{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T09:25:54Z","timestamp":1790673954343,"version":"4.1.0"},"reference-count":52,"publisher":"American Chemical Society (ACS)","issue":"32","license":[{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T00:00:00Z","timestamp":1786320000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100007249","name":"University of Minnesota","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007249","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM133475"],"award-info":[{"award-number":["R35 GM133475"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R37 GM058822"],"award-info":[{"award-number":["R37 GM058822"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Sinefungin is a potent nucleoside antimetabolite of S-adenosylmethionine (SAM). Since its discovery in the 1970s, sinefungin has generated significant scientific interest owing to its role as a bioisostere of SAM and its broad range of biological activities. Despite considerable efforts to uncover the enzymes responsible for sinefungin production in the following years, its biosynthesis remained unclear for decades. Here, we characterize the complete sinefungin biosynthetic gene cluster (sin BGC) from Streptomyces incarnatus NRRL 8089. In vitro and in vivo analyses support a recent finding that the defining carbon\u2013carbon (C\u2013C) bond is formed not by a long-hypothesized PLP-dependent process, but by a vitamin B12-dependent radical SAM enzyme. We provide direct mechanistic evidence, via isotope-labeled products, that the adenosyl group of sinefungin originates from adenosylcobalamin and is atypically consumed via a homolytic SH2 substitution reaction. We also characterize two peptide aminoacyl-tRNA ligases (PEARLs) that append alanines onto the nucleoside scaffold using tRNA-activated amino acids. The PEARLs act directly on small molecules rather than macromolecular substrates, with one PEARL capable of iterative elongation. In addition, we perform in-vitro substrate profiling of several sin BGC-encoded enzymes. We reveal that multiple enzymes show specificity toward phosphorylated intermediates, including the earliest-acting PEARL enzyme. These observations provide an explanation for a cryptic phosphorylation-dephosphorylation strategy observed in the pathway, as they prevent the formation of the highly toxic sinefungin inside the cell. Finally, we leverage these enzymes in a reduced multi-enzyme cascade to biosynthesize sinefungin. Together, these findings expand upon our current knowledge of radical-mediated C\u2013C bond formation and PEARL enzyme catalysis, unlocking biocatalytic possibilities to produce amino acid-nucleoside conjugates.<\/jats:p>","DOI":"10.1021\/jacs.6c10565","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T13:02:19Z","timestamp":1786366939000},"page":"34895-34906","source":"Crossref","is-referenced-by-count":1,"title":["Unconventional Biocatalytic\nStrategies Orchestrate\nthe Synthesis of the Nucleoside Analog Sinefungin"],"prefix":"10.1021","volume":"148","author":[{"given":"Chi-Fang","family":"Lee","sequence":"first","affiliation":[{"name":"University of Minnesota Twin Cities , , , ,","place":["St. Paul, Minnesota, United States, 55108"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tianhui H.","family":"Zhou","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-0684-8832","authenticated-orcid":true,"given":"Songyi","family":"Xue","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6657-271X","authenticated-orcid":true,"given":"Lingyang","family":"Zhu","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5467-7071","authenticated-orcid":true,"given":"Wilfred A.","family":"van der Donk","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]},{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]},{"name":"University of Illinois at Urbana-Champaign , , , ,","place":["Urbana, Illinois, United States, 61801"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0491-9618","authenticated-orcid":true,"given":"Michael F","family":"Freeman","sequence":"additional","affiliation":[{"name":"University of Minnesota Twin Cities , , , ,","place":["St. Paul, Minnesota, United States, 55108"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,10]]},"reference":[{"issue":"8","key":"2026081910231293400_cit1","doi-asserted-by":"publisher","first-page":"463","DOI":"10.7164\/antibiotics.26.463","article-title":"A9145, a New Adenine-Containing Antifungal Antibiotic\nI. Discovery and Isolation","volume":"26","author":"Hamill","year":"1973","journal-title":"J. Antibiot."},{"issue":"9","key":"2026081910231293400_cit2","doi-asserted-by":"publisher","first-page":"1521","DOI":"10.1039\/D2NP00086E","article-title":"S-Adenosylmethionine:\nMore than Just a Methyl Donor","volume":"40","author":"Lee","year":"2023","journal-title":"Nat. Prod. Rep."},{"issue":"4","key":"2026081910231293400_cit3","doi-asserted-by":"publisher","first-page":"1515","DOI":"10.1152\/physrev.00047.2011","article-title":"S-Adenosylmethionine in Liver Health,\nInjury, and Cancer","volume":"92","author":"Lu","year":"2012","journal-title":"Physiol. Rev."},{"key":"2026081910231293400_cit4","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1186\/1472-6807-5-19","article-title":"Natural History of S-Adenosylmethionine-Binding\nProteins","volume":"5","author":"Kozbial","year":"2005","journal-title":"BMC Struct. Biol."},{"issue":"3","key":"2026081910231293400_cit5","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1021\/acschembio.5b00812","article-title":"SAM\/SAH Analogs as Versatile Tools for SAM-Dependent\nMethyltransferases","volume":"11","author":"Zhang","year":"2016","journal-title":"ACS Chem. Biol."},{"issue":"8","key":"2026081910231293400_cit6","doi-asserted-by":"publisher","first-page":"466","DOI":"10.7164\/antibiotics.26.466","article-title":"A9145, a New Adenine-Containing\nAntifungal Antibiotic.\nII. Biological Activity","volume":"26","author":"Gordee","year":"1973","journal-title":"J. Antibiot."},{"issue":"9","key":"2026081910231293400_cit7","doi-asserted-by":"publisher","first-page":"4942","DOI":"10.3390\/app15094942","article-title":"The Impact of the S-Adenosylmethionine\nAnalogue Sinefungin on Viral Life Cycles","volume":"15","author":"Dell\u2019annunziata","year":"2025","journal-title":"Appl.\nSci."},{"issue":"43","key":"2026081910231293400_cit8","doi-asserted-by":"publisher","first-page":"18004","DOI":"10.1021\/ja307060p","article-title":"Sinefungin\nDerivatives as Inhibitors and Structure\nProbes of Protein Lysine Methyltransferase SETD2","volume":"134","author":"Zheng","year":"2012","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026081910231293400_cit9","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1042\/bj3050133","article-title":"Sinefungin\nShares AdoMet-Uptake System to Enter Leishmania donovani Promastigotes","volume":"305","author":"Phelouzat","year":"1995","journal-title":"Biochem. J."},{"issue":"1","key":"2026081910231293400_cit10","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/0014-4894(80)90010-7","article-title":"Plasmodium Falciparum: Antimalarial Activity in Culture of Sinefungin\nand Other Methylation Inhibitors","volume":"50","author":"Trager","year":"1980","journal-title":"Exp Parasitol."},{"issue":"3","key":"2026081910231293400_cit11","first-page":"255","article-title":"Evaluation\nof Sinefungin for the Treatment of Trypanosoma (Nannomonas) congolense Infections in Goats","volume":"37","author":"Zweygarth","year":"1986","journal-title":"Trop Med. Parasitol"},{"issue":"18","key":"2026081910231293400_cit12","doi-asserted-by":"publisher","first-page":"3957","DOI":"10.1021\/acs.orglett.4c01196","article-title":"Formal Synthesis of (+)-Sinefungin\nby Way of Sequential Asymmetric Metal Catalysis","volume":"26","author":"Dey","year":"2024","journal-title":"Org. Lett."},{"key":"2026081910231293400_cit13","unstructured":"Hamill, R. L.; Hoehn, M. M.\n          Antifungal\nantibiotic\nA-9145 and process for production thereof\n          EP 3,758,681 A1, 1973."},{"key":"2026081910231293400_cit14","unstructured":"Hamill, R. L.; Nagarajan, R.\n          Antifungal antibiotics\n          EP 4,087,603\nA1,1978."},{"key":"2026081910231293400_cit15","unstructured":"Florent, J.; Lunel, J.; Mancy, D.; Lactam, I.\n          \u03b1,\u03b4-Diaminoacid and its lactam\n          EP 4,189,349\nA1, 1980."},{"issue":"4","key":"2026081910231293400_cit16","doi-asserted-by":"publisher","first-page":"505","DOI":"10.7164\/antibiotics.40.505","article-title":"Biosynthesis of Sinefungin by Cell-Free\nExtract of Streptomyces incarnatus NRRL 8089","volume":"40","author":"Malina","year":"1987","journal-title":"J. Antibiot."},{"issue":"3","key":"2026081910231293400_cit17","doi-asserted-by":"publisher","first-page":"185","DOI":"10.7164\/antibiotics.31.185","article-title":"Incorporation of 14C-Labeled\nCompounds into\nSinefungin (A9145), a Nucleoside Antifungal Antibiotic","volume":"31","author":"Berry","year":"1978","journal-title":"J. Antibiot."},{"key":"2026081910231293400_cit18","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1007\/978-1-4612-5012-8_37","article-title":"Sinefungin and Derivatives:\nSynthesis, Biosynthesis and Molecular Target Studies in Leishmania","volume-title":"Biological Methylation and Drug Design","author":"Blanchard","year":"1986"},{"issue":"24","key":"2026081910231293400_cit19","doi-asserted-by":"publisher","first-page":"8981","DOI":"10.1021\/ja00206a066","article-title":"Biosynthesis of\nSinefungin: On the Mode of Incorporation of L-Ornithine","volume":"111","author":"Parry","year":"1989","journal-title":"J. Am. Chem. Soc."},{"issue":"5","key":"2026081910231293400_cit20","doi-asserted-by":"publisher","first-page":"1109","DOI":"10.1128\/aem.54.5.1109-1111.1988","article-title":"Regulation\nof Sinefungin Biosynthesis by the Wild-Type\nStrain and Mutants of Streptomyces incarnatus","volume":"54","author":"Malina","year":"1988","journal-title":"Appl. Environ. Microbiol."},{"issue":"31","key":"2026081910231293400_cit21","doi-asserted-by":"publisher","first-page":"6069","DOI":"10.1016\/S0040-4020(01)86497-8","article-title":"The Biosynthesis of\nSinefungin: Investigations Using a Cell-Free\nSystem","volume":"47","author":"Parry","year":"1991","journal-title":"Tetrahedron"},{"issue":"4","key":"2026081910231293400_cit22","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1128\/genomeA.00715-15","article-title":"Draft Genome\nSequence of Streptomyces incarnatus NRRL8089, Which\nProduces the Nucleoside\nAntibiotic Sinefungin","volume":"3","author":"Oshima","year":"2015","journal-title":"Genome Announc."},{"issue":"20","key":"2026081910231293400_cit23","doi-asserted-by":"publisher","first-page":"20343","DOI":"10.1021\/jacs.6c05246","article-title":"Sinefungin\nBiosynthesis Employs a B12-Dependent Radical S-Adenosyl-l-methionine Enzyme Catalyzing C-Adenosylation\nof Arginine","volume":"148","author":"Ueno","year":"2026","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"2026081910231293400_cit24","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1152\/physrev.00037.2016","article-title":"Arginase: A Multifaceted\nEnzyme Important in Health\nand Disease","volume":"98","author":"Caldwell","year":"2018","journal-title":"Physiol. Rev."},{"issue":"29","key":"2026081910231293400_cit25","doi-asserted-by":"publisher","first-page":"11763","DOI":"10.1002\/anie.201916321","article-title":"Landornamides: Antiviral\nOrnithine-containing Ribosomal Peptides Discovered through Genome\nMining","volume":"59","author":"Bo\u0308sch","year":"2020","journal-title":"Angew. Chem., Int. Ed."},{"issue":"2","key":"2026081910231293400_cit26","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1111\/j.1365-2958.1995.tb02295.x","article-title":"A Family of Bacteriocin ABC Transporters\nCarry out Proteolytic Processing of Their Substrates Concomitant with\nExport","volume":"16","author":"H\u00e5varstein","year":"1995","journal-title":"Mol. Microbiol."},{"issue":"9","key":"2026081910231293400_cit27","doi-asserted-by":"publisher","first-page":"1425","DOI":"10.1016\/j.peptides.2003.10.028","article-title":"Peptide Signal Molecules and Bacteriocins\nin Gram-Negative Bacteria: A Genome-Wide in Silico Screening for Peptides\nContaining a Double-Glycine Leader Sequence and Their Cognate Transporters","volume":"25","author":"Dirix","year":"2004","journal-title":"Peptides"},{"issue":"1","key":"2026081910231293400_cit28","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1039\/D0NP00027B","article-title":"New Developments in RiPP Discovery, Enzymology and\nEngineering","volume":"38","author":"Montalba\u0301n-Lo\u0301pez","year":"2021","journal-title":"Nat. Prod. Rep."},{"issue":"11","key":"2026081910231293400_cit29","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/ja.2010.102","article-title":"Sinefungin\nVA and Dehydrosinefungin\nV, New Antitrypanosomal Antibiotics Produced by Streptomyces sp. K05-0178","volume":"63","author":"Niitsuma","year":"2010","journal-title":"J. Antibiot."},{"issue":"6450","key":"2026081910231293400_cit30","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1126\/science.aau6232","article-title":"Use of\na Scaffold Peptide in the Biosynthesis of Amino\nAcid\u2013Derived Natural Products","volume":"365","author":"Ting","year":"2019","journal-title":"Science"},{"issue":"6","key":"2026081910231293400_cit31","doi-asserted-by":"publisher","first-page":"1242","DOI":"10.1021\/acscentsci.4c00044","article-title":"PEARL-Catalyzed Peptide Bond Formation after Chain\nReversal by Ureido-Forming Condensation Domains","volume":"10","author":"Yu","year":"2024","journal-title":"ACS Cent. Sci."},{"issue":"2","key":"2026081910231293400_cit32","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1038\/s41589-020-00656-8","article-title":"Cryptic Phosphorylation\nin Nucleoside Natural Product Biosynthesis","volume":"17","author":"Draelos","year":"2021","journal-title":"Nat. Chem. Biol."},{"issue":"12","key":"2026081910231293400_cit33","doi-asserted-by":"publisher","first-page":"2017","DOI":"10.1073\/pnas.2423858122","article-title":"Substrate\nRecognition by a Peptide-Aminoacyl-tRNA\nLigase","volume":"122","author":"Ramos-Figueroa","year":"2025","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"20","key":"2026081910231293400_cit34","doi-asserted-by":"publisher","first-page":"14235","DOI":"10.1021\/jacs.4c03677","article-title":"Unexpected\nTransformations during Pyrroloiminoquinone Biosynthesis","volume":"146","author":"Ramos Figueroa","year":"2024","journal-title":"J. Am. Chem. Soc."},{"issue":"4","key":"2026081910231293400_cit35","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1099\/00221287-131-4-775","article-title":"Mechanism\nof Action of Nikkomycin\nand the Peptide Transport System of Candida albicans","volume":"131","author":"McCarthy","year":"1985","journal-title":"J. Gen. Microbiol."},{"issue":"2","key":"2026081910231293400_cit36","doi-asserted-by":"publisher","first-page":"281","DOI":"10.2217\/fmb.11.148","article-title":"Microcin C Biosynthesis\nand Mechanisms of Bacterial\nResistance","volume":"7","author":"Severinov","year":"2012","journal-title":"Future Microbiol."},{"issue":"3","key":"2026081910231293400_cit37","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1128\/AAC.25.3.373","article-title":"Anti-Candida Activity\nof Polyoxin: Example of Peptide Transport in Yeasts","volume":"25","author":"Mehta","year":"1984","journal-title":"Antimicrob. Agents Chemother"},{"issue":"3","key":"2026081910231293400_cit38","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1021\/acsbiomedchemau.1c00051","article-title":"Cobalamin-Dependent\nRadical S-Adenosylmethionine Enzymes:\nCapitalizing on Old Motifs for New Functions","volume":"2","author":"Bridwell-Rabb","year":"2022","journal-title":"ACS Bio Med Chem Au."},{"issue":"11","key":"2026081910231293400_cit39","doi-asserted-by":"publisher","first-page":"1154","DOI":"10.1016\/j.bbapap.2012.03.012","article-title":"Adenosylcobalamin\nEnzymes: Theory\nand Experiment Begin to Converge","volume":"1824","author":"Marsh","year":"2012","journal-title":"Biochim. Biophys.\nActa"},{"issue":"1","key":"2026081910231293400_cit40","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1007\/s00253-010-2773-2","article-title":"Multiple Roles of ATP:\nCob(I)Alamin\nAdenosyltransferases in the Conversion of B12 to Coenzyme\nB12","volume":"88","author":"Mera","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"1","key":"2026081910231293400_cit41","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1186\/1471-2164-15-97","article-title":"Insights into Naturally Minimised Streptomyces albus J1074 Genome","volume":"15","author":"Zaburannyi","year":"2014","journal-title":"BMC Genomics"},{"key":"2026081910231293400_cit42","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/bs.mie.2021.09.013","article-title":"A Method for the Efficient\nAdenosylation of Corrinoids","volume":"668","author":"Costa","year":"2022","journal-title":"Methods Enzymol."},{"issue":"21","key":"2026081910231293400_cit43","doi-asserted-by":"publisher","first-page":"13264","DOI":"10.1074\/jbc.273.21.13264","article-title":"Assembly of Iron-Sulfur\nClusters. Identification on an iscSUA-HscBA-Fdx Gene\nCluster from Azotobacter vinelandii","volume":"273","author":"Zheng","year":"1998","journal-title":"J. Biol. Chem."},{"issue":"32","key":"2026081910231293400_cit44","doi-asserted-by":"publisher","first-page":"28380","DOI":"10.1074\/jbc.C200365200","article-title":"A Third Bacterial System\nfor the Assembly of Iron-Sulfur\nClusters with Homologs in Archaea and Plastids","volume":"277","author":"Takahashi","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"9","key":"2026081910231293400_cit45","doi-asserted-by":"publisher","first-page":"1475","DOI":"10.1021\/acs.biochem.7b01205","article-title":"Enhanced Solubilization of Class\nB Radical S-Adenosylmethionine Methylases by Improved\nCobalamin Uptake in Escherichia coli","volume":"57","author":"Lanz","year":"2018","journal-title":"Biochemistry"},{"issue":"11","key":"2026081910231293400_cit46","doi-asserted-by":"publisher","first-page":"5087","DOI":"10.1021\/jacs.1c13706","article-title":"Mechanism of Radical S-Adenosyl-l-Methionine Adenosylation:\nRadical Intermediates\nand the Catalytic Competence of the 5\u2032-Deoxyadenosyl Radical","volume":"144","author":"Lundahl","year":"2022","journal-title":"J. Am. Chem. Soc."},{"issue":"6465","key":"2026081910231293400_cit47","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1126\/science.aay0934","article-title":"Itaconyl-CoA Forms a Stable Biradical in Methylmalonyl-CoA\nMutase and Derails Its Activity and Repair","volume":"366","author":"Ruetz","year":"2019","journal-title":"Science"},{"issue":"12","key":"2026081910231293400_cit48","doi-asserted-by":"publisher","first-page":"1523","DOI":"10.1016\/j.chembiol.2013.10.011","article-title":"Core Assembly Mechanism\nof Quinocarcin\/SF-1739: Bimodular Complex Nonribosomal Peptide Synthetases\nfor Sequential Mannich-Type Reactions","volume":"20","author":"Hiratsuka","year":"2013","journal-title":"Chem.\nBiol."},{"issue":"3","key":"2026081910231293400_cit49","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1038\/nchembio.2009","article-title":"A Pyridoxal\nPhosphate\u2013Dependent\nEnzyme That Oxidizes an Unactivated Carbon-Carbon Bond","volume":"12","author":"Du","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"2026081910231293400_cit50","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fbioe.2020.500867","article-title":"Recent\nProgress in the Understanding and Engineering of Coenzyme B12-Dependent Glycerol Dehydratase","volume":"8","author":"Nasir","year":"2020","journal-title":"Front. Bioeng.\nBiotechnol."},{"issue":"17","key":"2026081910231293400_cit51","doi-asserted-by":"publisher","first-page":"3637","DOI":"10.1039\/C4CC08478K","article-title":"Rationally\nEngineered Variants of S-Adenosylmethionine (SAM)\nSynthase: Reduced Product Inhibition and\nSynthesis of Artificial Cofactor Homologues","volume":"51","author":"Dippe","year":"2015","journal-title":"Chem. Commun."},{"issue":"6572","key":"2026081910231293400_cit52","doi-asserted-by":"publisher","first-page":"1258","DOI":"10.1126\/science.abl4322","article-title":"A Biomimetic\nSH Cross-Coupling Mechanism\nfor Quaternary sp3-Carbon Formation","volume":"374","author":"Liu","year":"2021","journal-title":"Science"}],"container-title":["Journal of the American\nChemical Society"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.6c10565","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/148\/32\/34895\/66471962\/jacs.6c10565.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/148\/32\/34895\/66471962\/jacs.6c10565.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T14:45:09Z","timestamp":1787150709000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jacsat\/article\/148\/32\/34895\/5251149\/Unconventional-Biocatalytic-Strategies-Orchestrate"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,10]]},"references-count":52,"journal-issue":{"issue":"32","published-online":{"date-parts":[[2026,8,10]]},"published-print":{"date-parts":[[2026,8,19]]}},"URL":"https:\/\/doi.org\/10.1021\/jacs.6c10565","relation":{},"ISSN":["0002-7863","1520-5126"],"issn-type":[{"value":"0002-7863","type":"print"},{"value":"1520-5126","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,10]]}}}