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Literature summary extracted from

  • Pommier, J.; Mejean, V.; Giordano, G.; Iobbi-Nivol, C.
    TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli (1998), J. Biol. Chem., 273, 16615-16620.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.2.3 periplasm
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.3 Molybdenum
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Escherichia coli
-
 wild-type and mutant lacking a protein, TorD, which is a chaperone specific for the enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.3 using ion exchange chromatography on DE52, chromatography on a Mono Q HR 16/10 column and preparative electrophoresis 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 11
-
 periplasmic fraction of wild-type cells, initial activity Escherichia coli
1.7.2.3 250
-
 purified enzyme Escherichia coli
1.7.2.3 1350
-
 crude extract of mutant strain lacking the TorD protein Escherichia coli
1.7.2.3 1720
-
 crude extract of wild-type strain Escherichia coli
1.7.2.3 1810
-
 crude extract of mutant strain lacking the TorD protein but complemented by pTorD 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 benzyl viologen as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
1.7.2.3 trimethylamine N-oxide + electron donor quinone as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?