Biology:Violaxanthin de-epoxidase
From HandWiki
| Violaxanthin de-epoxidase | |||||||||
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| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] zeaxanthin + 2 L-dehydroascorbate + 2 H2O (overall reaction)
- (1a) violaxanthin + L-ascorbate [math]\displaystyle{ \rightleftharpoons }[/math] antheraxanthin + L-dehydroascorbate + H2O
- (1b) antheraxanthin + L-ascorbate [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Violaxanthin de-epoxidase. Lipid composition and substrate specificity". Archives of Biochemistry and Biophysics 190 (2): 514–22. October 1978. doi:10.1016/0003-9861(78)90305-3. PMID 102251.
- ↑ "Violaxanthin de-epoxidase". Plant Physiology 110 (2): 697–703. February 1996. doi:10.1104/pp.110.2.697. PMID 8742341.
- ↑ "Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants". The Journal of Biological Chemistry 273 (25): 15321–4. June 1998. doi:10.1074/jbc.273.25.15321. PMID 9624110.
- ↑ "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. November 1999. doi:10.1093/oxfordjournals.pcp.a029496. PMID 10635115.
- ↑ "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. September 2002. doi:10.1046/j.1432-1033.2002.03166.x. PMID 12230579.
- ↑ "Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)". Planta 217 (5): 801–12. September 2003. doi:10.1007/s00425-003-1044-1. PMID 12748855.
- ↑ "Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity". Biochemistry 43 (15): 4417–20. April 2004. doi:10.1021/bi049652g. PMID 15078086.
External links
- Violaxanthin+de-epoxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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