Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
1.5.1.20
-
 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.20
-
 Escherichia coli

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.20 0.0039
-
 5,10-methylenetetrahydrofolate
-
 Escherichia coli
1.5.1.20 0.017
-
 NADH
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.20 108000
-
 A177V mutant enzyme, gel filtration Escherichia coli
1.5.1.20 190000
-
 wild type enzyme, gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Escherichia coli P0AEZ1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20 homogeneity Escherichia coli

Subunits

EC Number Subunits Comment Organism
1.5.1.20 tetramer gel filtration Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.20 23.5
-
 NADH
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.20 FAD
-
 Escherichia coli