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Literature summary for 1.5.1.20 extracted from

  • Matthews, R.G.; Sheppard, C.; Goulding, C.
    Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology (1998), Eur. J. Pediatr., 157, 54-59.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
A177V enzyme is thermolabile Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
S-adenosylmethionine
-
Homo sapiens
S-adenosylmethionine allosteric inhibition Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
77000
-
2 * 77000 Homo sapiens
77000
-
2 * 77000 Sus scrofa

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 77000 Homo sapiens
dimer 2 * 77000 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens
FAD non covalently bound Sus scrofa
FAD flavoprotein with non-covalently bound FAD Escherichia coli