Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Simon, J.; van Spanning, R.J.; Richardson, D.J.
    The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems (2008), Biochim. Biophys. Acta, 1777, 1480-1490.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.5.3 membrane in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.5.3 formate + a quinone Escherichia coli in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane. The formate dehydrogenase (Fdh-N or FdnGHI complex) and nitrate reductase A (NarA or NarGHI complex) together form the paradigmatic Fdh-Nar full redox loop CO2 + a quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.5.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.5.3 formate + a quinone in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane. The formate dehydrogenase (Fdh-N or FdnGHI complex) and nitrate reductase A (NarA or NarGHI complex) together form the paradigmatic Fdh-Nar full redox loop Escherichia coli CO2 + a quinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.5.3 Fdh-N
-
 Escherichia coli
1.17.5.3 fdnGHI
-
 Escherichia coli