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Literature summary for 1.5.1.20 extracted from

  • Guenther, B.D.; Sheppard, C.A.; Tran, P.; Rozen, R.; Matthews, R.G.; Ludwig, M.L.
    The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia (1999), Nat. Struct. Biol., 6, 359-365.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
A177V mutation does not affect Km or kcat values for NADH or 5,10-methylenetetrahydrofolate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0039
-
5,10-methylenetetrahydrofolate
-
Escherichia coli
0.017
-
NADH
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
108000
-
A177V mutant enzyme, gel filtration Escherichia coli
190000
-
wild type enzyme, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEZ1
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity Escherichia coli

Subunits

Subunits Comment Organism
tetramer gel filtration Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
23.5
-
NADH
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD
-
Escherichia coli