Orotat reduktaza (NADH)
| Orotat reduktaza (NADH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.3.1.14 | ||||||||
| CAS broj | 37255-26-8 | ||||||||
| 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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Orotat reduktaza (NADH) (EC 1.3.1.14, orotatna reduktaza (NADH), orotatna reduktaza (NADH2), DHOdehaza (nespecifična), DHOD (nespecifična), DHODaza (spedifična), dihidroorotatna oksidaza, pyrD (gen)) je enzim sa sistematskim imenom (S)-dihidroorotat:NAD+ oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (S)-dihidroorotat + NAD+ orotat + NADH + H+
Ovaj enzim vezuje FMN, FAD i [2Fe-2S] kluster. On se sastoji od dve podjedinice: FMN vezujuće katalitičke podjedinice, i FAD i gvožđe-sumpor vezujuće podjedinice za transfer elektrona. Reakcija, koja se odvija u citozolu, je ona je jedina redox reakcija u de-novo biosintezi pirimidinskih nukleotida. Druga klasa 1 dihidroorotatnih dehidrogenaza koristi bilo fumarat (EC 1.3.98.1) ili NADP+ (EC 1.3.1.15) kao elektronski akceptor. Membranska klasa 2 dihidroorotatnih dehidrogenaza (EC 1.3.5.2) koristi hinon kao elektronski akceptor.
Reference[uredi | uredi kod]
- ↑ Friedmann, H.C. and Vennesland, B. (1958). „Purification and properties of dihydroorotic acid dehydrogenase”. J. Biol. Chem. 233: 1398-1406. PMID 13610849.
- ↑ Friedmann, H.C. and Vennesland, B. (1960). „Crystalline dihydroorotic dehydrogenase”. J. Biol. Chem. 235: 1526-1532. PMID 13825167.
- ↑ Lieberman, I. and Kornberg, A. (1953). „Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase”. Biochim. Biophys. Acta 12: 223-234. PMID 13115431.
- ↑ Nielsen, F.S., Andersen, P.S. and Jensen, K.F. (1996). „The B form of dihydroorotate dehydrogenase from Lactococcus lactis' consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers”. J. Biol. Chem. 271: 29359-29365. PMID 8910599.
- ↑ Rowland, P., Nørager, S., Jensen, K.F. and Larsen, S. (2000). „Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster”. Structure 8: 1227-1238. PMID 11188687.
- ↑ Kahler, A.E., Nielsen, F.S. and Switzer, R.L. (1999). „Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits”. Arch. Biochem. Biophys. 371: 191-201. PMID 10545205.
- ↑ Marcinkeviciene, J., Tinney, L.M., Wang, K.H., Rogers, M.J. and Copeland, R.A. (1999). „Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism”. Biochemistry 38: 13129-13137. PMID 10529184.
Literatura[uredi | uredi kod]
- 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.