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Literature summary extracted from

  • Pearson, A.G.M.; Turner, A.J.
    Folate-dependent 1-carbon transfer to biogenic amines mediated by methylenetetrahydrofolate reductase (1975), Nature, 258, 173-174.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.20 2,4-dihydroxyphenylacetic acid at 0.01 M Sus scrofa
1.5.1.20 S-adenosylmethionine inhibition partially reversed by S-adenosylhomocysteine Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.20 170000 190000 gel filtration, single enzyme with methylenetetrahydrofolate reductase and dopamine methyltransferase activity Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + NADPH Sus scrofa initial enzyme in pathway leading to synthesis of S-adenosylmethionine ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Sus scrofa
-
a single enzyme with methylenetetrahydrofolate reductase and dopamine methyltransferase activity
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.20 liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.20 0.1
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + NADPH
-
Sus scrofa 5-methyltetrahydrofolate + NADP+
-
?
1.5.1.20 5,10-methylenetetrahydrofolate + NADPH initial enzyme in pathway leading to synthesis of S-adenosylmethionine Sus scrofa ?
-
?