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Literature summary for 1.5.1.5 extracted from

  • Gardam, M.A.; Mejia, N.R.; MacKenzie, R.E.
    The NADP-dependent trifunctional methylenetetrahydrofolate dehydrogenase purified from mouse liver is immunologically distinct from the mouse NAD-dependent [corrected] bifunctional enzyme [published erratum appears in Biochem Cell Biol 1988 May;66(5):459] (1988), Biochem. Cell Biol., 66, 66-70.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
 NADP+
-
 Mus musculus
0.015
-
 5,10-methylenetetrahydrofolate
-
 Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + NADP+ Mus musculus
-
 5,10-methenyltetrahydrofolate + NADPH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
trifunctional enzyme: methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrase, formyltetrahydrofolate synthetase Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.53
-
-
 Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + NADP+
-
 Mus musculus 5,10-methenyltetrahydrofolate + NADPH + H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Mus musculus