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Literature summary extracted from

  • Yamada, K.; Chen, Z.; Rozen, R.; Matthews, R.G.
    Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase (2001), Proc. Natl. Acad. Sci. USA, 98, 14853-14858.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.5.1.20 medicine C677T mution of MTHRF gene is the most frequent genetic cause of mild hyperhomocysteinemia, a risk factor for cardiovascular disease Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.20 expression of recombinant human MTHFR at high levels in Sf9 cells from Spodoptera frugiperda by using a baculovirus expression system Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.20 A177V enzyme with decreased affinity for its FAD cofactor Escherichia coli
1.5.1.20 A222V most frequent genetic cause of mild hyperhomocysteinemia, enzyme with enhanced propensity to dissociate into monomers and to lose its FAD cofactor on dilution, increased thermolability of enzyme activity Homo sapiens
1.5.1.20 E429A A1298C mutation of the MTHRF gene, enzyme with indistinguishable properties from the wild-type Homo sapiens
1.5.1.20 additional information C677T mutation in MTHFR gene is a polymorphism which leads to the substitution of Ala-222 by valine Homo sapiens
1.5.1.20 additional information A1298C mutation of the MTHFR gene, which leads to the substitution of Glu-429 by alanine Homo sapiens

General Stability

EC Number General Stability Organism
1.5.1.20 methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution Escherichia coli
1.5.1.20 methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.20 S-adenosylmethionine strong, reversible allosteric inhibition, prevented by S-adenosylhomocysteine Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.20 33000
-
4 * 33000 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + NADPH Homo sapiens physiological NADPH-CH2-H4folate oxidoreductase activity 5-methyltetrahydrofolate + NADP+ 5-methyltetrahydrofolate is the major methyl donor for the conversion of homocysteine to methionine ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Escherichia coli
-
-
-
1.5.1.20 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20 62fold purification of recombinant enzyme, expressed in Sf9 cells from Spodoptera frugiperda Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.20 12.4
-
recombinant enzyme Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + NADPH physiological NADPH-CH2-H4folate oxidoreductase activity Homo sapiens 5-methyltetrahydrofolate + NADP+ 5-methyltetrahydrofolate is the major methyl donor for the conversion of homocysteine to methionine ?
1.5.1.20 5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: NADPH as reduced acceptor Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
?
1.5.1.20 5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: NADPH as reduced acceptor Homo sapiens 5-methyltetrahydrofolate + oxidized acceptor
-
?
1.5.1.20 5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: NADH as reduced acceptor Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
?

Subunits

EC Number Subunits Comment Organism
1.5.1.20 dimer
-
Homo sapiens
1.5.1.20 homotetramer 4 * 33000 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.20 additional information
-
thermolability is enhanced when the FAD cofactor dissociates form enzyme Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.20 FAD flavoprotein with FAD as cofactor Escherichia coli
1.5.1.20 FAD flavoprotein with FAD as cofactor Homo sapiens
1.5.1.20 FAD FAD is essential for electron transfer between NADH and methylenetetrahydrofolate Escherichia coli
1.5.1.20 NADH
-
Escherichia coli
1.5.1.20 NADPH
-
Escherichia coli
1.5.1.20 NADPH
-
Homo sapiens