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Literature summary extracted from

  • Misra, S.K.; Bhakuni, V.
    Unique holoenzyme dimers of the tetrameric enzyme Escherichia coli methylenetetrahydrofolate reductase: characterization of structural features associated with modulation of the enzyme's function (2003), Biochemistry, 42, 3921-3928.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.20 overexpression in strain BL21(DE3) Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.20 66000
-
 dimeric enzyme, gel filtration Escherichia coli
1.5.1.20 133000
-
 tetrameric enzyme, gel filtration Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20 recombinant enzyme from strain BL21(DE3) Escherichia coli

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.5.1.20 dissociated enzyme after treatment with 1 M urea, no refolding and renaturation is possible after treatment with 1.2 M NaCl Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 5-methyltetrahydrofolate + NADP+
-
 Escherichia coli 5,10-methylenetetrahydrofolate + NADPH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.20 dimer smallest functional unit of the enzyme Escherichia coli
1.5.1.20 More alterations in the hydrophobic interactions by 1 M urea lead to dissociation of the native tetramer, resulting in stabilization of enzymatically active holoenzyme dimers, at 3 M urea followed by unfolding of the dimers to denatured monomers along with dissociation of FAD from the enzyme subunits, alterations of the electrostatic interactions by 1.2 M NaCl lead to dissociation of the enzyme into inactive, partially denatured dimers Escherichia coli
1.5.1.20 tetramer composed of 2 active dimers Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.5.1.20 5,10-methylenetetrahydrofolate reductase (FADH2)
-
 Escherichia coli
1.5.1.20 5-methylenetetrahydrofolate:NADP+ oxidoreductase
-
 Escherichia coli
1.5.1.20 5-methyltetrahydrofolate:(acceptor) oxidoreductase
-
 Escherichia coli
1.5.1.20 methylenetetrahydrofolate reductase
-
 Escherichia coli
1.5.1.20 methylenetetrahydrofolate reductase (NADPH)
-
 Escherichia coli
1.5.1.20 More EC 1.7.99.5 included with EC 1.5.1.20 Escherichia coli
1.5.1.20 MTHFR
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.20 51
-
 dimeric enzyme, 50% inactivatin at pH 7.2 Escherichia coli
1.5.1.20 58
-
 tetrameric enzyme, 50% inactivatin at pH 7.2 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.20 FAD enzyme-bound Escherichia coli
1.5.1.20 NADPH
-
 Escherichia coli