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Literature summary for 1.7.2.3 extracted from

  • Genest, O.; Ilbert, M.; Mejean, V.; Iobbi-Nivol, C.
    TorD, an essential chaperone for TorA molybdoenzyme maturation at high temperature (2005), J. Biol. Chem., 280, 15644-15648.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
TorD at 42°C and in the absence of TorD TorA is poorly matured and almost completely degraded Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli TorD is an essentially required chaperone for cofactor binding and enzyme maturation of the trimethylamine oxide reductase TorA, EC 1.6.6.9, in absence of TorD at 42°C, the TorA is poorly maturated and almost completely degraded, at elevated temperatures above 37°C TorD prevents the missfolding of TorA apoenzyme before molybdenum cofactor binding, temperature-dependent effect ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
wild-type strain LCB514, enzyme-deficient mutant strain LCB515
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Chelating HP column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information TorD is an essentially required chaperone for cofactor binding and enzyme maturation of the trimethylamine oxide reductase TorA, EC 1.6.6.9, in absence of TorD at 42°C, the TorA is poorly maturated and almost completely degraded, at elevated temperatures above 37°C TorD prevents the missfolding of TorA apoenzyme before molybdenum cofactor binding, temperature-dependent effect Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
TorA
-
Escherichia coli
TorD
-
Escherichia coli
trimethylamine oxide reductase
-
Escherichia coli