Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline all-trans-violaxanthin Identifier CHEBI:35288 (Beilstein: 101269; CAS: 126-29-4) help_outline Charge 0 Formula C40H56O4 InChIKeyhelp_outline SZCBXWMUOPQSOX-WVJDLNGLSA-N SMILEShelp_outline CC(\C=C\C=C(C)\C=C\[C@@]12O[C@]1(C)C[C@@H](O)CC2(C)C)=C/C=C/C=C(C)/C=C/C=C(C)/C=C/[C@@]12O[C@]1(C)C[C@@H](O)CC2(C)C 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-ascorbate Identifier CHEBI:38290 (Beilstein: 3549814; CAS: 299-36-5) help_outline Charge -1 Formula C6H7O6 InChIKeyhelp_outline CIWBSHSKHKDKBQ-JLAZNSOCSA-M SMILEShelp_outline [H][C@@]1(OC(=O)C(O)=C1[O-])[C@@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 34 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline all-trans-antheraxanthin Identifier CHEBI:27867 (Beilstein: 101042; CAS: 640-03-9) help_outline Charge 0 Formula C40H56O3 InChIKeyhelp_outline OFNSUWBAQRCHAV-OYQUVCAXSA-N SMILEShelp_outline CC(\C=C\C=C(C)\C=C\C1=C(C)C[C@@H](O)CC1(C)C)=C/C=C/C=C(C)/C=C/C=C(C)/C=C/[C@@]12O[C@]1(C)C[C@@H](O)CC2(C)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 H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-dehydroascorbate Identifier CHEBI:58539 Charge -1 Formula C6H5O6 InChIKeyhelp_outline OESHPIGALOBJLM-REOHCLBHSA-N SMILEShelp_outline OC[C@H](O)[C-]1OC(=O)C(=O)C1=O 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15353 | RHEA:15354 | RHEA:15355 | RHEA:15356 | |
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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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Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli.
Bugos R.C., Yamamoto H.Y.
Plants need to avoid or dissipate excess light energy to protect photosystem II (PSII) from photoinhibitory damage. Higher plants have a conserved system that dissipates excess energy as heat in the light-harvesting complexes of PSII that depends on the transthylakoid delta pH and violaxanthin de- ... >> More
Plants need to avoid or dissipate excess light energy to protect photosystem II (PSII) from photoinhibitory damage. Higher plants have a conserved system that dissipates excess energy as heat in the light-harvesting complexes of PSII that depends on the transthylakoid delta pH and violaxanthin de-epoxidase (VDE) activity. To our knowledge, we report the first cloning of a cDNA encoding VDE and expression of functional enzyme in Escherichia coli. VDE is nuclear encoded and has a transit peptide with characteristic features of other lumen-localized proteins. The cDNA encodes a putative polypeptide of 473 aa with a calculated molecular mass of 54,447 Da. Cleavage of the transit peptide results in a mature putative polypeptide of 348 aa with a calculated molecular mass of 39,929 Da, close to the apparent mass of the purified enzyme (43 kDa). The protein has three interesting domains including (i) a cysteine-rich region, (ii) a lipocalin signature, and (iii) a highly charged region. The E. coli expressed enzyme de-epoxidizes violaxanthin sequentially to antheraxanthin and zeaxanthin, and is inhibited by dithiothreitol, similar to VDE purified from chloroplasts. This confirms that the cDNA encodes an authentic VDE of a higher plant and is unequivocal evidence that the same enzyme catalyzes the two-step mono de-epoxidation reaction. The cloning of VDE opens new opportunities for examining the function and evolution of the xanthophyll cycle, and possibly enhancing light-stress tolerance of plants. << Less
Proc. Natl. Acad. Sci. U.S.A. 93:6320-6325(1996) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
Comments
RHEA:15353 part of RHEA:32371 Published in: "Chemical and mutational modification of histidines in violaxanthinde-epoxidase from Spinacia oleracea." Emanuelsson A.K., Eskling M., Aakerlund H.-E. Physiol. Plantarum 119:97-104(2003)