Literature summary for 1.7.2.3 extracted from

Gon, S.; Giudici-Orticoni, M.T.; Mejean, V.; Iobbi-Nivol, C.
Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli (2001), J. Biol. Chem., 276, 11545-11551.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	Escherichia coli	reaction mechanism	trimethylamine + (ferricytochrome c)-subunit + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	reaction mechanism	Escherichia coli	trimethylamine + (ferricytochrome c)-subunit + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome c	c-type cytochrome Tor C is required for electron transfer to terminal enzyme Tor A	Escherichia coli

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Release 2023.1 (January 2023)