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Literature summary for 1.5.1.6 extracted from

  • Kutzbach, C.; Stokstad, E.L.R.
    Partial purification of a 10-formyl-tetrahydrofolate: NADP oxidoreductase from mammalian liver (1968), Biochem. Biophys. Res. Commun., 30, 111-117.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
tetrahydrofolate
-
Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
200fold partial purification Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.305
-
-
Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + NADP+ + H2O specific for NADP+ Sus scrofa tetrahydrofolate + CO2 + NADPH + H+
-
?
additional information not as substrate: 5-formyltetrahydrofolate Sus scrofa ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 in Tris buffer 30% faster reaction than in phosphate buffer Sus scrofa

Cofactor

Cofactor Comment Organism Structure
10-formyltetrahydrofolate 10-formyltetrahydrofolate Sus scrofa
additional information no effect: NADPH Sus scrofa
NAD+ less than 5% of the activity with NADP+ Sus scrofa
NADP+ specific for Sus scrofa
tetrahydrofolate
-
Sus scrofa