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Literature summary for 1.5.1.53 extracted from

  • Daubner, S.C.; Matthews, R.G.
    Purification and properties of methylenetetrahydrofolate reductase from pig liver (1982), J. Biol. Chem., 257, 140-145 .
    View publication on PubMed
Search for more literature for 1.5.1.53

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.016
-
 NADPH pH 6.7, 37°C Sus scrofa
0.019
-
 5,10-methylenetetrahydrofolate pH 6.7, 37°C Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
 gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
19.4
-
 pH 6.7, 37°C Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADPH + H+
-
 Sus scrofa 5-methyltetrahydrofolate + NADP+
-
 ?

Subunits

Subunits Comment Organism
? x * 77300, SDS-PAGE, x * 74500, calcuated from sequence Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
26.67
-
 NADPH pH 6.7, 37°C Sus scrofa

Cofactor

Cofactor Comment Organism Structure
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 Sus scrofa

General Information

General Information Comment Organism
metabolism kinetics suggest a ping-pong mechanism for methylenetetrahydrofolate reductase, or a ternary complex mechanism in which NADPH binding precedes 5,10-methylenetetrahydrofolate Sus scrofa