Zeaksantin epoksidaza

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
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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 + 2 NAD(P)H + 2 H+ + 2 O2 ⇌ {\displaystyle \rightleftharpoons } violaksantin + 2 NAD(P)+ + 2H2O (sveukupna reakcija)
(1a) zeaksantin + NAD(P)H + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } antheraksantin + NAD(P)+ + H2O
(1b) antheraksantin + NAD(P)H + H+ + O2 ⇌ {\displaystyle \rightleftharpoons } violaksantin + NAD(P)+ + H2O

Ovaj enzim je flavoprotein (FAD). On je aktivan pri slabom svetlu.

Reference

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ 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. 
  7. ↑ 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

  • 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. 

Spoljašnje veze

  • MeSH Zeaxanthin+epoxidase
  • p
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6