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Literature summary extracted from

  • Kutzbach, C.; Stokstad, E.
    Mammalian methylenetetrahydrofolate reductase partial purification, properties, and inhibition by S-adenosylmethionine (1971), Biochim. Biophys. Acta, 250, 459-477 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.53 S-adenosyl-L-methionine strong inhibition Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.53 0.021
-
5,10-methylenetetrahydrofolate pH 7.2, 30°C Sus scrofa
1.5.1.53 0.033
-
NADPH pH 7.2, 30°C Sus scrofa
1.5.1.53 0.31
-
NADH pH 7.2, 30°C Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.53 5,10-methylenetetrahydrofolate + NADPH + H+ Sus scrofa
-
5-methyltetrahydrofolate + NADP+
-
?
1.5.1.53 additional information Sus scrofa enzyme is specific for the (+) diastereoisomer of 5,10-methylenetetrahydrofolate as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.8.1.4) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.5.2 ) activity ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.53 Sus scrofa
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.53 5,10-methylenetetrahydrofolate + NADH + H+ NADH is a poor cofactor Sus scrofa 5-methyltetrahydrofolate + NAD+
-
?
1.5.1.53 5,10-methylenetetrahydrofolate + NADPH + H+
-
Sus scrofa 5-methyltetrahydrofolate + NADP+
-
?
1.5.1.53 5-methyltetrahydrofolate + oxidized menadione
-
Sus scrofa 5,10-methylenetetrahydrofolate + reduced menadione
-
?
1.5.1.53 additional information enzyme is specific for the (+) diastereoisomer of 5,10-methylenetetrahydrofolate as its physiological substrate. In addition, the enzyme exhibits a strong NADPH-specific diaphorase (reduced-NAD:lipoamide oxidoreductase, EC 1.8.1.4) or menadione reductase (reduced-NAD(P):(acceptor) oxidoreductase, EC 1.6.5.2 ) activity Sus scrofa ?
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.53 NADH NADPH is 10fold preferred over NADH Sus scrofa
1.5.1.53 NADPH enzyme is specifc for NADPH Sus scrofa