1.5.7.1: methylenetetrahydrofolate reductase (ferredoxin)

This is an abbreviated version!
For detailed information about methylenetetrahydrofolate reductase (ferredoxin), go to the full flat file.

Reaction

Synonyms

5,10-methylenetetrahydrofolate reductase, Fdred:methylene-THF oxidoreductase, metF, methylene-H4F reductase, methylene-tetrahydrofolate reductase, methylenetetrahydrofolate reductase, MetVF-type methylenetetrahydrofolate reductase, MetVF-type MTHFR, MTHFR

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.7 With an iron-sulfur protein as acceptor

                1.5.7.1 methylenetetrahydrofolate reductase (ferredoxin)

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Results	in table
1	Activating Compound
1	CAS Registry Number
1	Cloned(Commentary)
6	Cofactor
3	General Information
1	Inhibitors
4	KM Value [mM]
3	Localization
5	Metals/Ions
5	Molecular Weight [Da]
4	Organism
1	Oxidation Stability
5	Pathway
3	pH Optimum
2	pH Stability
3	Purification (Commentary)
1	Reaction
4	Reference
2	Source Tissue
3	Specific Activity [micromol/min/mg]
1	Storage Stability
14	Substrates and Products (Substrate)
4	Subunits
14	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]

Cofactor

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Cofactor on EC 1.5.7.1 - methylenetetrahydrofolate reductase (ferredoxin)

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

2 entries

Ferredoxin

Clostridium ljungdahlii

-

the dimer consisting of two of MetVF heterodimers contains 1.87 mol FMN per mol dimeric heterodimer. Reduced ferredoxin cannot be the physiological electron donor in vivo, since growth by acetogenesis from H2 + CO2 has a negative ATP yield

764936

-

FMN

Moorella thermoacetica

-

the enzyme contains 3.4 nmol FAD per mg of enzyme protein, the purified recombinant MetF contains FMN rather than FAD

742782

additional information

2 entries

-

FAD

Clostridium formicaceticum

-

contains 1.7 FAD per 237000 Da enzyme

437714

FAD

Moorella thermoacetica

-

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

742782

additional information

Moorella thermoacetica

-

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

742782

-

additional information

Clostridium ljungdahlii

-

NADH and NADPH are not used as electron donor. MTHFR is able to use artificial electron donors for the reduction of methylene-THF

764936

-