Violaksantin deepoksidaza
| Violaksantin deepoksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.10.99.3 | ||||||||
| CAS broj | 57534-73-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Violaksantin deepoksidaza (EC 1.10.99.3, VDE) je enzim sa sistematskim imenom violaksantin:askorbat oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- violaksantin + 2 L-askorbat zeaksantin + 2 L-dehidroaskorbat + 2H2O (sveukupna reakcija)
- (1a) violaksantin + L-askorbat anteraksantin + L-dehidroaskorbat + H2O
- (1b) antheraksantin + L-askorbat zeaksantin + L-dehidroaskorbat + H2O
Zajedno sa EC 1.14.13.90, zeaksantinskom epoksidazom, ovaj enzim formira deo ksantofilnog (ili violaksantinskog) ciklusa za kontrolu koncentracije zeaksantina u hloroplastima.
- ↑ Yamamoto, H.Y. and Higashi, R.M. (1978). „Violaxanthin de-epoxidase. Lipid composition and substrate specificity”. Arch. Biochem. Biophys. 190: 514-522. PMID 102251.
- ↑ Rockholm, D.C. and Yamamoto, H.Y. (1996). „Violaxanthin de-epoxidase”. Plant Physiol. 110: 697-703. PMID 8742341.
- ↑ 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: 15321-15324. PMID 9624110.
- ↑ 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: 1119-1126. PMID 10635115.
- ↑ 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: 4656-4665. PMID 12230579.
- ↑ Goss, R. (2003). „Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)”. Planta 217: 801-812. PMID 12748855.
- ↑ 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: 4417-4420. PMID 15078086.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.