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Literature summary extracted from

  • Cox, J.C.; Knight, R.
    Trimethylamine N-oxide (TMAO) reductase activity in chlorate-resistant or respiration-deficient mutants of Escherichia coli (1981), FEMS Microbiol. Lett., 12, 249-252.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.3 Molybdenum
-
 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 + electron donor Escherichia coli trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones trimethylamine + oxidized electron donor + H2O
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 trimethylamine N-oxide + electron donor NADH as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
1.7.2.3 trimethylamine-N-oxide + electron donor trimethylamine N-oxide acts as a terminal electron acceptor for an anaerobic respiratory chain which requires, in addition to a primary dehydrogenase, cytochromes and quinones Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.3 NADH
-
 Escherichia coli