InChI=1S/C20H32/c1-13-8-9-20-14(2)6-7-15(20)17-18(3,4)10-11-19(17,5)12-16(13)20/h14-15,17H,6-12H2,1-5H3/t14-,15-,17+,19+,20-/m0/s1 |
GQNONAWUSDSPNL-ZLOLBAIHSA-N |
[H][C@@]12CC[C@H](C)[C@@]11CCC(C)=C1C[C@@]1(C)CCC(C)(C)[C@@]21[H] |
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Kutzneria kofuensis
(NCBI:txid103725)
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of strain
DSM 43851
See:
PubMed
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Allokutzneria albata
(NCBI:txid211114)
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See:
PubMed
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bacterial metabolite
Any prokaryotic metabolite produced during a metabolic reaction in bacteria.
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View more via ChEBI Ontology
(3S,3aS,7aR,10aR,10bS)-3,6,7a,10,10-pentamethyl-1,2,3,4,5,7,7a,8,9,10,10a,10b-dodecahydrocyclopenta[d]-s-indacene
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Chhalodia AK, Xu H, Tabekoueng GB, Gu B, Taizoumbe KA, Lauterbach L, Dickschat JS (2023) Functional characterisation of twelve terpene synthases from actinobacteria. Beilstein journal of organic chemistry 19, 1386-1398 [PubMed:37736393] [show Abstract] Fifteen type I terpene synthase homologs from diverse actinobacteria that were selected based on a phylogenetic analysis of more than 4000 amino acid sequences were investigated for their products. For four enzymes with functions not previously reported from bacterial terpene synthases the products were isolated and their structures were elucidated by NMR spectroscopy, resulting in the discovery of the first terpene synthases for (+)-δ-cadinol and (+)-α-cadinene, besides the first two bacterial (-)-amorpha-4,11-diene synthases. For other terpene synthases with functions reported from bacteria before the products were identified by GC-MS. The characterised enzymes include a new epi-isozizaene synthase with monoterpene synthase side activity, a 7-epi-α-eudesmol synthase that also produces hedycaryol and germacrene A, and four more sesquiterpene synthases that produce mixtures of hedycaryol and germacrene A. Three phylogenetically related enzymes were in one case not expressed and in two cases inactive, suggesting pseudogenisation in the respective branch of the phylogenetic tree. Furthermore, a diterpene synthase for allokutznerene and a sesterterpene synthase for sesterviolene were identified. | Rinkel J, Steiner ST, Bian G, Chen R, Liu T, Dickschat JS (2020) A Family of Related Fungal and Bacterial Di- and Sesterterpenes: Studies on Fusaterpenol and Variediene. Chembiochem : a European journal of chemical biology 21, 486-491 [PubMed:31476106] [show Abstract] The absolute configuration of fusaterpenol (GJ1012E) has been revised by an enantioselective deuteration strategy. A bifunctional enzyme with a terpene synthase and a prenyltransferase domain from Aspergillus brasiliensis was characterised as variediene synthase, and the absolute configuration of its product was elucidated. The uniform absolute configurations of these and structurally related di- and sesterterpenes together with a common stereochemical course for the geminal methyl groups of GGPP unravel a similar conformational fold of the substrate in the active sites of the terpene synthases. For variediene, a thermal reaction observed during GC/MS analysis was studied in detail for which a surprising mechanism was uncovered. | Lauterbach L, Rinkel J, Dickschat JS (2018) Two Bacterial Diterpene Synthases from Allokutzneria albata Produce Bonnadiene, Phomopsene, and Allokutznerene. Angewandte Chemie (International ed. in English) 57, 8280-8283 [PubMed:29758116] [show Abstract] Two diterpene synthases from Allokutzneria albata were studied for their products, resulting in the identification of the new compound bonnadiene from the first enzyme. Although phylogenetically unrelated to fungal phomopsene synthase, the second enzyme produced a mixture of phomopsene and a biosynthetically linked new compound, allokutznerene, as well as spiroviolene. Both enzymes were subjected to in-depth mechanistic studies involving isotopic labelling experiments, metal-cofactor variation, and site-directed mutagenesis. Oxidation products of phomopsene and allokutznerene are also discussed. |
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