Literature summary extracted from

Yamamoto, I.; Hinakura, M.; Seki, S.; Seki, Y.; Kondo, H.
Anaerobic induction of trimethylamine N-oxide reductase and cytochromes by dimethyl sulfoxide in Escherichia coli (1990), Curr. Microbiol., 20, 245-249.

No PubMed abstract available

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.7.2.3	fusion protein with beta-galactosidase	Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.7.2.3	trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	Escherichia coli	reduction of trimethylamine N-oxide is catalyzed by at least 2 enzymes: trimethylamine N-oxide reductase and dimethyl sulfoxide reductase	trimethylamine + (ferricytochrome c)-subunit + H2O	-	?

Organism

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

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.7.2.3	additional information	-	specific activity in extracts after growth on various oxide compounds	Escherichia coli

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.7.2.3	trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+	reduction of trimethylamine N-oxide is catalyzed by at least 2 enzymes: trimethylamine N-oxide reductase and dimethyl sulfoxide reductase	Escherichia coli	trimethylamine + (ferricytochrome c)-subunit + H2O	-	?

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Release 2023.1 (January 2023)