From Wikipedia, the free encyclopedia
Zeaxanthin epoxidase
Identifiers
EC no. 1.14.13.90
CAS no. 149718-34-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Zeaxanthin epoxidase ( EC 1.14.13.90, Zea-epoxidase) is an enzyme with systematic name zeaxanthin,NAD(P)H:oxygen oxidoreductase. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

zeaxanthin + 2 NAD(P)H + 2 H+ + 2 O2 violaxanthin + 2 NAD(P)+ + 2 H2O (overall reaction)
(1a) zeaxanthin + NAD(P)H + H+ + O2 antheraxanthin + NAD(P)+ + H2O
(1b) antheraxanthin + NAD(P)H + H+ + O2 violaxanthin + NAD(P)+ + H2O

Zeaxanthin epoxidase is a flavoprotein (FAD) that is active under conditions of low light.

References

  1. ^ Büch K, Stransky H, Hager A (November 1995). "FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase". FEBS Letters. 376 (1–2): 45–8. doi: 10.1016/0014-5793(95)01243-9. PMID  8521963.
  2. ^ Bugos RC, Hieber AD, Yamamoto HY (June 1998). "Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants". The Journal of Biological Chemistry. 273 (25): 15321–4. doi: 10.1074/jbc.273.25.15321. PMID  9624110.
  3. ^ Thompson AJ, Jackson AC, Parker RA, Morpeth DR, Burbidge A, Taylor IB (April 2000). "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 Molecular Biology. 42 (6): 833–45. doi: 10.1023/A:1006448428401. PMID  10890531.
  4. ^ Hieber AD, Bugos RC, Yamamoto HY (October 2000). "Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1482 (1–2): 84–91. doi: 10.1016/s0167-4838(00)00141-2. PMID  11058750.
  5. ^ Frommolt R, Goss R, Wilhelm C (July 2001). "The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach". Planta. 213 (3): 446–56. doi: 10.1007/s004250100589. PMID  11506368.
  6. ^ Frommolt R, Goss R, Wilhelm C (2001). "Erratum Report. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach". Planta. 213 (3): 492. doi: 10.1007/s004250100619.
  7. ^ Matsubara S, Morosinotto T, Bassi R, Christian AL, Fischer-Schliebs E, Lüttge U, Orthen B, Franco AC, Scarano FR, Förster B, Pogson BJ, Osmond CB (October 2003). "Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae". Planta. 217 (6): 868–79. doi: 10.1007/s00425-003-1059-7. PMID  12844265.
From Wikipedia, the free encyclopedia
Zeaxanthin epoxidase
Identifiers
EC no. 1.14.13.90
CAS no. 149718-34-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Zeaxanthin epoxidase ( EC 1.14.13.90, Zea-epoxidase) is an enzyme with systematic name zeaxanthin,NAD(P)H:oxygen oxidoreductase. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

zeaxanthin + 2 NAD(P)H + 2 H+ + 2 O2 violaxanthin + 2 NAD(P)+ + 2 H2O (overall reaction)
(1a) zeaxanthin + NAD(P)H + H+ + O2 antheraxanthin + NAD(P)+ + H2O
(1b) antheraxanthin + NAD(P)H + H+ + O2 violaxanthin + NAD(P)+ + H2O

Zeaxanthin epoxidase is a flavoprotein (FAD) that is active under conditions of low light.

References

  1. ^ Büch K, Stransky H, Hager A (November 1995). "FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase". FEBS Letters. 376 (1–2): 45–8. doi: 10.1016/0014-5793(95)01243-9. PMID  8521963.
  2. ^ Bugos RC, Hieber AD, Yamamoto HY (June 1998). "Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants". The Journal of Biological Chemistry. 273 (25): 15321–4. doi: 10.1074/jbc.273.25.15321. PMID  9624110.
  3. ^ Thompson AJ, Jackson AC, Parker RA, Morpeth DR, Burbidge A, Taylor IB (April 2000). "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 Molecular Biology. 42 (6): 833–45. doi: 10.1023/A:1006448428401. PMID  10890531.
  4. ^ Hieber AD, Bugos RC, Yamamoto HY (October 2000). "Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1482 (1–2): 84–91. doi: 10.1016/s0167-4838(00)00141-2. PMID  11058750.
  5. ^ Frommolt R, Goss R, Wilhelm C (July 2001). "The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach". Planta. 213 (3): 446–56. doi: 10.1007/s004250100589. PMID  11506368.
  6. ^ Frommolt R, Goss R, Wilhelm C (2001). "Erratum Report. The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach". Planta. 213 (3): 492. doi: 10.1007/s004250100619.
  7. ^ Matsubara S, Morosinotto T, Bassi R, Christian AL, Fischer-Schliebs E, Lüttge U, Orthen B, Franco AC, Scarano FR, Förster B, Pogson BJ, Osmond CB (October 2003). "Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae". Planta. 217 (6): 868–79. doi: 10.1007/s00425-003-1059-7. PMID  12844265.

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