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Literature summary for 1.5.1.20 extracted from

  • Matthews, R.G.; Daubner, S.C.
    Modulation of methylenetetrahydrofolate reductase activity by S-adenosylmethionine and by dihydrofolate and its polyglutamate analogues (1982), Adv. Enzyme Regul., 20, 123-131.
    View publication on PubMed
Search for more literature for 1.5.1.20

Inhibitors

Inhibitors Comment Organism Structure
dihydrofolate competitive with respect to 5,10-methylenetetrahydrofolate and uncompetitive with respect to NADPH Sus scrofa
dihydropteroylpolyglutamate
-
 Sus scrofa
Polyglutamate analogues
-
 Sus scrofa
S-adenosylmethionine inhibition partially reversed by S-adenosylhomocysteine Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + NADPH Sus scrofa branch point in folate metabolism ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity 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
-
 Sus scrofa 5-methyltetrahydrofolate + NADP+
-
 ir
5,10-methylenetetrahydrofolate + NADPH branch point in folate metabolism Sus scrofa ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Sus scrofa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information dihydropteroylpolyglutamate inhibitors with different numbers of glutamyl residues Sus scrofa
0.0065
-
 dihydrofolate
-
 Sus scrofa