| Entry |
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| Name |
methylenetetrahydrofolate reductase (NADPH);
MTHFR (gene name);
methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase;
5,10-methylenetetrahydrofolate reductase (NADPH);
5,10-methylenetetrahydrofolic acid reductase (ambiguous);
5,10-CH2-H4folate reductase (ambiguous);
methylenetetrahydrofolate reductase (NADPH2);
5,10-methylenetetrahydrofolate reductase (ambiguous);
methylenetetrahydrofolate reductase (ambiguous);
N5,10-methylenetetrahydrofolate reductase (ambiguous);
5,10-methylenetetrahydropteroylglutamate reductase (ambiguous);
N5,N10-methylenetetrahydrofolate reductase (ambiguous);
methylenetetrahydrofolic acid reductase (ambiguous);
5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect);
5,10-methylenetetrahydrofolate reductase (FADH2) (ambiguous)
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| Class |
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
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| Sysname |
5-methyltetrahydrofolate:NADP+ oxidoreductase
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| Reaction(IUBMB) |
5-methyltetrahydrofolate + NADP+ = 5,10-methylenetetrahydrofolate + NADPH + H+ [RN: R01224]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
A flavoprotein (FAD). The enzyme from yeast and mammals catalyses a physiologically irreversible reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using NADPH as the electron donor. It plays an important role in folate metabolism by regulating the distribution of one-carbon moieties between cellular methylation reactions and nucleic acid synthesis. The enzyme contains an N-terminal catalytic domain and a C-terminal allosteric regulatory domain that binds S-adenosyl-L-methionine, which acts as an inhibitor. cf. EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]; and EC 1.5.7.1, methylenetetrahydrofolate reductase (ferredoxin).
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| History |
EC 1.5.1.53 created 2021
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| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K25004 | methylenetetrahydrofolate reductase (NADPH) |
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| Genes |
» show all
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| Reference |
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| Authors |
DONALDSON KO, KERESZTESY JC. |
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| Title |
Naturally occurring forms of folic acid. I. "Prefolic A": preparation of concentrate and enzymatic conversion to citrovorum factor. |
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| Journal |
J Biol Chem 234:3235-40 (1959) |
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| Reference |
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| Authors |
Kutzbach C, Stokstad EL. |
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| Title |
Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. |
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| Journal |
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| Reference |
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| Authors |
Daubner SC, Matthews RG. |
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| Title |
Purification and properties of methylenetetrahydrofolate reductase from pig liver. |
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| Journal |
J Biol Chem 257:140-5 (1982) |
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| Reference |
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| Authors |
Zhou J, Kang SS, Wong PW, Fournier B, Rozen R. |
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| Title |
Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver. |
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| Journal |
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| Reference |
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| Authors |
Roje S, Chan SY, Kaplan F, Raymond RK, Horne DW, Appling DR, Hanson AD. |
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| Title |
Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo. |
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| Journal |
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| Reference |
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| Authors |
Froese DS, Kopec J, Rembeza E, Bezerra GA, Oberholzer AE, Suormala T, Lutz S, Chalk R, Borkowska O, Baumgartner MR, Yue WW. |
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| Title |
Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.5.1.53 |
| ExPASy - ENZYME nomenclature database: | 1.5.1.53 |
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