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Information on EC 1.5.1.53 - methylenetetrahydrofolate reductase (NADPH)
for references in articles please use BRENDA:EC1.5.1.53
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
1.5.1.53 methylenetetrahydrofolate reductase (NADPH)
IUBMB Comments
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).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
5,10-CH2-H4folate reductase, 5,10-methylenetetrahydrofolate reductase, 5,10-methylenetetrahydrofolate reductase (FADH2), 5,10-methylenetetrahydrofolate reductase (NADPH), 5,10-methylenetetrahydrofolic acid reductase, 5,10-methylenetetrahydropteroylglutamate reductase, 5-methyltetrahydrofolate:(acceptor) oxidoreductase, MET13, methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase, methylenetetrahydrofolate reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-CH2-H4folate reductase
-
-
ambiguous
-
5,10-methylenetetrahydrofolate reductase
-
-
ambiguous
-
5,10-methylenetetrahydrofolate reductase (FADH2)
-
-
ambiguous
-
5,10-methylenetetrahydrofolate reductase (NADPH)
-
-
-
-
5,10-methylenetetrahydrofolic acid reductase
-
-
ambiguous
-
5,10-methylenetetrahydropteroylglutamate reductase
-
-
ambiguous
-
5-methyltetrahydrofolate:(acceptor) oxidoreductase
-
-
incorrect
-
methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase
-
-
-
-
methylenetetrahydrofolate reductase
-
-
ambiguous
-
methylenetetrahydrofolate reductase (NADPH2)
-
-
-
-
methylenetetrahydrofolic acid reductase
-
-
ambiguous
-
MTHFR
N5,10-methylenetetrahydrofolate reductase
-
-
ambiguous
-
N5,N10-methylenetetrahydrofolate reductase
-
-
ambiguous
-
MTHFR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + NADP+ = 5,10-methylenetetrahydrofolate + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
folate transformations I
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SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:NADP+ oxidoreductase
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + NADPH
5-methyltetrahydrofolate + NADP+
-
Substrates: -
Products: -
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5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
6,7-dimethyl-7,8-dihydropterin + NADH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
-
Substrates: -
Products: -
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?
dihydrobiopterin + NADPH + H+
tetrahydrobiopterin + NADP+
-
Substrates: -
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?
5,10-methylenetetrahydrofolate + NADH + H+
5-methyltetrahydrofolate + NAD+
Substrates: -
Products: -
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?
5,10-methylenetetrahydrofolate + NADH + H+
5-methyltetrahydrofolate + NAD+
Substrates: -
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5,10-methylenetetrahydrofolate + NADH + H+
5-methyltetrahydrofolate + NAD+
-
Substrates: -
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5,10-methylenetetrahydrofolate + NADH + H+
5-methyltetrahydrofolate + NAD+
-
Substrates: NADH is a poor cofactor
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?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
-
Substrates: -
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?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
Substrates: -
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?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
Substrates: -
Products: -
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?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
Substrates: -
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?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
-
Substrates: -
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?
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
-
Substrates: -
Products: -
Products: -
?
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
-
Substrates: -
Products: -
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?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
-
Substrates: -
Products: -
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?
NADPH + H+ + oxidized menadione
NADP+ + reduced menadione
-
Substrates: -
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?
additional information
?
-
-
Substrates: enzyme is specific for the (+) diastereoisomer of 5,10-methylenetetrahydrofolate as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.8.1.4) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.5.2 ) activity
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additional information
?
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-
Substrates: no substrate: dihydrofolate
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additional information
?
-
-
Substrates: under Vmax conditions, the turnover numbers for the NADPH-linked reductions of the quinonoid forms of 6,7-dimethyldihydropterin, dihydrobiopterin, and dihydrofolate are all about the same as that for the reduction of methylenetetrahydrofolate. The reduction of quinonoid dihydropterins is inhibited by S-adenosyl-L-methionine and dihydropteroylhexaglutamate
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
-
Substrates: -
Products: -
Products: -
?
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
-
Substrates: -
Products: -
Products: -
?
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is specific for the (+) diastereoisomer of 5,10-methylenetetrahydrofolate as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.8.1.4) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.5.2 ) activity
Products: -
Products: -
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additional information
?
-
-
Substrates: no substrate: dihydrofolate
Products: -
Products: -
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
reduction of 1 mol of enzyme-bound FAD requires 1.1 mol of NADPH. The reduced enzyme can be reoxidized by (6-R)-methylenetetrahydrofolate, again with nearly 1:1 stoichiometry
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-SKI-72
presence of (S)-SKI-72 leads to a Tm shift of approximately 10 degrees
NADPH
-
substrate inhibition. NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states
S-adenosyl-L-methionine
presence of S-adenosyl-L-methionine leads to a Tm shift of about 4 degrees
S-adenosyl-L-methionine
-
NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.038
5-methyltetrahydrofolate
-
pH not specified in the publication, temperature not specified in the publication
0.011
5,10-methylenetetrahydrofolate
wild-type, cosubstrate NADPH, pH 7.2, temperature not specified in the publication
0.0224
5,10-methylenetetrahydrofolate
wild-type, pH 6.6, temperature not specified in the publication
0.0255
5,10-methylenetetrahydrofolate
truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication
0.106
5,10-methylenetetrahydrofolate
Chimera-1, cosubstrate NADPH, pH 7.2, temperature not specified in the publication
0.152
5,10-methylenetetrahydrofolate
Chimera-1, cosubstrate NADH, pH 7.2, temperature not specified in the publication
2.16
NADH
truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication
3.76
NADH
wild-type, pH 6.6, temperature not specified in the publication
0.011
NADPH
wild-type, pH 7.2, temperature not specified in the publication
0.0235
NADPH
truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication
0.0355
NADPH
wild-type, pH 6.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
40.7
5,10-methylenetetrahydrofolate
wild-type, pH 6.6, temperature not specified in the publication
51.4
5,10-methylenetetrahydrofolate
truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00078
(S)-SKI-72
pH not specified in the publication, temperature not specified in the publication
0.0025
S-adenosyl-L-methionine
wild-type, pH 6.6, temperature not specified in the publication
0.0058
S-adenosyl-L-methionine
pH not specified in the publication, temperature not specified in the publication
0.021
S-adenosyl-L-methionine
truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.367
-
substrate 5-methyltetrahydrofolate, pH not specified in the publication, temperature not specified in the publication
19.4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
kinetics suggest a ping-pong mechanism for methylenetetrahydrofolate reductase, or a ternary complex mechanism in which NADPH binding precedes 5,10-methylenetetrahydrofolate
metabolism
-
Methylenetetrahydrofolate reductase presents reacts with both NADPH and 5,10-methylenetetrahydrofolate at the si face. The reaction involves successive hydride transfers to and from the flavin cofactor. NADP+ dissociates before 5,10-methylenetetrahydrofolate binds the reduced enzyme
metabolism
-
methylenetetrahydrofolate reductase stereospecifically removes the pro-S hydrogen from the 4-position of NADPH. The oxidation of NADPH is largely or entirely rate limiting in the reductive half-reaction and in NADPH-menadione oxidoreductase turnover at saturating menadione concentration
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MTHR2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
600
0
68560
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylation of up to 11 residues. Phosphorylation does not alter MTHFR kinetic parameters
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of human MTHFR at 2.5 A resolution reveals a unique architecture, appending the well-conserved catalytic TIM-barrel to a eukaryote-only SAM-binding domain. The latter domain provides the predominant interface for MTHFR homo-dimerization and positions the N-terminal serine-rich phosphorylation region near the C-terminal SAM-binding domain. MTHFR phosphorylation, identified on 11 N-terminal residues (16 in total), increases sensitivity to SAM binding and inhibition. The 25-amino-acid inter-domain linker enables conformational plasticity and may be a key mediator of SAM regulation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
expression of a truncated protein, residues 38-644, lacking the phosphorylation sites. Nonphosphorylated MHTFR has similar kinetic values as wild-type
additional information
expression of constructs encompassing the full-length, just the catalytic and regulatory domain (amino acids 38-644), and encompassing the regulatory domain and part of the linker region (amino acids 348-656)
additional information
chromosomal copy of MET13 is replaced by an Arabidopsis thaliana MTHFR cDNA (AtMTHFR-1) or by a chimeric sequence (Chimera-1) comprising the yeast N-terminal domain and the AtMTHFR-1 C-terminal domain. Chimera-1 uses both NADH and NADPH and is insensitive to S-adenosyl-L-methionine. Engineered yeast expressing Chimera-1 accumulates 140fold more S-adenosyl-L-methionine and 7fold more methionine than does the wild-type and grows normally. Yeast expressing AtMTHFR-1 accumulates 8fold more S-adenosyl-L-methionine
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
sensitive radioenzymatic assay that measures directly the reductive catalysis of N ,N -methylenetetrahydrofolate. The radio-labeled substrate, [ C14]N ,N -methyl enetetrahydrofolate, is prepared by condensation of [C14]formaldehyde with tetrahydrofolate. Its stability is maintained for several months by storage at -80°C in a pH 9.5 buffer
medicine
medicine
-
patients with severe methylenetetrahydrofolate reductase deficiency show neurologic disorders, mental retardation, and rapid deterioration
medicine
testing of 478 individuals with myelomeningocele for attention-deficit hyperactivity disorder (ADHD) behavior plus genotyping for seven single nucleotide polymorphisms in the MTHFR gene. 28.7% of myelomeningocele participants exhibit rating scale elevations consistent with ADHD, of these 70.1% have scores consistent with the predominantly inattentive subtype. There is a positive association between the SNP rs4846049 in the 39-untranslated region of the MTHFR gene and the attention-deficit hyperactivity disorder phenotype in myelomeningocele participants
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daubner, S.C.; Matthews, R.G.
Purification and properties of methylenetetrahydrofolate reductase from pig liver
J. Biol. Chem.
257
140-145
1982
Sus scrofa
brenda
Zhou, J.; Kang, S.S.; Wong, P.W.; Fournier, B.; Rozen, R.
Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver
Biochem. Med. Metab. Biol.
43
234-242
1990
Homo sapiens
brenda
Matthews, R.; Bobbie, H.
Inhibition of pig liver methylenetetrahydrofolate reductase by dihydrofolate some mechanistic and regulatory implications
Biochemistry
18
4845-4851
1979
Sus scrofa
brenda
Vanoni, M.A.; Matthews, R.G.
Kinetic isotope effects on the oxidation of reduced nicotinamide adenine dinucleotide phosphate by the flavoprotein methylenetetrahydrofolate reductase
Biochemistry
23
5272-5279
1984
Sus scrofa
brenda
Kutzbach, C.; Stokstad, E.
Mammalian methylenetetrahydrofolate reductase partial purification, properties, and inhibition by S-adenosylmethionine
Biochim. Biophys. Acta
250
459-477
1971
Sus scrofa
brenda
Bezerra, G.A.; Holenstein, A.; Foster, W.R.; Xie, B.; Hicks, K.G.; Buerer, C.; Lutz, S.; Mukherjee, A.; Sarkar, D.; Bhattacharya, D.; Rutter, J.; Talukdar, A.; Brown, P.J.; Luo, M.; Shi, L.; Froese, D.S.; Yue, W.W.
Identification of small molecule allosteric modulators of 5,10-methylenetetrahydrofolate reductase (MTHFR) by targeting its unique regulatory domain
Biochimie
183
100-107
2021
Homo sapiens (P42898)
brenda
Sumner, J.; Matthews, R.
Stereochemistry and mechanism of hydrogen transfer between NADPH and methylenetetrahydrofolate in the reaction catalyzed by methylenetetrahydrofolate reductase from pig liver
J. Am. Chem. Soc.
114
6949-6956
1992
Sus scrofa
-
brenda
Sobti, P.; Rothenberg, S.P.; Quadros, E.V.
Radioenzymatic assay for reductive catalysis of N(5),N(10)-methylenetetrahydrofolate by methylenetetrahydrofolate reductase
J. Biochem. Biophys. Methods
46
11-20
2000
Rattus norvegicus (D4A7E8)
brenda
Matthews, R.G.; Kaufman, S.
Characterization of the dihydropterin reductase activity of pig liver methylenetetrahydrofolate reductase
J. Biol. Chem.
255
6014-6017
1980
Sus scrofa
brenda
Daubner, S.C.; Matthews, R.G.
Purification and properties of methylenetetrahydrofolate reductase from pig liver
J. Biol. Chem.
257
140-145
1982
Sus scrofa
brenda
Jencks, D.A.; Mathews, R.G.
Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium
J. Biol. Chem.
262
2485-2493
1987
Sus scrofa
brenda
Roje, S.; Chan, S.Y.; Kaplan, F.; Raymond, R.K.; Horne, D.W.; Appling, D.R.; Hanson, A.D.
Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo
J. Biol. Chem.
277
4056-4061
2002
Saccharomyces cerevisiae (P53128)
brenda
Froese, D.; Kopec, J.; Rembeza, E.; Bezerra, G.; Oberholzer, A.; Suormala, T.; Lutz, S.; Chalk, R.; Borkowska, O.; Baumgartner, M.; Yue, W.
Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition
Nat. Commun.
9
2261
2018
Homo sapiens (P42898)
brenda
Yu, L.; Xu, J.; Liu, L.; Bian, X.; Liu, Y.
Purification and catalytic properties of methylenetetrahydrofolate reductase
Pharm. Biotechnol.
18
300-303
2011
Sus scrofa
-
brenda
Spellicy, C.J.; Northrup, H.; Fletcher, J.M.; Cirino, P.T.; Dennis, M.; Morrison, A.C.; Martinez, C.A.; Au, K.S.
Folate metabolism gene 5,10-methylenetetrahydrofolate reductase (MTHFR) is associated with ADHD in myelomeningocele patients
PLoS ONE
7
e51330
2012
Homo sapiens (P42898)
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.1.53)
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