{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T14:05:06Z","timestamp":1789567506623,"version":"build-2803163510"},"reference-count":26,"publisher":"American Chemical Society (ACS)","issue":"36","license":[{"start":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T00:00:00Z","timestamp":1788393600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T00:00:00Z","timestamp":1788393600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T00:00:00Z","timestamp":1788393600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM147018"],"award-info":[{"award-number":["R35 GM147018"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["00006628"],"award-info":[{"award-number":["00006628"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"PharmaScienceHub","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Chorismate is an important precursor of many primary and secondary metabolites. Enzymes that can transform chorismate are therefore useful biocatalysts for constructing bioactive molecules, yet the scope of known chorismate biochemistry is limited. Here, we identify TunB, an enzyme that catalyzes an intermolecular carbon\u2013carbon bond formation with chorismate in the absence of any cofactors. TunB is involved in the biosynthesis of tundrenone, a natural product produced by a methane-oxidizing bacterium, and was not predicted to use chorismate as a substrate on the basis of amino acid sequence homology. The discovery of the function of TunB therefore reveals an unexpected chorismate-converting enzyme that may enable the construction of additional scaffolds based on this important metabolite.<\/jats:p>","DOI":"10.1021\/jacs.6c09780","type":"journal-article","created":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T04:25:50Z","timestamp":1788495950000},"page":"38549-38554","source":"Crossref","is-referenced-by-count":0,"title":["Intermolecular\nCarbon\u2013Carbon Bond Formation\nby a Chorismate-Converting Enzyme"],"prefix":"10.1021","volume":"148","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4918-4595","authenticated-orcid":true,"given":"Rachel C.","family":"Hurrell","sequence":"first","affiliation":[{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]},{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iqra","family":"Ilyas","sequence":"additional","affiliation":[{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]},{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-0581-5976","authenticated-orcid":true,"given":"Maddox B.","family":"Riewald","sequence":"additional","affiliation":[{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]},{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Hubrich","sequence":"additional","affiliation":[{"name":"Saarland University , , , ,","place":["Saarbru\u0308cken, Germany, 66123"]},{"name":"Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz-Centre for Infection Research (HZI) , , , ,","place":["Saarbru\u0308cken, Germany, 66123"]},{"name":"Saarland University , , , ,","place":["Saarbru\u0308cken, Germany, 66123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6378-678X","authenticated-orcid":true,"given":"Aaron W.","family":"Puri","sequence":"additional","affiliation":[{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]},{"name":"University of Utah , , , ,","place":["Salt Lake City, Utah, United States, 84112"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,3]]},"reference":[{"key":"2026091609115461900_cit1","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1039\/D3NP00037K","article-title":"The Shikimate Pathway: Gateway to\nMetabolic Diversity","volume":"41","author":"Shende","year":"2024","journal-title":"Nat. Prod. Rep."},{"issue":"20","key":"2026091609115461900_cit2","doi-asserted-by":"publisher","first-page":"2441","DOI":"10.1039\/D0CC08078K","article-title":"Chorismate- and Isochorismate Converting\nEnzymes: Versatile Catalysts Acting on an Important Metabolic Node","volume":"57","author":"Hubrich","year":"2021","journal-title":"Chem. Commun."},{"issue":"12","key":"2026091609115461900_cit3","doi-asserted-by":"publisher","first-page":"4776","DOI":"10.1073\/pnas.1015773108","article-title":"Biosynthesis\nof the Immunosuppressants FK506, FK520, and Rapamycin Involves a Previously\nUndescribed Family of Enzymes Acting on Chorismate","volume":"108","author":"Andexer","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"2026091609115461900_cit4","doi-asserted-by":"publisher","first-page":"494","DOI":"10.1073\/pnas.0708750105","article-title":"Biosynthesis of the\nEnediyne Antitumor Antibiotic C-1027 Involves a New Branching Point\nin Chorismate Metabolism","volume":"105","author":"Van Lanen","year":"2008","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"issue":"28","key":"2026091609115461900_cit5","doi-asserted-by":"publisher","first-page":"8495","DOI":"10.1021\/bi970453p","article-title":"Enterobactin Biosynthesis in Escherichia coli: Isochorismate Lyase (EntB) Is a Bifunctional\nEnzyme That Is Phosphopantetheinylated by EntD and Then Acylated by\nEntE Using ATP and 2,3-Dihydroxybenzoate","volume":"36","author":"Gehring","year":"1997","journal-title":"Biochemistry"},{"issue":"6","key":"2026091609115461900_cit6","doi-asserted-by":"publisher","first-page":"1496","DOI":"10.1073\/pnas.0308331100","article-title":"Folate Synthesis\nin Plants: The p-Aminobenzoate Branch Is Initiated\nby a Bifunctional PabA-PabB Protein That Is Targeted to Plastids","volume":"101","author":"Basset","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. 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Chem."},{"issue":"7397","key":"2026091609115461900_cit10","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1038\/nature11117","article-title":"Engineering the Third\nWave of Biocatalysis","volume":"485","author":"Bornscheuer","year":"2012","journal-title":"Nature"},{"issue":"6","key":"2026091609115461900_cit11","doi-asserted-by":"publisher","first-page":"2002","DOI":"10.1021\/jacs.7b12240","article-title":"Tundrenone: An Atypical\nSecondary\nMetabolite from Bacteria with Highly Restricted Primary Metabolism","volume":"140","author":"Puri","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"2026091609115461900_cit12","doi-asserted-by":"publisher","first-page":"Ahead of print","DOI":"10.1039\/d6np00014b","article-title":"Inverse Stable Isotopic\nLabeling for Natural Product\nCharacterization and Discovery","author":"Robes","year":"2026","journal-title":"Nat. Prod. 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Microbiol.\nBiotechnol."},{"issue":"19","key":"2026091609115461900_cit15","doi-asserted-by":"publisher","first-page":"4348","DOI":"10.1021\/bi00690a032","article-title":"Uncatalyzed Rates of Enolization\nof Dihydroxyacetone\nPhosphate and of Glyceraldehyde 3-Phosphate in Neutral Aqueous Solution.\nQuantitative Assessment of the Effectiveness of an Enzyme Catalyst","volume":"14","author":"Hall","year":"1975","journal-title":"Biochemistry"},{"issue":"11","key":"2026091609115461900_cit16","doi-asserted-by":"publisher","first-page":"2509","DOI":"10.1021\/acs.accounts.6b00414","article-title":"The Remarkable\nCharacter of Porphobilinogen Synthase","volume":"49","author":"Jaffe","year":"2016","journal-title":"Acc.\nChem. 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Chem."},{"issue":"19","key":"2026091609115461900_cit24","doi-asserted-by":"publisher","first-page":"2997","DOI":"10.1021\/acs.biochem.5b00176","article-title":"Mechanism\nof the Enzymatic Synthesis of 4-(Hydroxymethyl)-2-Furancarboxaldehyde-Phosphate\n(4-HFC-P) from Glyceraldehyde-3-Phosphate Catalyzed by 4-HFC-P Synthase","volume":"54","author":"Wang","year":"2015","journal-title":"Biochemistry"},{"issue":"5\u20136","key":"2026091609115461900_cit25","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1006\/bioo.1997.1073","article-title":"Efficient in vivo Synthesis and Rapid Purification of Chorismic Acid\nUsing an Engineered Escherichia coli Strain","volume":"25","author":"Grisostomi","year":"1997","journal-title":"Bioorganic Chem."},{"issue":"5509","key":"2026091609115461900_cit26","doi-asserted-by":"publisher","first-page":"1790","DOI":"10.1126\/science.1058092","article-title":"Biosynthesis\nof Complex Polyketides in a Metabolically Engineered Strain of E. coli","volume":"291","author":"Pfeifer","year":"2001","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.6c09780","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/148\/36\/38549\/68332789\/jacs.6c09780.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jacsat\/article-pdf\/148\/36\/38549\/68332789\/jacs.6c09780.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T13:16:48Z","timestamp":1789564608000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jacsat\/article\/148\/36\/38549\/5416594\/Intermolecular-Carbon-Carbon-Bond-Formation-by-a"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,3]]},"references-count":26,"journal-issue":{"issue":"36","published-online":{"date-parts":[[2026,9,3]]},"published-print":{"date-parts":[[2026,9,16]]}},"URL":"https:\/\/doi.org\/10.1021\/jacs.6c09780","relation":{"has-preprint":[{"id-type":"doi","id":"10.26434\/chemrxiv.15002986\/v1","asserted-by":"object"}]},"ISSN":["0002-7863","1520-5126"],"issn-type":[{"value":"0002-7863","type":"print"},{"value":"1520-5126","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,3]]}}}