In enzymology, a methylenetetrahydrofolate reductase (ferredoxin) (EC 1.5.7.1) is an enzyme that catalyzes the chemical reaction
| Methylenetetrahydrofolate reductase (ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.7.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 5-methyltetrahydrofolate + 2 oxidized ferredoxin 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
Thus, the two substrates of this enzyme are 5-methyltetrahydrofolate and oxidized ferredoxin, whereas its 3 products are 5,10-methylenetetrahydrofolate, reduced ferredoxin, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 5-methyltetrahydrofolate:ferredoxin oxidoreductase. This enzyme is also called 5,10-methylenetetrahydrofolate reductase. This enzyme participates in one carbon pool by folate.
References
edit- Clark JE, Ljungdahl LG (1984). "Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum". J. Biol. Chem. 259 (17): 10845–9. PMID 6381490.
