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(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene |
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CHEBI:138307 |
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(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene |
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A squalene triterpenoid obtained by epoxidation accross the 2,3- and 22,23-double bonds of squalene. |
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This entity has been manually annotated by the ChEBI Team.
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Kristian Axelsen
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ZINC000013509871 |
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Molfile
XML
SDF
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InChI=1S/C30H50O2/c1-23(15-11-17-25(3)19-21-27-29(5,6)31-27)13-9-10-14-24(2)16-12-18-26(4)20-22-28-30(7,8)32-28/h13-14,17-18,27-28H,9-12,15-16,19-22H2,1-8H3/b23-13+,24-14+,25-17+,26-18+/t27-,28-/m0/s1 |
KABSNIWLJXCBGG-OQSIWNGOSA-N |
C(C/C=C(/CC/C=C(/CC[C@H]1C(O1)(C)C)\C)\C)/C=C(/CC/C=C(/CC[C@H]2C(O2)(C)C)\C)\C |
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Lycopodium clavatum
(NCBI:txid3252)
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See:
PubMed
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plant metabolite
Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
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View more via ChEBI Ontology
Outgoing
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(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene
(CHEBI:138307)
has role
plant metabolite
(CHEBI:76924)
(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene
(CHEBI:138307)
is a
epoxide
(CHEBI:32955)
(3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene
(CHEBI:138307)
is a
squalene triterpenoid
(CHEBI:26747)
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(2S,2'S)-2,2'-[(3E,7E,11E,15E)-3,7,12,16-tetramethyloctadeca-3,7,11,15-tetraene-1,18-diyl]bis(3,3-dimethyloxirane)
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(3S,22S)-2,3:22,23-diepoxysqualene
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UniProt
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(3S,22S)-2,3:22,23-dioxidosqualene
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ChEBI
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8657029
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Reaxys Registry Number
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Reaxys
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Araki T, Saga Y, Marugami M, Otaka J, Araya H, Saito K, Yamazaki M, Suzuki H, Kushiro T (2016) Onocerin Biosynthesis Requires Two Highly Dedicated Triterpene Cyclases in a Fern Lycopodium clavatum. Chembiochem : a European journal of chemical biology 17, 288-290 (Source: SUBMITTER) [PubMed:26663356] [show Abstract] Onocerin is known for its unusual structure among triterpenoids, with a symmetrical structure that is formed by cyclizations at the both termini of dioxidosqualene. The nature of the enzyme catalyzing these unusual cyclizations has remained elusive for decades. Here, we report the cloning of genes responsible for these reactions; they exhibited unprecedented substrate specificities among oxidosqualene cyclase family members. Two genes, LCC and LCD, were identified from the fern Lycopodium clavatum. Expression in yeast revealed that both were required to produce α-onocerin. LCC, the first dioxidosqualene cyclase, catalyzed the production of a novel intermediate pre-α-onocerin from only dioxidosqualene as a substrate; LCD catalyzed the second half of the cyclization, exclusively from pre-α-onocerin. These results demonstrated that these two most unusual oxidosqualene cyclases were involved in onocerin biosynthesis. | Abe I, Abe T, Lou W, Masuoka T, Noguchi H (2007) Site-directed mutagenesis of conserved aromatic residues in rat squalene epoxidase. Biochemical and biophysical research communications 352, 259-263 [PubMed:17112472] [show Abstract] Squalene epoxidase catalyzes the conversion of squalene to (3S)2,3-oxidosqualene, which is a rate-limiting step of the cholesterol biogenesis. To evaluate the importance of conserved aromatic residues, 15 alanine-substituted mutants were constructed and tested for the enzyme activity. Except F203A, all the mutants significantly lost the enzyme activity, confirming the importance of the residues, either for correct folding of the protein, or for the catalytic machinery of the enzyme. Further, interestingly, F223A mutant no longer accepted (3S)2,3-oxidosqualene as a substrate, while Y473A mutant converted (3S)2,3-oxidosqualene to (3S,22S)2,3:22,23-dioxidosqualene twice more efficiently than wild-type enzyme. It is remarkable that the single amino acid replacement yielded mutants with altered substrate and product specificities. These aromatic residues are likely to be located at the substrate-binding domain of the active-site, and control the stereochemical course of the enzyme reaction. | Shan H, Segura MJ, Wilson WK, Lodeiro S, Matsuda SP (2005) Enzymatic cyclization of dioxidosqualene to heterocyclic triterpenes. Journal of the American Chemical Society 127, 18008-18009 [PubMed:16366544] [show Abstract] Oxidosqualene cyclases normally produce triterpenes from 2,3-(S)-oxidosqualene (OS) but also can cyclize its minor companion (3S,22S)-2,3:22,23-dioxidosqualene (DOS). We explored DOS cyclization in plant triterpene synthesis using a recombinant lupeol synthase (LUP1) heterologously expressed in yeast. Incubation of LUP1 with 3S,22S-DOS gave epoxydammaranes epimeric at C20 and a 17,24-epoxybaccharane in a 4:2:3 ratio. The products reflected a new mechanistic paradigm for DOS cyclization. The structures were determined by NMR and GC-MS, and recent errors in the epoxydammarane literature were rectified. Some DOS metabolites are likely candidates for regulating triterpenoid biosynthesis, while others may be precursors of saponin aglycones. Our in vivo experiments in yeast generated substantial amounts of DOS metabolites in a single enzymatic step, suggesting a seminal role for the DOS shunt pathway in the evolution of saponin synthesis. Quantum mechanical calculations revealed oxonium ion intermediates, whose reactivity altered the usual mechanistic patterns of triterpene synthesis. Further analysis indicated that the side chain of the epoxydammarenyl cation intermediate is in an extended conformation. The overall results establish new roles for DOS in triterpene synthesis and exemplify how organisms can increase the diversity of secondary metabolites without constructing new enzymes. |
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