| Description | Formylmethanofuran dehydrogenases ( ), found in methanogenic archaea, are molybdenum or tungsten iron-sulphur proteins containing a pterin dinucleotide cofactor. Formylmethanofuran dehydrogenase catalyses the reversible reduction of CO 2and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO 2[ ]. There are two isoenzymes of formylmethanofuran dehydrogenase: a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The tungsten isoenzyme is constitutively transcribed, whereas transcription of the molybdenum operon is induced by molybdate [].This entry represents subunit E of formylmethanofuran dehydrogenase (FmdE). It has been shown that FmdE is not present in the purified enzyme in Methanosarcina barkeri [ ], so the exact role of this subunit is unclear. | Name | Formylmethanofuran dehydrogenase, subunit E |
| Short Name | FmdE | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
