3-Demetilubikvinon-9 3-O-metiltransferaza
3-demetilubikvinon-9 3-O-metiltransferaza (EC 2.1.1.64, 5-demetilubihinon-9 metiltransferaza, OMHMB-metiltransferaza, 2-oktaprenil-3-metil-5-hidroksi-6-metoksi-1,4-benzohinon metiltransferaza, S-adenozil-L-metionin:2-oktaprenil-3-metil-5-hidroksi-6-metoksi-1,4-benzohinon-O-metiltransferaza, COQ3 (gen), Coq3 O-metiltransferaza, ubiG (gen)) je enzim sa sistematskim imenom S-adenozil-L-metionin:3-hidroksi-2-metoksi-5-metil-6-(sve-trans-poliprenil)-1,4-benzohinol 3-O-metiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 3-demetilubikvinon-9 3-O-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.64 | ||||||||
| CAS broj | 63774-48-1 | ||||||||
| 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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- S-adenozil-L-metionin + 3-demetilubikvinol-n S-adenozil-L-homocistein + ubikvinol-n
Ovaj enzim učestvuje u biosintezi ubihinona. Ubihinoni iz različitih organisma imaju različiti broj prenilnih jedinica (na primer, ubihinon-6 kod Saccharomyces, ubihinon-9 kod rat i ubihinon-10 kod čoveka). Prirodni supstrat enzima iz različitih organisma ima različiti broj prenilnih jedinica.
Reference uredi
- ↑ Houser, R.M. and Olson, R.E. (1977). „5-Demethylubiquinone-9-methyltransferase from rat liver mitochondria. Characterization, localization, and solubilization”. J. Biol. Chem. 252: 4017-4021. PMID 863914.
- ↑ Leppik, R.A., Stroobant, P., Shineberg, B., Young, I.G. and Gibson, F. (1976). „Membrane-associated reactions in ubiquinone biosynthesis. 2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase”. Biochim. Biophys. Acta 428: 146-156. PMID 769831.
- ↑ Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. (1999). „Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis”. J. Biol. Chem. 274: 21665-21672. PMID 10419476.
- ↑ Jonassen, T. and Clarke, C.F. (2000). „Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis”. J. Biol. Chem. 275: 12381-12387. PMID 10777520.
Literatura uredi
- 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.