Formate dehydrogenase
| Formate dehydrogenase N, transmembrane | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Form-deh_trans | ||||||||
| Pfam | PF09163 | ||||||||
| InterPro | IPR015246 | ||||||||
| SCOP | 1kqf | ||||||||
| SUPERFAMILY | 1kqf | ||||||||
| OPM superfamily | 3 | ||||||||
| OPM protein | 1kqf | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.2.1.2) or to a in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1).
NAD-dependent formate dehydrogenases are important in methylotrophic yeast and bacteria and are vital in the catabolism of C1 compounds such as methanol. The cytochrome-dependent enzymes are more important in anaerobic metabolism in prokaryotes. For example, in E. coli, the formate:ferricytochrome-b1 oxidoreductase is an intrinsic membrane protein with two subunits and is involved in anaerobic nitrate respiration.
NAD-dependent reaction
Formate + NAD+ ⇌ CO2 + NADH + H+
Cytochrome-dependent reaction
Formate + 2 ferricytochrome b1 ⇌ CO2 + 2 ferrocytochrome b1 + 2 H+
One of the enzymes in the oxidoreductase family that sometimes employ tungsten (bacterial formate dehydrogenase H) is known to use a selenium-molybdenum version of molybdopterin.
The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein.
...
Wikipedia