EC 1.5.1.20 - Methylenetetrahydrofolate reductase [NAD(P)H]

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IntEnz Enzyme Nomenclature
EC 1.5.1.20

Names

Accepted name:
methylenetetrahydrofolate reductase [NAD(P)H]
Other names:
5,10-CH2-H4folate reductase
5,10-methylenetetrahydrofolate reductase (NADPH)
5,10-methylenetetrahydrofolic acid reductase
methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase
5,10-methylenetetrahydrofolate reductase (FADH2)
5,10-methylenetetrahydrofolate reductase
5,10-methylenetetrahydropteroylglutamate reductase
5-methyltetrahydrofolate:(acceptor) oxidoreductase [incorrect]
5-methyltetrahydrofolate:NAD oxidoreductase
5-methyltetrahydrofolate:NAD+ oxidoreductase
5-methyltetrahydrofolate:NADP+ oxidoreductase
methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase
methylenetetrahydrofolate reductase
methylenetetrahydrofolate reductase (NADPH)
methylenetetrahydrofolate reductase (NADPH2)
methylenetetrahydrofolic acid reductase
N5,10-methylenetetrahydrofolate reductase
N5,N10-methylenetetrahydrofolate reductase
MetF
MTHFR
Systematic name:
5-methyltetrahydrofolate:NAD(P)+ oxidoreductase

Reactions

Cofactor

Comments:

A flavoprotein (FAD). Menadione can also serve as an electron acceptor.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004489
CAS Registry Number: 71822-25-8
UniProtKB/Swiss-Prot: (25) [show] [UniProt]

References

  1. Daubner, S.C. and Matthews, R.T.
    Purification and properties of methylenetetrahydrofolate reductase from pig liver.
    J. Biol. Chem. 257: 140-145 (1982). [PMID: 6975779]
  2. Kutzbach, C. and Stokstad, E.L.R.
    Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine.
    Biochim. Biophys. Acta 250: 459-477 (1971). [PMID: 4399897]
  3. Sheppard, C.A., Trimmer, E.E. and Matthews, R.G.
    Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli.
    J. Bacteriol. 181: 718-725 (1999). [PMID: 9922232]
  4. Guenther, B.D., Sheppard, C.A., Tran, P., Rozen, R., Matthews, R.G. and Ludwig, M.L.
    The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
    Nat. Struct. Biol. 6: 359-365 (1999). [PMID: 10201405]

[EC 1.5.1.20 created 1978 as EC 1.1.1.171, transferred 1984 to EC 1.5.1.20 (EC 1.7.99.5 incorporated 2005), modified 2005]