EC
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1.10.99.3
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Transferred entry: | violaxanthin de-epoxidase. Now classified as EC 1.23.5.1, violaxanthin de-epoxidase.
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[EC 1.10.99.3 created 2005, deleted 2014] |
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EC |
1.13.11.51 |
Accepted name: |
9-cis-epoxycarotenoid dioxygenase |
Reaction: |
(1) a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12′-apo-carotenal (2) 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12′-apo-β-caroten-12′-al (3) 9′-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12′-apo-β-caroten-12′-al |
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For diagram of abscisic-acid biosynthesis, click here |
Other name(s): |
nine-cis-epoxycarotenoid dioxygenase; NCED; AtNCED3; PvNCED1; VP14 |
Systematic name: |
9-cis-epoxycarotenoid 11,12-dioxygenase |
Comments: |
Requires iron(II). Acts on 9-cis-violaxanthin and 9′-cis-neoxanthin but not on the all-trans isomers [2,3]. In vitro, it will cleave 9-cis-zeaxanthin. Catalyses the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress. The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic-aldehyde oxidase) and EC 1.14.13.93 [(+)-abscisic acid 8′-hydroxylase]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 199877-10-6 |
References: |
1. |
Schwartz, S.H., Tan, B.C., Gage, D.A., Zeevaart, J.A. and McCarty, D.R. Specific oxidative cleavage of carotenoids by VP14 of maize. Science 276 (1997) 1872–1874. [DOI] [PMID: 9188535] |
2. |
Tan, B.C., Schwartz, S.H., Zeevaart, J.A. and McCarty, D.R. Genetic control of abscisic acid biosynthesis in maize. Proc. Natl. Acad. Sci. USA 94 (1997) 12235–12240. [DOI] [PMID: 9342392] |
3. |
Qin, X. and Zeevaart, J.A. The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of abscisic acid biosynthesis in water-stressed bean. Proc. Natl. Acad. Sci. USA 96 (1999) 15354–15361. [DOI] [PMID: 10611388] |
4. |
Thompson, A.J., Jackson, A.C., Symonds, R.C., Mulholland, B.J., Dadswell, A.R., Blake, P.S., Burbidge, A. and Taylor, I.B. Ectopic expression of a tomato 9-cis-epoxycarotenoid dioxygenase gene causes over-production of abscisic acid. Plant J. 23 (2000) 363–374. [DOI] [PMID: 10929129] |
5. |
Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of
9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid
biosynthesis in Arabidopsis. Plant J. 27 (2001) 325–333. [DOI] [PMID: 11532178] |
6. |
Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of
9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Plant J. 30 (2002) 611. |
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[EC 1.13.11.51 created 2005] |
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EC
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1.14.13.90
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Transferred entry: | zeaxanthin epoxidase. Now EC 1.14.15.21, zeaxanthin epoxidase
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[EC 1.14.13.90 created 2005, deleted 2016] |
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EC |
1.14.15.21 |
Accepted name: |
zeaxanthin epoxidase |
Reaction: |
zeaxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = violaxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (overall reaction) (1a) zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (1b) antheraxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = violaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
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For diagram of the xanthophyll cycle, click here |
Other name(s): |
Zea-epoxidase |
Systematic name: |
zeaxanthin,reduced ferredoxin:oxygen oxidoreductase |
Comments: |
A flavoprotein (FAD) that is active under conditions of low light. Along with EC 1.23.5.1, violaxanthin de-epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. It will also epoxidize lutein in some higher-plant species. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 149718-34-3 |
References: |
1. |
Buch, K., Stransky, H. and Hager, A. FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase. FEBS Lett. 376 (1995) 45–48. [DOI] [PMID: 8521963] |
2. |
Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321–15324. [DOI] [PMID: 9624110] |
3. |
Thompson, A.J., Jackson, A.C., Parker, R.A., Morpeth, D.R., Burbidge, A. and Taylor, I.B. Abscisic acid biosynthesis in tomato: regulation of zeaxanthin epoxidase and 9-cis-epoxycarotenoid dioxygenase mRNAs by light/dark cycles, water stress and abscisic acid. Plant Mol. Biol. 42 (2000) 833–845. [PMID: 10890531] |
4. |
Hieber, A.D., Bugos, R.C. and Yamamoto, H.Y. Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase. Biochim. Biophys. Acta 1482 (2000) 84–91. [DOI] [PMID: 11058750] |
5. |
Frommolt, R., Goss, R. and Wilhelm, C. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 446–456. [PMID: 11506368] |
6. |
Frommolt, R., Goss, R. and Wilhelm, C. Erratum Report. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach. Planta 213 (2001) 492. |
7. |
Matsubara, S., Morosinotto, T., Bassi, R., Christian, A.L., Fischer-Schliebs, E., Luttge, U., Orthen, B., Franco, A.C., Scarano, F.R., Forster, B., Pogson, B.J. and Osmond, C.B. Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae. Planta 217 (2003) 868–879. [DOI] [PMID: 12844265] |
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[EC 1.14.15.21 created 2005 as EC 1.14.13.90, transferred 2016 to EC 1.14.15.21] |
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EC |
1.23.5.1 |
Accepted name: |
violaxanthin de-epoxidase |
Reaction: |
violaxanthin + 2 L-ascorbate = zeaxanthin + 2 L-dehydroascorbate + 2 H2O (overall reaction) (1a) violaxanthin + L-ascorbate = antheraxanthin + L-dehydroascorbate + H2O (1b) antheraxanthin + L-ascorbate = zeaxanthin + L-dehydroascorbate + H2O |
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For diagram of the xanthophyll cycle, click here |
Glossary: |
violaxanthin = (3S,3′S,5R,5′R,6S,6′S)-5,6:5′,6′-diepoxy-5,5′,6,6′-tetrahydro-β,β-carotene-3,3′-diol
antheraxanthin = (3R,3′S,5′R,6′S)-5′,6′-epoxy-5′,6′-dihydro-β,β-carotene-3,3′-diol
zeaxanthin = (3R,3′R)-β,β-carotene-3,3′-diol |
Other name(s): |
VDE |
Systematic name: |
violaxanthin:ascorbate oxidoreductase |
Comments: |
Along with EC 1.14.15.21, zeaxanthin epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. It is activated by a low pH of the thylakoid lumen (produced by high light intensity). Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57534-73-3 |
References: |
1. |
Yamamoto, H.Y. and Higashi, R.M. Violaxanthin de-epoxidase. Lipid composition and substrate specificity. Arch. Biochem. Biophys. 190 (1978) 514–522. [DOI] [PMID: 102251] |
2. |
Rockholm, D.C. and Yamamoto, H.Y. Violaxanthin de-epoxidase. Plant Physiol. 110 (1996) 697–703. [PMID: 8742341] |
3. |
Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 273 (1998) 15321–15324. [DOI] [PMID: 9624110] |
4. |
Kuwabara, T., Hasegawa, M., Kawano, M. and Takaichi, S. Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A. Plant Cell Physiol. 40 (1999) 1119–1126. [PMID: 10635115] |
5. |
Latowski, D., Kruk, J., Burda, K., Skrzynecka-Jaskierm, M., Kostecka-Gugala, A. and Strzalka, K. Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers. Eur. J. Biochem. 269 (2002) 4656–4665. [DOI] [PMID: 12230579] |
6. |
Goss, R. Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae). Planta 217 (2003) 801–812. [DOI] [PMID: 12748855] |
7. |
Latowski, D., Akerlund, H.E. and Strzalka, K. Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. Biochemistry 43 (2004) 4417–4420. [DOI] [PMID: 15078086] |
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[EC 1.23.5.1 created 2005 as EC 1.10.99.3, transferred 2015 to EC 1.23.5.1] |
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EC |
5.3.99.8 |
Accepted name: |
capsanthin/capsorubin synthase |
Reaction: |
(1) violaxanthin = capsorubin (2) antheraxanthin = capsanthin |
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For diagram of the biosynthesis of capsanthin, capsarubin and neoxanthin, click here and for diagram of carotenoid epoxide rearrangements, click here |
Other name(s): |
CCS; ketoxanthophyll synthase; capsanthin-capsorubin synthase |
Systematic name: |
violaxanthin—capsorubin isomerase (ketone-forming) |
Comments: |
This multifunctional enzyme is induced during chromoplast differentiation in plants [1]. Isomerization of the epoxide ring of violaxanthin gives the cyclopentyl-ketone of capsorubin or capsanthin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 162032-85-1 |
References: |
1. |
Bouvier, F., Hugueney, P., d'Harlingue, A., Kuntz, M. and Camara, B. Xanthophyll biosynthesis in chromoplasts: isolation and molecular cloning of an enzyme catalyzing the conversion of 5,6-epoxycarotenoid into ketocarotenoid. Plant J. 6 (1994) 45–54. [DOI] [PMID: 7920703] |
2. |
Lefebvre, V., Kuntz, M., Camara, B. and Palloix, A. The capsanthin-capsorubin synthase gene: a candidate gene for the y locus controlling the red fruit colour in pepper. Plant Mol. Biol. 36 (1998) 785–789. [PMID: 9526511] |
3. |
Xu, C.J., Chen, D.M. and Zhang, S.L. [Molecular cloning of full length capsanthin/capsorubin synthase
homologous gene from orange (Citrus sinensis)] Shi Yan Sheng Wu Xue Bao 34 (2001) 147–150. [PMID: 12549109] (in Chinese) |
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[EC 5.3.99.8 created 2005] |
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EC |
5.3.99.9 |
Accepted name: |
neoxanthin synthase |
Reaction: |
violaxanthin = neoxanthin |
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For diagram of the biosynthesis of capsanthin, capsarubin and neoxanthin, click here and for diagram of carotenoid epoxide rearrangements, click here |
Other name(s): |
NSY |
Systematic name: |
violaxanthin—neoxanthin isomerase (epoxide-opening) |
Comments: |
The opening of the epoxide ring of violaxanthin generates a chiral allene. Neoxanthin is a precursor of the plant hormone abscisic acid and the last product of carotenoid synthesis in green plants [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 318960-21-3 |
References: |
1. |
Al-Babili, S., Hugueney, P., Schledz, M., Welsch, R., Frohnmeyer, H., Laule, O. and Beyer, P. Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum. FEBS Lett. 485 (2000) 168–172. [DOI] [PMID: 11094161] |
2. |
Bouvier, F., d'Harlingue, A., Backhaus, R.A., Kumagai, M.H. and Camara, B. Identification of neoxanthin synthase as a carotenoid cyclase paralog. Eur. J. Biochem. 267 (2000) 6346–6352. [DOI] [PMID: 11029576] |
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[EC 5.3.99.9 created 2005] |
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