Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (2E)-geranyl diphosphate Identifier CHEBI:58057 (Beilstein: 4549979) help_outline Charge -3 Formula C10H17O7P2 InChIKeyhelp_outline GVVPGTZRZFNKDS-JXMROGBWSA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 59 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline isopentenyl diphosphate Identifier CHEBI:128769 (Beilstein: 1824090) help_outline Charge -3 Formula C5H9O7P2 InChIKeyhelp_outline NUHSROFQTUXZQQ-UHFFFAOYSA-K SMILEShelp_outline CC(=C)CCOP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E,6E,10E,14E)-geranylfarnesyl diphosphate Identifier CHEBI:57907 Charge -3 Formula C25H41O7P2 InChIKeyhelp_outline JMVSBFJBMXQNJW-GIXZANJISA-K SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\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 18 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
Cross-references
| RHEA:66856 | RHEA:66857 | RHEA:66858 | RHEA:66859 | |
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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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A geranylfarnesyl diphosphate synthase provides the precursor for sesterterpenoid (C25) formation in the glandular trichomes of the mint species Leucosceptrum canum.
Liu Y., Luo S.-H., Schmidt A., Wang G.-D., Sun G.-L., Grant M., Kuang C., Yang M.-J., Jing S.-X., Li C.-H., Schneider B., Gershenzon J., Li S.-H.
Plant sesterterpenoids, an important class of terpenoids, are widely distributed in various plants, including food crops. However, little is known about their biosynthesis. Here, we cloned and functionally characterized a plant geranylfarnesyl diphosphate synthase (Lc-GFDPS), the enzyme producing ... >> More
Plant sesterterpenoids, an important class of terpenoids, are widely distributed in various plants, including food crops. However, little is known about their biosynthesis. Here, we cloned and functionally characterized a plant geranylfarnesyl diphosphate synthase (Lc-GFDPS), the enzyme producing the C25 prenyl diphosphate precursor to all sesterterpenoids, from the glandular trichomes of the woody plant Leucosceptrum canum. GFDPS catalyzed the formation of GFDP after expression in Escherichia coli. Overexpressing GFDPS in Arabidopsis thaliana also gave an extract catalyzing GFDP formation. GFDPS was strongly expressed in glandular trichomes, and its transcript profile was completely in accordance with the sesterterpenoid accumulation pattern. GFDPS is localized to the plastids, and inhibitor studies indicated its use of isoprenyl diphosphate substrates supplied by the 2-C-methyl-D-erythritol 4-phosphate pathway. Application of a jasmonate defense hormone induced GFDPS transcript and sesterterpenoid accumulation, while reducing feeding and growth of the generalist insect Spodoptera exigua, suggesting that these C25 terpenoids play a defensive role. Phylogenetic analysis suggested that GFDPS probably evolved from plant geranylgeranyl diphosphate synthase under the influence of positive selection. The isolation of GFDPS provides a model for investigating sesterterpenoid formation in other species and a tool for manipulating the formation of this group in plants and other organisms. << Less
Plant Cell 28:804-822(2016) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.