Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline (2E,6E)-farnesol Identifier CHEBI:16619 (CAS: 106-28-5) help_outline Charge 0 Formula C15H26O InChIKeyhelp_outline CRDAMVZIKSXKFV-YFVJMOTDSA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CO 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CTP Identifier CHEBI:37563 (Beilstein: 4732530) help_outline Charge -4 Formula C9H12N3O14P3 InChIKeyhelp_outline PCDQPRRSZKQHHS-XVFCMESISA-J SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 86 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E,6E)-farnesyl phosphate Identifier CHEBI:88226 Charge -2 Formula C15H25O4P InChIKeyhelp_outline ALEWCKXBHSDCCT-YFVJMOTDSA-L SMILEShelp_outline C(\C)(/CCC=C(C)C)=C\CC\C(=C\COP([O-])(=O)[O-])\C 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CDP Identifier CHEBI:58069 Charge -3 Formula C9H12N3O11P2 InChIKeyhelp_outline ZWIADYZPOWUWEW-XVFCMESISA-K SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 28 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:51680 | RHEA:51681 | RHEA:51682 | RHEA:51683 | |
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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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Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase.
Bentinger M., Grunler J., Peterson E., Swiezewska E., Dallner G.
As farnesol may serve as a nonsterol endogenous regulator of the mevalonate pathway, the possibility that a kinase specific for its phosphorylation is present in the rat liver was investigated. In the 10,000 g supernatant of rat liver, farnesyl monophosphate was synthesized in the presence of ATP. ... >> More
As farnesol may serve as a nonsterol endogenous regulator of the mevalonate pathway, the possibility that a kinase specific for its phosphorylation is present in the rat liver was investigated. In the 10,000 g supernatant of rat liver, farnesyl monophosphate was synthesized in the presence of ATP. The Km value for farnesol was 2.3 microM. Various detergents inhibited the activity of the enzyme. The farnesol kinase was present in rough and in smooth I microsomes, but not in smooth II microsomes, mitochondria, peroxisomes, Golgi, or plasma membranes. The enzyme was associated with the inner, luminal surface of the vesicles. Further analyses have demonstrated that an enzymatic mechanism exists which catalyzes the phosphorylation of farnesyl-P to farnesyl-PP. Activity of the farnesyl phosphate kinase resulted in the phosphorylation of the monophosphate by CTP but not by ATP, GTP, or UTP. This enzyme is activated by low concentrations of detergents. Treatment with proteases and chemical probes indicate that this second phosphorylation reaction probably takes place on the outer, cytoplasmic surface of microsomal vesicles. These results demonstrate that rat liver microsomes contain two enzymes for the consecutive phosphorylation of farnesol to farnesyl-PP. << Less
Arch Biochem Biophys 353:191-198(1998) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis.
Fitzpatrick A.H., Bhandari J., Crowell D.N.
Farnesol, which is toxic to plant cells at high concentrations, is sequentially phosphorylated to farnesyl phosphate and farnesyl diphosphate. However, the genes responsible for the sequential phosphorylation of farnesol have not been identified and the physiological role of farnesol phosphorylati ... >> More
Farnesol, which is toxic to plant cells at high concentrations, is sequentially phosphorylated to farnesyl phosphate and farnesyl diphosphate. However, the genes responsible for the sequential phosphorylation of farnesol have not been identified and the physiological role of farnesol phosphorylation has not been fully elucidated. To address these questions, we confirmed the presence of farnesol kinase activity in Arabidopsis (Arabidopsis thaliana) membranes and identified the corresponding gene (At5g58560, FOLK). Heterologous expression in recombinant yeast cells established farnesol as the preferred substrate of the FOLK-encoded kinase. Moreover, loss-of-function mutations in the FOLK gene abolished farnesol kinase activity, caused an abscisic acid-hypersensitive phenotype and promoted the development of supernumerary carpels under water-stress conditions. In wild-type plants, exogenous abscisic acid repressed FOLK gene expression. These observations demonstrate a role for farnesol kinase in negative regulation of abscisic acid signaling, and provide molecular evidence for a link between farnesol metabolism, abiotic stress signaling and flower development. << Less
Plant J. 66:1078-1088(2011) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.