Dihidroorotat dehidrogenaza (hinon)

Dihidroorotat dehidrogenaza (hinon)
Identifikatori
EC broj 1.3.5.2
CAS broj 59088-23-2
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
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Dihidroorotat dehidrogenaza (hinon) (EC 1.3.5.2, dihidroorotat:ubihinon oksidoreduktaza, (S)-dihidroorotat:(akceptor) oksidoreduktaza, (S)-dihidroorotat:akceptor oksidoreduktaza, DHOdehaza (nespecifična), DHOD (nespecifična), DHODase (nespecifična), DHODH) je enzim sa sistematskim imenom (S)-dihidroorotat:hinon oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

(S)-dihidroorotat + hinon ⇌ {\displaystyle \rightleftharpoons } orotat + hinol

Ova dihidroorotatna dehidrogenaza klase 2 sadrži contains FMN. Enzim je prisutan kod eukariota u mitohondrijskoj membrani, i u pojedinim gram negativnim bakterijama vezan za ćelijsku membranu. Reakcija posredovana ovim enzimom je jedina redoks reakcija u de novo biosintezi pirimidinskih nukleotida. Najbolji hinonski elektronski akceptori za enzim iz goveđe jetre su ubihinon-6 i ubihinon-7, mada jednostavni hinoni, kao što je benzohinon, takođe mogu deluju kao manje efikasni akceptori.

Reference

  1. ↑ Forman, H.J. and Kennedy, J. (1978). „Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme”. Arch. Biochem. Biophys. 191: 23-31. PMID 216313. 
  2. ↑ Hines, V., Keys, L.D., III and Johnston, M. (1986). „Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase”. J. Biol. Chem. 261: 11386-11392. PMID 3733756. 
  3. ↑ Bader, B., Knecht, W., Fries, M. and Löffler, M. (1998). „Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase”. Protein Expr. Purif. 13: 414-422. PMID 9693067. 
  4. ↑ Fagan, R.L., Nelson, M.N., Pagano, P.M. and Palfey, B.A. (2006). „Mechanism of flavin reduction in Class 2 dihydroorotate dehydrogenases”. Biochemistry 45: 14926-14932. PMID 17154530. 
  5. ↑ Björnberg, O., Grüner, A.C., Roepstorff, P. and Jensen, K.F. (1999). „The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis”. Biochemistry 38: 2899-2908. PMID 10074342. 

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 Dihydroorotate+dehydrogenase+(quinone)
  • p
  • r
  • u
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