EC 1.17.5.3 - Formate dehydrogenase-N

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IntEnz Enzyme Nomenclature
EC 1.17.5.3

Names

Accepted name:
formate dehydrogenase-N
Other names:
Fdh-N
FdnGHI
nitrate-inducible formate dehydrogenase
formate dehydrogenase N
FDH-N
nitrate inducible Fdn
nitrate inducible formate dehydrogenase
Systematic name:
formate:quinone oxidoreductase

Reactions

Cofactors

Comments:

The enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups. Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00392
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Enoch, H. G., Lester, R. L.
    The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli.
    J. Biol. Chem. 250 : 6693-6705 (1975). [PMID: 1099093]
  2. Jormakka, M., Tornroth, S., Byrne, B., Iwata, S.
    Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
    Science 295 : 1863-1868 (2002). [PMID: 11884747]
  3. Jormakka, M., Tornroth, S., Abramson, J., Byrne, B., Iwata, S.
    Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.
    Acta Crystallogr. D Biol. Crystallogr. 58 : 160-162 (2002). [PMID: 11752799]

[EC 1.17.5.3 created 2010 as EC 1.1.5.6, transferred 2017 to EC 1.17.5.3]