| Description | Formylmethanofuran dehydrogenase ( ) is found in methanogenic and sulphate-reducing archaea. The enzyme contains molybdenum or tungsten, a molybdopterin guanine dinuceotide cofactor (MGD) and iron-sulphur clusters [ ]. It catalyses the reversible reduction of CO2and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO 2[ , ]. This reaction is important for the reduction of CO2to methane, in autotrophic CO 2fixation, and in CO 2formation from reduced C 1units [ ]. The synthesis of formylmethanofuran is crucial for the energy metabolism of archaea. Methanogenic archaea derives the energy for autrophic growth from the reduction of CO2with molecular hydrogen as the electron donor [ ]. The process of methanogenesis consists of a series of reduction reactions at which the one-carbon unit derived from CO2is bound to C 1carriers. 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 [ ]. The archaean Methanobacterium thermoautotrophicum contains a 4-subunit (FwdA, FwdB, FwdC, FwdD) tungsten formylmethanofuran dehydrogenase and a 3-subunit (FmdA, FmdB, FmdC) molybdenum formylmethanofuran dehydrogenase [ ].This entry represents a fusion of subunits C (FmdC) and D (FmdD) of molybdenum-containing formylmethanofuran dehydrogenase. These enzymes consist of five subunits: FmdA ( ), FmdB ( ), FmdC, FmdD and FmdE ( ). | Name | Formylmethanofuran dehydrogenase, fused subunit C/D |
| Short Name | Formylmethanofuran_DH_csu/dsu | Type | Family |
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