Reaction participants Show >> << Hide
- Name help_outline δ-tocopherol Identifier CHEBI:47772 (Beilstein: 92691; CAS: 119-13-1) help_outline Charge 0 Formula C27H46O2 InChIKeyhelp_outline GZIFEOYASATJEH-VHFRWLAGSA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC[C@]1(C)CCc2cc(O)cc(C)c2O1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-methyl-6-phytyl-1,4-benzene-1,4-diol Identifier CHEBI:75920 Charge 0 Formula C27H46O2 InChIKeyhelp_outline GTWCNYRFOZKWTL-UOFXASEASA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC\C(C)=C\Cc1cc(O)cc(C)c1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:37987 | RHEA:37988 | RHEA:37989 | RHEA:37990 | |
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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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Isolation of an Arabidopsis mutant lacking vitamin E and identification of a cyclase essential for all tocopherol biosynthesis.
Porfirova S., Bergmueller E., Tropf S., Lemke R., Doermann P.
Tocopherol (vitamin E) is a plant chloroplast lipid presumed to be involved in the response to oxidative stress. A tocopherol-deficient mutant (vte1) was isolated from Arabidopsis thaliana by using a TLC-based screening approach. Mutant plants lacked all four tocopherol forms and were deficient in ... >> More
Tocopherol (vitamin E) is a plant chloroplast lipid presumed to be involved in the response to oxidative stress. A tocopherol-deficient mutant (vte1) was isolated from Arabidopsis thaliana by using a TLC-based screening approach. Mutant plants lacked all four tocopherol forms and were deficient in tocopherol cyclase activity. Genetic mapping of vte1 and a genomics-based approach led to the identification of the ORF At4g32770 as a candidate gene for tocopherol cyclase. In vte1, At4g32770 contains a splicing site mutation and the corresponding mRNA expression is reduced. Expression of VTE1 in Escherichia coli resulted in the production of a protein with high tocopherol cyclase and tocotrienol cyclase activity. The VTE1 sequence shows no similarities to genes with known function, but is similar to that of SXD1, a gene that was recently isolated based on the availability of the sucrose export defective1 maize mutant (sxd1). Growth of the vte1 mutant, chlorophyll content, and photosynthetic quantum yield were similar to wild type under optimal growth conditions. Therefore, absence of tocopherol has no large impact on photosynthesis or plant viability, suggesting that other antioxidants can compensate for the loss of tocopherol. During photo-oxidative stress, chlorophyll content and photosynthetic quantum yield were slightly reduced in vte1 as compared with wild type indicating a potential role for tocopherol in maintaining an optimal photosynthesis rate under high-light stress. << Less
Proc. Natl. Acad. Sci. U.S.A. 99:12495-12500(2002) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Characterization of tocopherol cyclases from higher plants and cyanobacteria. Evolutionary implications for tocopherol synthesis and function.
Sattler S.E., Cahoon E.B., Coughlan S.J., DellaPenna D.
Tocopherols are lipophilic antioxidants synthesized exclusively by photosynthetic organisms and collectively constitute vitamin E, an essential nutrient for both humans and animals. Tocopherol cyclase (TC) catalyzes the conversion of various phytyl quinol pathway intermediates to their correspondi ... >> More
Tocopherols are lipophilic antioxidants synthesized exclusively by photosynthetic organisms and collectively constitute vitamin E, an essential nutrient for both humans and animals. Tocopherol cyclase (TC) catalyzes the conversion of various phytyl quinol pathway intermediates to their corresponding tocopherols through the formation of the chromanol ring. Herein, the molecular and biochemical characterization of TCs from Arabidopsis (VTE1 [VITAMIN E 1]), Zea mays (SXD1 [Sucrose Export Deficient 1]) and Synechocystis sp. PCC6803 (slr1737) are described. Mutations in the VTE1, SXD1, or slr1737 genes resulted in both tocopherol deficiency and the accumulation of 2,3-dimethyl-6-phytyl-1,4-benzoquinone (DMPBQ), a TC substrate. Recombinant SXD1 and VTE1 proteins are able to convert DMPBQ to gamma-tocopherol in vitro. In addition, expression of maize SXD1 in a Synechocystis sp. PCC6803 slr1737 knockout mutant restored tocopherol synthesis, indicating that TC activity is evolutionarily conserved between plants and cyanobacteria. Sequence analysis identified a highly conserved 30-amino acid C-terminal domain in plant TCs that is absent from cyanobacterial orthologs. vte1-2 causes a truncation within this C-terminal domain, and the resulting mutant phenotype suggests that this domain is necessary for TC activity in plants. The defective export of Suc in sxd1 suggests that in addition to presumed antioxidant activities, tocopherols or tocopherol breakdown products also function as signal transduction molecules, or, alternatively, the DMPBQ that accumulates in sxd1 disrupts signaling required for efficient Suc export in maize. << Less
Plant Physiol. 132:2184-2195(2003) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.