Zeaksantin epoksidaza
(Preusmjereno sa stranice Zeaksantin,NAD(P)H:kiseonik oksidoreduktaza)
Zeaksantin epoksidaza (EC 1.14.13.90, Zea-epoksidaza) je enzim sa sistematskim imenom zeaksantin,NAD(P)H:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Zeaksantin epoksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.90 | ||||||||
| CAS broj | 149718-34-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- zeaksantin + 2 NAD(P)H + 2 H+ + 2 O2 violaksantin + 2 NAD(P)+ + 2H2O (sveukupna reakcija)
- (1a) zeaksantin + NAD(P)H + H+ + O2 antheraksantin + NAD(P)+ + H2O
- (1b) antheraksantin + NAD(P)H + H+ + O2 violaksantin + NAD(P)+ + H2O
Ovaj enzim je flavoprotein (FAD). On je aktivan pri slabom svetlu.
Reference uredi
- ↑ Buch, K., Stransky, H. and Hager, A. (1995). „FAD is a further essential cofactor of the NAD(P)H and O2-dependent zeaxanthin-epoxidase”. FEBS Lett. 376: 45-48. PMID 8521963.
- ↑ 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.
- ↑ Thompson, A.J., Jackson, A.C., Parker, R.A., Morpeth, D.R., Burbidge, A. and Taylor, I.B. (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 Mol. Biol. 42: 833-845. PMID 10890531.
- ↑ Hieber, A.D., Bugos, R.C. and Yamamoto, H.Y. (2000). „Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase”. Biochim. Biophys. Acta 1482: 84-91. PMID 11058750.
- ↑ Frommolt, R., Goss, R. and Wilhelm, C. (2001). „The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach”. Planta 213: 446-456. PMID 11506368.
- ↑ Frommolt, R., Goss, R. and 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: 492-492. PMID 11506368.
- ↑ Matsubara, S., Morosinotto, T., Bassi, R., Christian, A.L., Fischer-Schliebs, E., Luttge, U., Orthen, B., Franco, A.C., Scarano, F.R., Forster, B., Pogson, B.J. and Osmond, C.B. (2003). „Occurrence of the lutein-epoxide cycle in mistletoes of the Loranthaceae and Viscaceae”. Planta 217: 868-879. PMID 12844265.
Literatura uredi
- 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.