Dihidroorotat dehidrogenaza (fumarat)
(преусмерено са EC 1.3.98.1)
| Dihidroorotat dehidrogenaza (fumarat) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.3.98.1 | ||||||||
| CAS broj | 2603876 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Dihidroorotat dehidrogenaza (fumarat) (EC 1.3.98.1, DHOdehaza (nespecifična), dihidroorotat dehidrogenaza (nespecifična), dihidoorotna kiselina dehidrogenaza (nespecifična), DHOD (nespecifična), DHODaza (nespecifična), dihidroorotatna oksidaza, pyr4 (gen)) je enzim sa sistematskim imenom (S)-dihidroorotat:fumarat oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (S)-dihidroorotat + fumarat orotat + sukcinat
Ovaj enzim vezuje FMN. Reakcija, koja se odvija u citozolu, je jedina redoks reakcija u de novo biosinteza pirimidinskih nukleotida.
Reference
[уреди | уреди извор]- ^ Björnberg, O., Rowland, P., Larsen, S. and Jensen, K.F. (1997). „Active site of dihydroorotate dehydrogenase A from Lactococcus lactis' investigated by chemical modification and mutagenesis”. Biochemistry. 36: 16197—16205. PMID 9405053.
- ^ Rowland, P., Björnberg, O., Nielsen, F.S., Jensen, K.F. and Larsen, S. (1998). „The crystal structure of Lactococcus lactis' dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function”. Protein Sci. 7: 1269—1279. PMID 9655329.
- ^ Nørager, S., Arent, S., Björnberg, O., Ottosen, M., Lo Leggio, L., Jensen, K.F. and Larsen, S. (2003). „Lactococcus lactis' dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function”. J. Biol. Chem. 278: 28812—28822. PMID 12732650.
- ^ Zameitat, E., Pierik, A.J., Zocher, K. and Löffler, M. (2007). „Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues”. FEMS Yeast Res. 7: 897—904. PMID 17617217.
- ^ Inaoka, D.K., Sakamoto, K., Shimizu, H., Shiba, T., Kurisu, G., Nara, T., Aoki, T., Kita, K. and Harada, S. (2008). „Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction”. Biochemistry. 47: 10881—10891. PMID 18808149.
- ^ Cheleski, J., Wiggers, H.J., Citadini, A.P., da Costa Filho, A.J., Nonato, M.C. and Montanari, C.A. (2010). „Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry”. Anal. Biochem. 399: 13—22. PMID 19932077.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
[уреди | уреди извор]- Dihydroorotate+dehydrogenase+(fumarate) на US National Library of Medicine Medical Subject Headings (MeSH)
