{"entity": "researcher", "timestamp": "2026-09-23T08:25:50.054Z", "family": "Hamberger", "given": "Bj\u00f6rn", "initials": "B", "orcid": "0000-0003-1249-1807", "affiliations": ["Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.", "Center for Synthetic Biology \"bioSYNergy\", Copenhagen, Denmark."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/ace77139b1be4968ab60f3f0279753dd.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/ace77139b1be4968ab60f3f0279753dd"}}, "publications": [{"entity": "publication", "iuid": "f42927c624e8402a825ed6aeb3b18259", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/f42927c624e8402a825ed6aeb3b18259.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/f42927c624e8402a825ed6aeb3b18259"}}, "title": "Total biosynthesis of the cyclic AMP booster forskolin from Coleus forskohlii.", "authors": [{"family": "Pateraki", "given": "Irini", "initials": "I", "orcid": "0000-0002-7526-2334", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f381311f92a54a9f84e44b2fb109dca0.json"}}, {"family": "Andersen-Ranberg", "given": "Johan", "initials": "J"}, {"family": "Jensen", "given": "Niels Bjerg", "initials": "NB"}, {"family": "Wubshet", "given": "Sileshi Gizachew", "initials": "SG"}, {"family": "Heskes", "given": "Allison Maree", "initials": "AM", "orcid": "0000-0002-2732-5185", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e99a3bb8ac3b4d858d2d5aade3fe518d.json"}}, {"family": "Forman", "given": "Victor", "initials": "V"}, {"family": "Hallstr\u00f6m", "given": "Bj\u00f6rn", "initials": "B"}, {"family": "Hamberger", "given": "Britta", "initials": "B"}, {"family": "Motawia", "given": "Mohammed Saddik", "initials": "MS"}, {"family": "Olsen", "given": "Carl Erik", "initials": "CE"}, {"family": "Staerk", "given": "Dan", "initials": "D"}, {"family": "Hansen", "given": "J\u00f8rgen", "initials": "J"}, {"family": "M\u00f8ller", "given": "Birger Lindberg", "initials": "BL"}, {"family": "Hamberger", "given": "Bj\u00f6rn", "initials": "B", "orcid": "0000-0003-1249-1807", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ace77139b1be4968ab60f3f0279753dd.json"}}], "type": "journal article", "published": "2017-03-14", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "6", "issue": null, "issn-l": "2050-084X"}, "abstract": "Forskolin is a unique structurally complex labdane-type diterpenoid used in the treatment of glaucoma and heart failure based on its activity as a cyclic AMP booster. Commercial production of forskolin relies exclusively on extraction from its only known natural source, the plant Coleus forskohlii, in which forskolin accumulates in the root cork. Here, we report the discovery of five cytochrome P450s and two acetyltransferases which catalyze a cascade of reactions converting the forskolin precursor 13R-manoyl oxide into forskolin and a diverse array of additional labdane-type diterpenoids. A minimal set of three P450s in combination with a single acetyl transferase was identified that catalyzes the conversion of 13R-manoyl oxide into forskolin as demonstrated by transient expression in Nicotiana benthamiana. The entire pathway for forskolin production from glucose encompassing expression of nine genes was stably integrated into Saccharomyces cerevisiae and afforded forskolin titers of 40 mg/L.", "doi": "10.7554/eLife.23001", "pmid": "28290983", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5388535"}, {"db": "pii", "key": "e23001"}], "notes": [], "created": "2018-12-05T11:04:51.290Z", "modified": "2026-09-23T07:31:47.886Z"}, {"entity": "publication", "iuid": "11b5d6ca459744c281e2ab4723e14a58", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/11b5d6ca459744c281e2ab4723e14a58.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/11b5d6ca459744c281e2ab4723e14a58"}}, "title": "Oxidation and cyclization of casbene in the biosynthesis of Euphorbia factors from mature seeds of Euphorbia lathyris L.", "authors": [{"family": "Luo", "given": "Dan", "initials": "D"}, {"family": "Callari", "given": "Roberta", "initials": "R"}, {"family": "Hamberger", "given": "Britta", "initials": "B"}, {"family": "Wubshet", "given": "Sileshi Gizachew", "initials": "SG"}, {"family": "Nielsen", "given": "Morten T", "initials": "MT"}, {"family": "Andersen-Ranberg", "given": "Johan", "initials": "J"}, {"family": "Hallstr\u00f6m", "given": "Bj\u00f6rn M", "initials": "BM"}, {"family": "Cozzi", "given": "Federico", "initials": "F"}, {"family": "Heider", "given": "Harald", "initials": "H", "orcid": "0000-0002-3252-3119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1ecb1b56a03b4140a97d6593abed51f5.json"}}, {"family": "Lindberg M\u00f8ller", "given": "Birger", "initials": "B"}, {"family": "Staerk", "given": "Dan", "initials": "D", "orcid": "0000-0003-1249-1807", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ace77139b1be4968ab60f3f0279753dd.json"}}, {"family": "Hamberger", "given": "Bj\u00f6rn", "initials": "B"}], "type": "journal article", "published": "2016-08-23", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "113", "issue": "34", "pages": "E5082-E5089", "issn-l": "0027-8424"}, "abstract": "The seed oil of Euphorbia lathyris L. contains a series of macrocyclic diterpenoids known as Euphorbia factors. They are the current industrial source of ingenol mebutate, which is approved for the treatment of actinic keratosis, a precancerous skin condition. Here, we report an alcohol dehydrogenase-mediated cyclization step in the biosynthetic pathway of Euphorbia factors, illustrating the origin of the intramolecular carbon-carbon bonds present in lathyrane and ingenane diterpenoids. This unconventional cyclization describes the ring closure of the macrocyclic diterpene casbene. Through transcriptomic analysis of E. lathyris L. mature seeds and in planta functional characterization, we identified three enzymes involved in the cyclization route from casbene to jolkinol C, a lathyrane diterpene. These enzymes include two cytochromes P450 from the CYP71 clan and an alcohol dehydrogenase (ADH). CYP71D445 and CYP726A27 catalyze regio-specific 9-oxidation and 5-oxidation of casbene, respectively. When coupled with these P450-catalyzed monooxygenations, E. lathyris ADH1 catalyzes dehydrogenation of the hydroxyl groups, leading to the subsequent rearrangement and cyclization. The discovery of this nonconventional cyclization may provide the key link to complete elucidation of the biosynthetic pathways of ingenol mebutate and other bioactive macrocyclic diterpenoids.", "doi": "10.1073/pnas.1607504113", "pmid": "27506796", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5003294"}, {"db": "pii", "key": "1607504113"}, {"db": "GENBANK", "key": "KR350665"}, {"db": "GENBANK", "key": "KR350666"}, {"db": "GENBANK", "key": "KR350667"}, {"db": "GENBANK", "key": "KR350668"}, {"db": "GENBANK", "key": "KR350669"}, {"db": "GENBANK", "key": "KR350671"}, {"db": "GENBANK", "key": "KX428471"}], "notes": [], "created": "2018-12-05T09:44:37.321Z", "modified": "2026-09-23T07:43:30.904Z"}]}