Metilentetrahidrofolat dehidrogenaza (NADP+)
| Metilentetrahidrofolat dehidrogenaza (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Metilentetrahidrofolat dehidrogenaza dimer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.5.1.5 | ||||||||
| CAS broj | 9029-14-5 | ||||||||
| 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 dehidrogenaza (NADP+) (EC 1.5.1.5, N5,N10-metilintetrahidrofolat dehidrogenaza, 5,10-metilintetrahidrofolat:NADP oksidoreduktaza, 5,10-metilintetrahidrofolat dehidrogenaza, metilintetrahidrofolat dehidrogenaza, metilintetrahidrofolat dehidrogenaza (NADP)) je enzim sa sistematskim imenom 5,10-metilintetrahidrofolat:NADP+ oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5,10-metilintetrahidrofolat + NADP+ 5,10-metheniltetrahidrofolat + NADPH + H+
Kod eukariota se ovaj enzim javlja kao trifunkcionalni enzim, koji takođe deluje kao meteniltetrahidrofolatna ciklohidrolaza (EC 3.5.4.9) i format---tetrahidrofolatna ligaza (EC 6.3.4.3). On se kod nekih prokariota javlja koa bifunkcionalanni enzim, koji takođe funkcioniše kao meteniltetrahidrofolatna ciklohidrolaza (EC 3.5.4.9).
Reference[uredi | uredi kod]
- ↑ Hatefi, Y., Osborn, M.J., Kay, L.D. and Huennekens, F.M. (1957). „Hydroxymethyl tetrahydrofolic dehydrogenase”. J. Biol. Chem. 227: 637-647. PMID 13462986.
- ↑ Osborn, M.J. and Huennekens, F.M. (1957). „Participation of anhydroleucovorin in the hydroxymethyl tetrahydrofolic dehydrogenase system”. Biochim. Biophys. Acta 26: 646-647. PMID 13499428.
- ↑ Ramasastri, B.V. and Blakley, R.L. (1962). „5,10-Methylenetetrahydrofolic acid dehydrogenase from Bakers’ yeast. I. Partial purification and some properties”. J. Biol. Chem. 237: 1982-1988. PMID 14490085.
- ↑ Yeh, Y.-C. and Greenberg, D.M. (1965). „Purification and properties of N5,N10-methylenetetrahydrofolate dehydrogenase of calf thymus”. Biochim. Biophys. Acta 105: 279-291. PMID 4379024.
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.