| EC |
1.5.7.1 |
| Accepted name: |
methylenetetrahydrofolate reductase (ferredoxin) |
| Reaction: |
5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+ |
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For diagram of folate species interconversions, click here |
| Other name(s): |
5,10-methylenetetrahydrofolate reductase |
| Systematic name: |
5-methyltetrahydrofolate:ferredoxin oxidoreductase |
| Comments: |
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+. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Clark, J.E. and Ljungdahl, L.G. Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum. J. Biol. Chem. 259 (1984) 10845–10849. [PMID: 6381490] |
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| [EC 1.5.7.1 created 2005, modified 2021] |
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