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 cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1).

Function

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⁺

Molybdopterin, molybdenum and selenium dependence

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.

Transmembrane domain

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.

See also

• Formate dehydrogenase (cytochrome)
• Formate dehydrogenase (cytochrome-c-553)
• Formate dehydrogenase (NADP+)
• Microbial metabolism

External links

• ENZYME link for EC 1.2.2.1
• ENZYME link for EC 1.2.1.2