EC Number   |
Cofactor |
Reference |
|---|
   1.5.7.1 | FAD |
contains 1.7 FAD per 237000 Da enzyme |
437714 |
| 1.5.7.1 | FAD |
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 |
| 1.5.7.1 | Ferredoxin |
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 |
| 1.5.7.1 | FMN |
the enzyme contains 3.4 nmol FAD per mg of enzyme protein, the purified recombinant MetF contains FMN rather than FAD |
742782 |
| 1.5.7.1 | more |
NADH and NADPH are not used as electron donor. MTHFR is able to use artificial electron donors for the reduction of methylene-THF |
764936 |
| 1.5.7.1 | more |
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 |
