Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline (2E,6E,10E)-geranylgeranyl diphosphate Identifier CHEBI:58756 (Beilstein: 3574726) help_outline Charge -3 Formula C20H33O7P2 InChIKeyhelp_outline OINNEUNVOZHBOX-QIRCYJPOSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C\COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 55 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,085 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline tsukubadiene Identifier CHEBI:137528 Charge 0 Formula C20H32 InChIKeyhelp_outline JZGOFJIAHJJJDK-ICZJPRMTSA-N SMILEShelp_outline [H][C@@]12CC[C@H](C)\C1=C\[C@@]1(C)CCC(C)(C)[C@]1([H])C\C=C(C)/C2 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:53624 | RHEA:53625 | RHEA:53626 | RHEA:53627 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Novel terpenes generated by heterologous expression of bacterial terpene synthase genes in an engineered Streptomyces host.
Yamada Y., Arima S., Nagamitsu T., Johmoto K., Uekusa H., Eguchi T., Shin-ya K., Cane D.E., Ikeda H.
Mining of bacterial genome data has revealed numerous presumptive terpene synthases. Heterologous expression of several putative terpene synthase genes in an engineered Streptomyces host has revealed 13 newly discovered terpenes whose GC-MS and NMR data did not match with any known compounds in sp ... >> More
Mining of bacterial genome data has revealed numerous presumptive terpene synthases. Heterologous expression of several putative terpene synthase genes in an engineered Streptomyces host has revealed 13 newly discovered terpenes whose GC-MS and NMR data did not match with any known compounds in spectroscopic databases. Each of the genes encoding the corresponding terpene synthases were silent in their parent microorganisms. Heterologous expression and detailed NMR spectroscopic analysis allowed assignment of the structures of 13 new cyclic terpenes. Among these newly identified compounds, two were found to be linear triquinane sesquiterpenes that have never previously been isolated from bacteria or any other source. The remaining 11 new compounds were shown to be diterpene hydrocarbons and alcohol, including hydropyrene (1), hydropyrenol (2), tsukubadiene (11) and odyverdienes A (12) and B (13) each displaying a novel diterpene skeleton that had not previously been reported. << Less
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Mechanistic investigations of two bacterial diterpene cyclases: spiroviolene synthase and tsukubadiene synthase.
Rabe P., Rinkel J., Dolja E., Schmitz T., Nubbemeyer B., Luu T.H., Dickschat J.S.
The mechanisms of two diterpene cyclases from streptomycetes-one with an unknown product that was identified as the spirocyclic hydrocarbon spiroviolene and one with the known product tsukubadiene-were investigated in detail by isotope labeling experiments. Although the structures of the products ... >> More
The mechanisms of two diterpene cyclases from streptomycetes-one with an unknown product that was identified as the spirocyclic hydrocarbon spiroviolene and one with the known product tsukubadiene-were investigated in detail by isotope labeling experiments. Although the structures of the products were very different, the cyclization mechanisms of both enzymes proceed through the same initial cyclization reactions, before they diverge towards the individual products, which is reflected in the close phylogenetic relationship of the enzymes. << Less
Angew. Chem. Int. Ed. 56:2776-2779(2017) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.