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Literature summary for 1.5.1.20 extracted from

  • Yu, L.; Xu, J.; Liu, L.; Bian, X.; Liu, Y.
    Purification and catalytic properties of methylenetetrahydrofolate reductase (2011), Pharm. Biotechnol., 18, 300-303+307.
No PubMed abstract available
Search for more literature for 1.5.1.20

Inhibitors

Inhibitors Comment Organism Structure
S-adenosylmethionine
-
 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0703
-
 5,10-methylenetetrahydrofolate at pH 6.8 and 37°C Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + NADPH + H+ Sus scrofa
-
 5-methyltetrahydrofolate + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
salting out and DEAE Sepharose column chromatography Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
MTHFR
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADPH the optimum concentration is 1.2 mM Sus scrofa