Metilentetrahidrofolat reduktaza (NAD(P)H)

Metilentetrahidrofolat reduktaza (NAD(P)H)
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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PMC articles
PubMed articles
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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)+ ⇌ {\displaystyle \rightleftharpoons } 5,10-metilintetrahidrofolat + NAD(P)H + H+

Ova enzim je flavoprotein (FAD). Menadion može takođe da služi kao elektronski akceptor.

Reference

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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

  • 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. 

Spoljašnje veze

  • MeSH Methylenetetrahydrofolate+reductase+(NAD(P)H)
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6