An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); or EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with either NADH or NADP+.
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The enzyme appears in viruses and cellular organisms
An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.53, methylenetetrahydrofolate reductase (NADPH); EC 1.5.1.54, methylenetetrahydrofolate reductase (NADH); or EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with either NADH or NADP+.
the enzyme catalyzes reduction of methylenetetrahydrofolate with reduced benzyl viologen but not with NAD(P)H in either the absence or presence of oxidized ferredoxin. The enzyme also catalyzes the reversible reduction of benzyl viologen with NADH (diaphorase activity) at 48 U/mg
the enzyme catalyzes reduction of methylenetetrahydrofolate with reduced benzyl viologen but not with NAD(P)H in either the absence or presence of oxidized ferredoxin. The enzyme also catalyzes the reversible reduction of benzyl viologen with NADH (diaphorase activity) at 48 U/mg
The enzyme complex does not catalyze the reduction of methylene-H4F with NADH or NADPH. The enzyme complex subunit HdrA contains iron-sulfur clusters and 2 FADs and catalyzes the reduction of benzyl viologen with NADH. But the physiological electron donor for methylenetetrahydrofolate reduction in Moorella thermoacetica is NADH, and the exergonic reduction of methylenetetrahydrofolate with NADH is coupled via flavin-based electron bifurcation with the endergonic reduction of an yet unknown electron acceptor
the enzyme contains 3.1 nmol FAD per mg of enzyme protein. In the absence of FAD, the enzyme is still active, the purified recombinant MetF contains FMN rather than FAD
the enzyme complex subunit MetV, an iron-sulfur zinc protein, is required by MetF for full activity, and activates the enzyme 70fold with benzyl viologen
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme loses 50% of the activity within 2 h in aerobic buffer (0.1 M Tris/HCl buffer, pH 7.4) with or without a reducing agent and in anaerobic buffer without a reducing agent
native enzyme aerobically 40fold by ultracentrifugation, anion exchange chromatography, gel filtration, ultrafiltration, hydroxyapatite chromatography, followed by again ultrafiltration and gel filtration, enzyme MetF copurifies with the other five proteins encoded in the unit in a hexaheteromeric complex with an apparent molecular mass in the 320-kDa range. Recombinant Strep-tagged enzyme MetF anaerobically from Escherichia coli strain C41(DE3) by avidine affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene metF, which is part of a transcription unit also containing the genes hdrCBA, mvhD, and metV, genetic structure, recombinant expression of Strep-tagged enzyme MetF in Escherichia coli strain C41(DE3) harboring pCodonPlus and pRKISC, the recombinant MetF contains FMN rather than FAD
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1.5.7.1 methylenetetrahydrofolate reductase (ferredoxin)
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