Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline (2E,6E)-farnesyl diphosphate Identifier CHEBI:175763 Charge -3 Formula C15H25O7P2 InChIKeyhelp_outline VWFJDQUYCIWHTN-YFVJMOTDSA-K SMILEShelp_outline CC(C)=CCC\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 175 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 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline selina-4(15),7(11)-diene Identifier CHEBI:138051 (CAS: 515-17-3) help_outline Charge 0 Formula C15H24 InChIKeyhelp_outline RMZHSBMIZBMVMN-LSDHHAIUSA-N SMILEShelp_outline C1CCC([C@]2([C@]1(CCC(C2)=C(C)C)C)[H])=C 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:54112 | RHEA:54113 | RHEA:54114 | RHEA:54115 | |
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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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Induced-fit mechanism in class I terpene cyclases.
Baer P., Rabe P., Fischer K., Citron C.A., Klapschinski T.A., Groll M., Dickschat J.S.
We present crystallographic and functional data of selina-4(15),7(11)-diene synthase (SdS) from Streptomyces pristinaespiralis in its open and closed (ligand-bound) conformation. We could identify an induced-fit mechanism by elucidating a rearrangement of the G1/2 helix-break motif upon substrate ... >> More
We present crystallographic and functional data of selina-4(15),7(11)-diene synthase (SdS) from Streptomyces pristinaespiralis in its open and closed (ligand-bound) conformation. We could identify an induced-fit mechanism by elucidating a rearrangement of the G1/2 helix-break motif upon substrate binding. This rearrangement highlights a novel effector triad comprising the pyrophosphate sensor Arg178, the linker Asp181, and the effector Gly182-O. This structural motif is strictly conserved in class I terpene cyclases from bacteria, fungi, and plants, including epi-isozizaene synthase (3KB9), aristolochene synthase (4KUX), bornyl diphosphate synthase (1N20), limonene synthase (2ONG), 5-epi-aristolochene synthase (5EAT), and taxa-4(5),11(12)-diene synthase (3P5R). An elaborate structure-based mutagenesis in combination with analysis of the distinct product spectra confirmed the mechanistic models of carbocation formation and stabilization in SdS. << Less
Angew. Chem. Int. Ed. 53:7652-7656(2014) [PubMed] [EuropePMC]
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Rapid chemical characterization of bacterial terpene synthases.
Rabe P., Dickschat J.S.
Angew. Chem. Int. Ed. 52:1810-1812(2013) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.