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Literature summary for 1.7.2.3 extracted from

  • Hatzixanthis, K.; Richardson, D.J.; Sargent, F.
    Chaperones involved in assembly and export of N-oxide reductases (2005), Biochem. Soc. Trans., 33, 124-126.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli
overexpression Shewanella massilia
overexpression as His-tagged protein Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-
soluble
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe-S cluster
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme binds to the trimethylamine oxide reductase TorA apoenzyme, EC 1.6.6.9, recognizing a signal peptide, and allows TorA to bind the essential molybdenum cofactor for transport from the periplasm across the cytoplasmic membrane, TorD is not involved in the transport itself, TorD has a regulatory and controlling function on TorA assembly ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Shewanella massilia
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Q FF column chromatography Escherichia coli
recombinant His-tagged enzyme by nickel affinity and anion exchange chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme binds to the trimethylamine oxide reductase TorA apoenzyme, EC 1.6.6.9, recognizing a signal peptide, and allows TorA to bind the essential molybdenum cofactor for transport from the periplasm across the cytoplasmic membrane, TorD is not involved in the transport itself, TorD has a regulatory and controlling function on TorA assembly Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
monomer
-
Escherichia coli
More overexpressed enzyme forms monomers and dimers, a subunit contains 2 distinct domains separated by a short hinge region, dimerization by domain-swapping Shewanella massilia
trimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
More enzyme belongs to the TorD-family chaperones Escherichia coli
More enzyme belongs to the TorD-family chaperones Shewanella massilia
TMAO reductase
-
Escherichia coli
TorD
-
Escherichia coli
TorD
-
Shewanella massilia

Cofactor

Cofactor Comment Organism Structure
molybdopterin guanine dinucleotide
-
Escherichia coli