Metilentetrahidrofolat reduktaza (NAD(P)H)
| Metilentetrahidrofolat reduktaza (NAD(P)H) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 1.5.1.20 | ||||||||
| CAS broj | 71822-25-8 | ||||||||
| 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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Metilentetrahidrofolat reduktaza (NAD(P)H) (EC 1.5.1.20, metilintetrahidrofolat (redukovani nikotinamid adenin dinukleotid fosfat) reduktaza, 5,10-metilintetrahidrofolat reduktaza (NADPH), 5,10-metilintetrahidrofolna kiselina reduktaza, 5,10-CH2-H4folat reduktaza, metilintetrahidrofolat reduktaza (NADPH2), 5-metiltetrahidrofolat:NAD+ oksidoreduktaza, 5-metiltetrahidrofolat:NAD+ oksidoreduktaza, metilintetrahidrofolat (redukovani riboflavin adenin dinukleotid) reduktaza, 5,10-metilintetrahidrofolat reduktaza, metilintetrahidrofolat reduktaza, N5,10-metilintetrahidrofolat reduktaza, 5,10-metilintetrahidropteroilglutamat reduktaza, N5,N10-metilintetrahidrofolat reduktaza, metilintetrahidrofolna kiselina reduktaza, 5,10-metilintetrahidrofolat reduktaza (FADH2), MetF, metilintetrahidrofolat reduktaza (NADPH), 5-metiltetrahidrofolat:NADP+ oksidoreduktaza) je enzim sa sistematskim imenom 5-metiltetrahidrofolat:NAD(P)+ oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5-metiltetrahidrofolat + NAD(P)+ 5,10-metilintetrahidrofolat + NAD(P)H + H+
Ova enzim je flavoprotein (FAD). Menadion može takođe da služi kao elektronski akceptor.
Reference[uredi | uredi kod]
- ↑ Daubner, S.C. and Matthews, R.T. (1982). „Purification and properties of methylenetetrahydrofolate reductase from pig liver”. J. Biol. Chem. 257: 140-145. PMID 6975779.
- ↑ Kutzbach, C. and Stokstad, E.L.R. (1971). „Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine”. Biochim. Biophys. Acta 250: 459-477. PMID 4399897.
- ↑ Sheppard, C.A., Trimmer, E.E. and Matthews, R.G. (1999). „Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli”. J. Bacteriol. 181: 718-725. PMID 9922232.
- ↑ Guenther, B.D., Sheppard, C.A., Tran, P., Rozen, R., Matthews, R.G. and Ludwig, M.L. (1999). „The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia”. Nat. Struct. Biol. 6: 359-365. PMID 10201405.
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.