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Literature summary for 1.7.2.3 extracted from

  • Bragg, P.D.; Hackett, N.R.
    Cytochromes of the trimethylamine N-oxide anaerobic respiratory pathway of Escherichia coli (1983), Biochim. Biophys. Acta, 725, 168-177.
    View publication on PubMed
Search for more literature for 1.7.2.3

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
trimethylamine-N-oxide + electron donor Escherichia coli cytochrome 554,557 may be the physiological electron donor trimethylamine + oxidized electron donor + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine N-oxide + electron donor formate as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
trimethylamine N-oxide + electron donor NADH as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
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
-
 ?
trimethylamine-N-oxide + electron donor cytochrome 554,557 may be the physiological electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Escherichia coli