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 de-epoxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.10.99.3 | ||||||||
CAS no. | 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 | ||||||||
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- 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
Violaxanthin de-epoxidase is a part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts.
References
edit- ^ Yamamoto HY, Higashi RM (October 1978). "Violaxanthin de-epoxidase. Lipid composition and substrate specificity". Archives of Biochemistry and Biophysics. 190 (2): 514–22. doi:10.1016/0003-9861(78)90305-3. PMID 102251.
- ^ Rockholm DC, Yamamoto HY (February 1996). "Violaxanthin de-epoxidase". Plant Physiology. 110 (2): 697–703. doi:10.1104/pp.110.2.697. PMC 157766. PMID 8742341.
- ^ 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.
- ^ Kuwabara T, Hasegawa M, Kawano M, Takaichi S (November 1999). "Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A". Plant & Cell Physiology. 40 (11): 1119–26. doi:10.1093/oxfordjournals.pcp.a029496. PMID 10635115.
- ^ Latowski D, Kruk J, Burda K, Skrzynecka-Jaskier M, Kostecka-Gugała A, Strzałka K (September 2002). "Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers". European Journal of Biochemistry. 269 (18): 4656–65. doi:10.1046/j.1432-1033.2002.03166.x. PMID 12230579.
- ^ Goss R (September 2003). "Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)". Planta. 217 (5): 801–12. doi:10.1007/s00425-003-1044-1. PMID 12748855.
- ^ Latowski D, Akerlund HE, Strzałka K (April 2004). "Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity". Biochemistry. 43 (15): 4417–20. doi:10.1021/bi049652g. PMID 15078086.
External links
edit- Violaxanthin+de-epoxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)