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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

General Stability

General Stability Organism
inclusion of 10% glycerol during purification is essential for stability Sus scrofa

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
74500
-
calculated from amino acid sequence Sus scrofa
77300
-
SDS-PAGE Sus scrofa
210000
-
gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity 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
-
-
Sus scrofa

Storage Stability

Storage Stability Organism
-20°C, for at least 2 weeks in 10% glycerol Sus scrofa

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 77300, SDS-PAGE, gel filtration Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
26.7
-
NADPH
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Sus scrofa
FAD each subunit of the dimer or trimer contains bound FAD Sus scrofa