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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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 ⇌ {\displaystyle \rightleftharpoons } zeaksantin + 2 L-dehidroaskorbat + 2H2O (sveukupna reakcija)
(1a) violaksantin + L-askorbat ⇌ {\displaystyle \rightleftharpoons } anteraksantin + L-dehidroaskorbat + H2O
(1b) antheraksantin + L-askorbat ⇌ {\displaystyle \rightleftharpoons } 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.

Reference

  1. ↑ Yamamoto, H.Y. and Higashi, R.M. (1978). „Violaxanthin de-epoxidase. Lipid composition and substrate specificity”. Arch. Biochem. Biophys. 190: 514-522. PMID 102251. 
  2. ↑ Rockholm, D.C. and Yamamoto, H.Y. (1996). „Violaxanthin de-epoxidase”. Plant Physiol. 110: 697-703. PMID 8742341. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ Goss, R. (2003). „Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)”. Planta 217: 801-812. PMID 12748855. 
  7. ↑ 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. 

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 Violaxanthin+de-epoxidase
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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