Information on EC 1.5.7.1 - methylenetetrahydrofolate reductase (ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.7.1
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RECOMMENDED NAME
GeneOntology No.
methylenetetrahydrofolate reductase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
folate transformations I
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reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
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reductive acetyl coenzyme A pathway
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One carbon pool by folate
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:ferredoxin oxidoreductase
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 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-69-7
cf. EC 1.7.99.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + FADH2
5,10-methylenetetrahydrofolate + FAD
show the reaction diagram
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?
5,10-methylenetetrahydrofolate + reduced ferredoxin
5-methyltetrahydrofolate + ferredoxin
show the reaction diagram
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?
5-methyltetrahydrofolate + 2 benzyl viologen
5,10-methylenetetrahydrofolate + 2 reduced benzyl viologen + 2 H+
show the reaction diagram
5-methyltetrahydrofolate + benzyl viologen
5,10-methylenetetrahydrofolate + reduced benzyl viologen
show the reaction diagram
5-methyltetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + FADH2
show the reaction diagram
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11% of the activity with methylene blue
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?
5-methyltetrahydrofolate + menadione
5,10-methylenetetrahydrofolate + reduced menadiol
show the reaction diagram
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25% of the activity with methylene blue
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?
5-methyltetrahydrofolate + rubredoxin
5,10-methylenetetrahydrofolate + reduced rubredoxin
show the reaction diagram
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11% of the activity with methylene blue
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
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the enzyme contains 3.4 nmol FAD per mg of enzyme protein, the purified recombinant MetF contains FMN rather than FAD
additional information
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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the enzyme contains 110 nmol FAD per mg of enzyme protein
Iron
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iron-sulfur protein, contains 15.2 iron and 19.5 acid labile sulfide per 237000 Da enzyme
Zinc
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enzyme contains 2.3 zinc per 237000 Da enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the reduction of benzyl viologen with NADH is competitively inhibited by NADP+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MetV
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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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 1.8
5-methyltetrahydrofolate
0.1 - 11.1
benzyl viologen
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16
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purified enzyme, substrate 5-methyltetrahydrofolate, pH 7.5, 45C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 55
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at 55C the activity is twice as high as at 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
32000
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about, hexaheteromeric complex including MetF
35000
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
237000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
octamer
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 7.6
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the enzyme is more stable in Tris/HCl than in triethanolamine/HCl or phosphate buffer
437714
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
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437714
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
10C, pH 7.4, 50 mM Tris/HCl containing 20% glycerol and 2 mM dithionite in an anaerobic chamber
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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