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Literature summary 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

EC Number General Stability Organism
1.5.1.20 FAD stabilizes Escherichia coli

Inhibitors

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + FADH2 Escherichia coli biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine 5-methyltetrahydrofolate + FAD
-
?
1.5.1.20 5,10-methylenetetrahydrofolate + FADH2 Escherichia coli 113-3 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine 5-methyltetrahydrofolate + FAD
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.20 Escherichia coli
-
-
-
1.5.1.20 Escherichia coli 113-3
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.20 about 100fold purification Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.20 5,10-methylenetetrahydrofolate + FADH2 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine Escherichia coli 5-methyltetrahydrofolate + FAD
-
?
1.5.1.20 5,10-methylenetetrahydrofolate + FADH2 biosynthesis of 5-methyltetrahydrofolate, a donor of methyl groups of methionine Escherichia coli 113-3 5-methyltetrahydrofolate + FAD
-
?
1.5.1.20 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
1.5.1.20 5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: reduced acceptor is FADH2 Escherichia coli 5-methyltetrahydrofolate + oxidized acceptor
-
r
1.5.1.20 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
1.5.1.20 5,10-methylenetetrahydrofolate + reduced acceptor forward reaction: reduced acceptor is FADH2 Escherichia coli 113-3 5-methyltetrahydrofolate + oxidized acceptor
-
r
1.5.1.20 additional information no direct activity with pyridine nucleotides Escherichia coli ?
-
?
1.5.1.20 additional information no direct activity with pyridine nucleotides Escherichia coli 113-3 ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.20 37
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.20 6.3 6.4 formation of 5-methyltetrahydrofolate Escherichia coli

Cofactor

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