"A reductive aminase from Aspergillus oryzae","volume":"9","author":"Aleku","year":"2017","journal-title":"Nat. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib2","doi-asserted-by":"crossref","first-page":"4697","DOI":"10.1039\/D2SC00124A","article-title":"Reductive aminations by imine reductases: from milligrams to tons","volume":"13","author":"Gilio","year":"2022","journal-title":"Chem. Sci."},{"key":"10.1016\/j.checat.2024.101160_bib3","doi-asserted-by":"crossref","first-page":"6794","DOI":"10.1021\/acssuschemeng.2c01180","article-title":"Enzymatic N-Allylation of Primary and Secondary Amines Using Renewable Cinnamic Acids Enabled by Bacterial Reductive Aminases","volume":"10","author":"Aleku","year":"2022","journal-title":"ACS Sustain. Chem. Eng."},{"key":"10.1016\/j.checat.2024.101160_bib4","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1021\/jacs.8b11561","article-title":"Biocatalytic N-Alkylation of Amines Using Either Primary Alcohols or Carboxylic Acids via Reductive Aminase Cascades","volume":"141","author":"Ramsden","year":"2019","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.checat.2024.101160_bib5","doi-asserted-by":"crossref","first-page":"8263","DOI":"10.1021\/acscatal.7b02686","article-title":"Discovery, Engineering, and Synthetic Application of Transaminase Biocatalysts","volume":"7","author":"Slabu","year":"2017","journal-title":"ACS Catal."},{"key":"10.1016\/j.checat.2024.101160_bib6","doi-asserted-by":"crossref","first-page":"11857","DOI":"10.1021\/acs.chemrev.9b00383","article-title":"Reductive Amination in the Synthesis of Pharmaceuticals","volume":"119","author":"Afanasyev","year":"2019","journal-title":"Chem. Rev."},{"key":"10.1016\/j.checat.2024.101160_bib7","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1038\/s41929-019-0341-4","article-title":"Chiral synthesis of LSD1 inhibitor GSK2879552 enabled by directed evolution of an imine reductase","volume":"2","author":"Schober","year":"2019","journal-title":"Nat. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib8","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1038\/s41929-021-00671-5","article-title":"Biocatalytic reductive amination from discovery to commercial manufacturing applied to abrocitinib JAK1 inhibitor","volume":"4","author":"Kumar","year":"2021","journal-title":"Nat. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib9","doi-asserted-by":"crossref","first-page":"12433","DOI":"10.1021\/acscatal.1c02786","article-title":"Machine-Directed Evolution of an Imine Reductase for Activity and Stereoselectivity","volume":"11","author":"Ma","year":"2021","journal-title":"ACS Catal."},{"key":"10.1016\/j.checat.2024.101160_bib10","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1021\/acs.oprd.1c00255","article-title":"Application of Biocatalytic Reductive Amination for the Synthesis of a Key Intermediate to a CDK 2\/4\/6 Inhibitor","volume":"26","author":"Duan","year":"2022","journal-title":"Org. Process Res. Dev."},{"key":"10.1016\/j.checat.2024.101160_bib11","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aay9320","article-title":"Characterization of imine reductases in reductive amination for the exploration of structure-activity relationships","volume":"6","author":"Montgomery","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.checat.2024.101160_bib12","doi-asserted-by":"crossref","first-page":"2022","DOI":"10.1002\/cbic.201700257","article-title":"Photometric Characterization of the Reductive Amination Scope of the Imine Reductases from Streptomyces tsukubaensis and Streptomyces ipomoeae","volume":"18","author":"Matzel","year":"2017","journal-title":"Chembiochem"},{"key":"10.1016\/j.checat.2024.101160_bib13","doi-asserted-by":"crossref","first-page":"4533","DOI":"10.1039\/C0OB00353K","article-title":"Asymmetric synthesis of chiral cyclic amine from cyclic imine by bacterial whole-cell catalyst of enantioselective imine reductase","volume":"8","author":"Mitsukura","year":"2010","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib14","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1271\/bbb.110303","article-title":"Purification and Characterization of a Novel (R)-Imine Reductase from Streptomyces sp.","volume":"75","author":"Mitsukura","year":"2011","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.checat.2024.101160_bib15","doi-asserted-by":"crossref","first-page":"8079","DOI":"10.1007\/s00253-012-4629-4","article-title":"A NADPH-dependent (S)-imine reductase (SIR) from Streptomyces sp. GF3546 for asymmetric synthesis of optically active amines: purification, characterization, gene cloning, and expression","volume":"97","author":"Mitsukura","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.checat.2024.101160_bib16","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1002\/cctc.201701408","article-title":"Identification of Novel Bacterial Members of the Imine Reductase Enzyme Family that Perform Reductive Amination","volume":"10","author":"France","year":"2018","journal-title":"ChemCatChem"},{"key":"10.1016\/j.checat.2024.101160_bib17","doi-asserted-by":"crossref","first-page":"1692","DOI":"10.1002\/adsc.201500160","article-title":"Efficient Synthesis of Chiral Indolines using an Imine Reductase from Paenibacillus lactis","volume":"357","author":"Li","year":"2015","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib18","doi-asserted-by":"crossref","first-page":"4475","DOI":"10.1002\/cctc.201701379","article-title":"Efficient Biocatalytic Reductive Aminations by Extending the Imine Reductase Toolbox","volume":"9","author":"Roiban","year":"2017","journal-title":"ChemCatChem"},{"key":"10.1016\/j.checat.2024.101160_bib19","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1002\/cbic.201700261","article-title":"Extended Catalytic Scope of a Well-Known Enzyme: Asymmetric Reduction of Iminium Substrates by Glucose Dehydrogenase","volume":"18","author":"Roth","year":"2017","journal-title":"Chembiochem Eur. J. Chem. Biol"},{"key":"10.1016\/j.checat.2024.101160_bib20","doi-asserted-by":"crossref","first-page":"2201","DOI":"10.1002\/cbic.201402213","article-title":"Enzyme Toolbox: Novel Enantiocomplementary Imine Reductases","volume":"15","author":"Scheller","year":"2014","journal-title":"Chembiochem"},{"key":"10.1016\/j.checat.2024.101160_bib21","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1002\/cbic.201500218","article-title":"Expanding the Imine Reductase Toolbox by Exploring the Bacterial Protein-Sequence Space","volume":"16","author":"Wetzl","year":"2015","journal-title":"Chembiochem"},{"key":"10.1016\/j.checat.2024.101160_bib22","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1002\/adsc.201801326","article-title":"Imine Reductase-Catalyzed Enantioselective Reduction of Bulky \u03b1,\u03b2-Unsaturated Imines en Route to a Pharmaceutically Important Morphinan Skeleton","volume":"361","author":"Yao","year":"2019","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib23","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1002\/prot.25008","article-title":"Identification of imine reductase-specific sequence motifs","volume":"84","author":"Fademrecht","year":"2016","journal-title":"Proteins"},{"key":"10.1016\/j.checat.2024.101160_bib24","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1002\/adsc.202000094","article-title":"Metagenomic Mining for Amine Dehydrogenase Discovery","volume":"362","author":"Caparco","year":"2020","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib25","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/s41557-020-00606-w","article-title":"Screening and characterization of a diverse panel of metagenomic imine reductases for biocatalytic reductive amination","volume":"13","author":"Marshall","year":"2021","journal-title":"Nat. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib26","doi-asserted-by":"crossref","first-page":"3511","DOI":"10.1002\/cbic.202000526","article-title":"Engineering of Thermostable \u03b2-Hydroxyacid Dehydrogenase for the Asymmetric Reduction of Imines","volume":"21","author":"Stockinger","year":"2020","journal-title":"Chembiochem"},{"key":"10.1016\/j.checat.2024.101160_bib27","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1002\/cbic.201800291","article-title":"Exploiting the Catalytic Diversity of Short-Chain Dehydrogenases\/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope","volume":"19","author":"Roth","year":"2018","journal-title":"Chembiochem"},{"key":"10.1016\/j.checat.2024.101160_bib28","doi-asserted-by":"crossref","first-page":"12258","DOI":"10.1021\/jacs.9b03307","article-title":"An Asymmetric Reductase That Intercepts Acyclic Imino Acids Produced in Situ by a Partner Oxidase","volume":"141","author":"Guo","year":"2019","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.checat.2024.101160_bib29","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.cbpa.2016.11.022","article-title":"Imine reductases (IREDs)","volume":"37","author":"Mangas-Sanchez","year":"2017","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.checat.2024.101160_bib30","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1002\/adsc.201500213","article-title":"Biocatalytic Imine Reduction and Reductive Amination of Ketones","volume":"357","author":"Schrittwieser","year":"2015","journal-title":"Adv. Synth. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib31","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1038\/s41467-018-03841-5","article-title":"Enantioselective reduction of sulfur-containing cyclic imines through biocatalysis","volume":"9","author":"Zumbr\u00e4gel","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.checat.2024.101160_bib32","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.cbpa.2009.11.028","article-title":"What makes an enzyme promiscuous?","volume":"14","author":"Babtie","year":"2010","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.checat.2024.101160_bib33","doi-asserted-by":"crossref","first-page":"6032","DOI":"10.1002\/anie.200460416","article-title":"Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways","volume":"43","author":"Bornscheuer","year":"2004","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.checat.2024.101160_bib34","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-biochem-030409-143718","article-title":"Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective","volume":"79","author":"Tawfik","year":"2010","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.checat.2024.101160_bib35","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1038\/nchembio.1879","article-title":"Stereochemical inversion of (S)-reticuline by a cytochrome P450 fusion in opium poppy","volume":"11","author":"Farrow","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.checat.2024.101160_bib36","doi-asserted-by":"crossref","first-page":"16740","DOI":"10.1074\/jbc.M116.717827","article-title":"Identification of a Noroxomaritidine Reductase with Amaryllidaceae Alkaloid Biosynthesis Related Activities","volume":"291","author":"Kilgore","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib37","doi-asserted-by":"crossref","first-page":"4328","DOI":"10.1039\/c0ob01215g","article-title":"New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine","volume":"9","author":"Matuschek","year":"2011","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib38","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.chembiol.2015.02.006","article-title":"Unlocking the Diversity of Alkaloids in Catharanthus roseus: Nuclear Localization Suggests Metabolic Channeling in Secondary Metabolism","volume":"22","author":"Stavrinides","year":"2015","journal-title":"Chem. Biol."},{"key":"10.1016\/j.checat.2024.101160_bib39","doi-asserted-by":"crossref","first-page":"18397","DOI":"10.1074\/jbc.M109.088989","article-title":"Structure and Mechanism of Sanguinarine Reductase, an Enzyme of Alkaloid Detoxification","volume":"285","author":"Vogel","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib40","doi-asserted-by":"crossref","first-page":"7085","DOI":"10.1038\/s41467-021-27404-3","article-title":"Reductive inactivation of the hemiaminal pharmacophore for resistance against tetrahydroisoquinoline antibiotics","volume":"12","author":"Wen","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.checat.2024.101160_bib41","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1038\/s41586-019-1748-4","article-title":"Marine Proteobacteria metabolize glycolate via the \u03b2-hydroxyaspartate cycle","volume":"575","author":"Schada von Borzyskowski","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.checat.2024.101160_bib42","doi-asserted-by":"crossref","first-page":"2457","DOI":"10.1007\/s00726-015-2044-8","article-title":"Ketimine reductase\/CRYM catalyzes reductive alkylamination of \u03b1-keto acids, confirming its function as an imine reductase","volume":"47","author":"Hallen","year":"2015","journal-title":"Amino Acids"},{"key":"10.1016\/j.checat.2024.101160_bib43","doi-asserted-by":"crossref","first-page":"5329","DOI":"10.1074\/jbc.M411918200","article-title":"The putative malate\/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent delta1-piperideine-2-carboxylate\/delta1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline","volume":"280","author":"Muramatsu","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.checat.2024.101160_bib44","article-title":"Imine reduction by an Ornithine cyclodeaminase\/\u03bc-crystallin homolog purified from Candida parapsilosis ATCC 7330","volume":"31","author":"Uma Mahesh","year":"2021","journal-title":"Biotechnol. Rep."},{"key":"10.1016\/j.checat.2024.101160_bib45","doi-asserted-by":"crossref","first-page":"6044","DOI":"10.1021\/jacs.5b01968","article-title":"Targeted Metagenomics: Finding Rare Tryptophan Dimer Natural Products in the Environment","volume":"137","author":"Chang","year":"2015","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.checat.2024.101160_bib52","doi-asserted-by":"crossref","first-page":"4169","DOI":"10.1021\/acs.biochem.9b00735","article-title":"The EFI Web Resource for Genomic Enzymology Tools: Leveraging Protein, Genome, and Metagenome Databases to Discover Novel Enzymes and Metabolic Pathways","volume":"58","author":"Zallot","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.checat.2024.101160_bib53","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.1101\/gr.1239303","article-title":"Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks","volume":"13","author":"Shannon","year":"2003","journal-title":"Genome Res."},{"key":"10.1016\/j.checat.2024.101160_bib46","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/s41929-019-0249-z","article-title":"A family of native amine dehydrogenases for the asymmetric reductive amination of ketones","volume":"2","author":"Mayol","year":"2019","journal-title":"Nat. Catal."},{"key":"10.1016\/j.checat.2024.101160_bib47","doi-asserted-by":"crossref","first-page":"3880","DOI":"10.1021\/acscatal.6b00782","article-title":"Stereoselectivity and Structural Characterization of an Imine Reductase (IRED) from Amycolatopsis orientalis","volume":"6","author":"Aleku","year":"2016","journal-title":"ACS Catal."},{"key":"10.1016\/j.checat.2024.101160_bib48","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1038\/s41589-020-0603-0","article-title":"Enzymatic C\u2013H activation of aromatic compounds through CO\u00a02 fixation","volume":"16","author":"Aleku","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.checat.2024.101160_bib49","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/cssc.202100159","article-title":"Synthetic Enzyme-Catalyzed CO2 Fixation Reactions","volume":"14","author":"Aleku","year":"2021","journal-title":"ChemSusChem"},{"key":"10.1016\/j.checat.2024.101160_bib54","doi-asserted-by":"crossref","first-page":"14308","DOI":"10.1021\/acscatal.4c04756","article-title":"Imine Reductases and Reductive Aminases in Organic Synthesis","volume":"14","author":"Aleku","year":"2024","journal-title":"ACS Catal"},{"key":"10.1016\/j.checat.2024.101160_bib50","series-title":"Methods in Enzymology New Approaches\u00a0for Flavin Catalysis","first-page":"315","article-title":"Chapter Twelve - Exploring the sequence, function, and evolutionary space of protein superfamilies using sequence similarity networks and phylogenetic reconstructions","author":"Copp","year":"2019"},{"key":"10.1016\/j.checat.2024.101160_bib51","doi-asserted-by":"crossref","first-page":"5656","DOI":"10.1038\/s41467-021-25975-9","article-title":"Mapping the glycosyltransferase fold landscape using interpretable deep learning","volume":"12","author":"Taujale","year":"2021","journal-title":"Nat. Commun."}],"container-title":["Chem Catalysis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2667109324003531?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2667109324003531?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T11:07:15Z","timestamp":1778929635000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2667109324003531"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12]]},"references-count":54,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2024,12]]}},"alternative-id":["S2667109324003531"],"URL":"https:\/\/doi.org\/10.1016\/j.checat.2024.101160","relation":{},"ISSN":["2667-1093"],"issn-type":[{"value":"2667-1093","type":"print"}],"subject":[],"published":{"date-parts":[[2024,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Expanding the repertoire of imine reductases by mining divergent biosynthetic pathways for promiscuous reactivity","name":"articletitle","label":"Article Title"},{"value":"Chem Catalysis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.checat.2024.101160","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"101160"}}