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Literature summary extracted from

  • Igari, S.; Ohtaki, A.; Yamanaka, Y.; Sato, Y.; Yohda, M.; Odaka, M.; Noguchi, K.; Yamada, K.
    Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8 (2011), PLoS ONE, 6, e23716.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.20 expressed in Escherichia coli BL21(DE3) cells Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.20 hanging drop vapor diffusion method, using 0.1 M sodium acetate buffer (NaOAc, pH 4.3,4.5), 1 M lithium chloride, 10% (w/v) polyethylene glycol 6000, 10-20% (v/v) glycerol, and 2-5% (v/v) dioxane, at 20°C Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.20 A222V the mutant shows enhanced instability upon loss of FAD Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.20 0.18
-
 (6R)-5,10-methylenetetrahydrofolate at pH 7.0 and 50°C Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.20 (6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+ Thermus thermophilus
-
 (6S)-5-methyltetrahydrofolate + NAD(P)+
-
 r
1.5.1.20 (6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+ Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 (6S)-5-methyltetrahydrofolate + NAD(P)+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Thermus thermophilus Q5SLG6
-
-
1.5.1.20 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SLG6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20 Toyopearl SuperQ-650M column chromatography and nickel affinity column chromatography Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 (6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+
-
 Thermus thermophilus (6S)-5-methyltetrahydrofolate + NAD(P)+
-
 r
1.5.1.20 (6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (6S)-5-methyltetrahydrofolate + NAD(P)+
-
 r

Subunits

EC Number Subunits Comment Organism
1.5.1.20 heterodimer x-ray crystallography Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.5.1.20 MTHFR
-
 Thermus thermophilus
1.5.1.20 NADH:CH2-H4folate oxidoreductase
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.20 FAD the enzyme contains one FAD prosthetic group bound per dimer. Km for FAD is 0.005 mM. The enzyme activity of the FAD-replete enzyme is approximately 50% compared to the normal purified enzyme Thermus thermophilus
1.5.1.20 NADH
-
 Thermus thermophilus
1.5.1.20 NADPH
-
 Thermus thermophilus