Violaxanthin de-epoxidase

Violaxanthin de-epoxidase
Identifiers
EC number 1.10.99.3
CAS number 57534-73-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Violaxanthin de-epoxidase (EC 1.10.99.3, VDE) is an enzyme with systematic name violaxanthin:ascorbate oxidoreductase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

violaxanthin + 2 L-ascorbate \rightleftharpoons zeaxanthin + 2 L-dehydroascorbate + 2 H2O (overall reaction)
(1a) violaxanthin + L-ascorbate \rightleftharpoons antheraxanthin + L-dehydroascorbate + H2O
(1b) antheraxanthin + L-ascorbate \rightleftharpoons zeaxanthin + L-dehydroascorbate + H2O

Violaxanthin de-epoxidase is a part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts.

References

  1. Yamamoto, H.Y. and Higashi, R.M. (1978). "Violaxanthin de-epoxidase. Lipid composition and substrate specificity". Arch. Biochem. Biophys. 190 (2): 514–522. doi:10.1016/0003-9861(78)90305-3. PMID 102251.
  2. Rockholm, D.C. and Yamamoto, H.Y. (1996). "Violaxanthin de-epoxidase". Plant Physiol. 110 (2): 697–703. doi:10.1104/pp.110.2.697. PMC 157766. PMID 8742341.
  3. Bugos, R.C., Hieber, A.D. and Yamamoto, H.Y. (1998). "Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants". J. Biol. Chem. 273 (25): 15321–15324. doi:10.1074/jbc.273.25.15321. PMID 9624110.
  4. Kuwabara, T., Hasegawa, M., Kawano, M. and Takaichi, S. (1999). "Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A". Plant Cell Physiol. 40 (11): 1119–1126. doi:10.1093/oxfordjournals.pcp.a029496. PMID 10635115.
  5. Latowski, D., Kruk, J., Burda, K., Skrzynecka-Jaskierm, M., Kostecka-Gugala, A. and Strzalka, K. (2002). "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 (18): 4656–4665. doi:10.1046/j.1432-1033.2002.03166.x. PMID 12230579.
  6. Goss, R. (2003). "Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)". Planta 217 (5): 801–812. doi:10.1007/s00425-003-1044-1. PMID 12748855.
  7. Latowski, D., Akerlund, H.E. and Strzalka, K. (2004). "Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity". Biochemistry 43 (15): 4417–4420. doi:10.1021/bi049652g. PMID 15078086.

External links

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