Literature summary for 1.7.2.3 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.

Search for more literature for 1.7.2.3

Localization

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Molybdenum	-	Escherichia coli

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
11	-	periplasmic fraction of wild-type cells, initial activity	Escherichia coli
250	-	purified enzyme	Escherichia coli
1350	-	crude extract of mutant strain lacking the TorD protein	Escherichia coli
1720	-	crude extract of wild-type strain	Escherichia coli
1810	-	crude extract of mutant strain lacking the TorD protein but complemented by pTorD	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trimethylamine N-oxide + electron donor	benzyl viologen as electron donor	Escherichia coli	trimethylamine + oxidized electron donor + H2O	-	?
trimethylamine N-oxide + electron donor	quinone as electron donor	Escherichia coli	trimethylamine + oxidized electron donor + H2O	-	?

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Release 2023.1 (January 2023)