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Literature summary for 1.5.1.20 extracted from

  • Katzen, H.M.; Buchanan, J.M.
    Enzymatic synthesis of the methyl group of methionine. VIII. Repression ûderepression, purification, and properties of 5,10-methylene-tetrahydrofolate reductase from Escherichia coli (1965), J. Biol. Chem., 240, 825-835.
    View publication on PubMed

General Stability

General Stability Organism
FAD stabilizes Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information vitamin B12 and methionine can repress enzyme biosynthesis Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methylenetetrahydrofolate + FADH2 Escherichia coli biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine 5-methyltetrahydrofolate + FAD
-
?
5,10-methylenetetrahydrofolate + FADH2 Escherichia coli 113-3 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine 5-methyltetrahydrofolate + FAD
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli 113-3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
about 100fold purification Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methylenetetrahydrofolate + FADH2 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine Escherichia coli 5-methyltetrahydrofolate + FAD
-
?
5,10-methylenetetrahydrofolate + FADH2 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine Escherichia coli 113-3 5-methyltetrahydrofolate + FAD
-
?
5,10-methylenetetrahydrofolate + reduced acceptor under anaerobic conditions and in absence of electron acceptors, the equilibrium lies far to the 5-methyltetrahydrofolate formation, inclusion of menadione or oxygen promotes the oxidation of 5-methyltetrahydrofolate Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: reduced acceptor is FADH2 Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor under anaerobic conditions and in absence of electron acceptors, the equilibrium lies far to the 5-methyltetrahydrofolate formation, inclusion of menadione or oxygen promotes the oxidation of 5-methyltetrahydrofolate Escherichia coli 113-3 5-methyltetrahydrofolate + oxidized acceptor
-
r
5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: reduced acceptor is FADH2 Escherichia coli 113-3 5-methyltetrahydrofolate + oxidized acceptor
-
r
additional information no direct activity with pyridine nucleotides Escherichia coli ?
-
?
additional information no direct activity with pyridine nucleotides Escherichia coli 113-3 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3 6.4 formation of 5-methyltetrahydrofolate Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD enzyme-bound FAD Escherichia coli
FAD flavoprotein, oxidized acceptor in reverse reaction Escherichia coli
FADH2 flavoprotein, reduced acceptor in forward reaction Escherichia coli
additional information no direct activity with pyridine nucleotides: NADH, NADPH Escherichia coli