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Literature summary extracted from

  • Hemmis, C.; Berkmen, M.; Eser, M.; Schildbach, J.
    TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance (2011), J. Bacteriol., 193, 4588-4597 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.16 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.16 cytoplasmic membrane
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.16 a [protein] carrying a disulfide bond + thioredoxin Escherichia coli overall reaction a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.16 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.16 a [protein] carrying a disulfide bond + thioredoxin overall reaction Escherichia coli a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
 ?
1.8.4.16 additional information the periplasmic protein TrbB relies on the enzyme from Escherichia coli for maintenance of its C-X-X-C redox active site motif which is responsible for its enzymatic activity Escherichia coli ?
-
-

Synonyms

EC Number Synonyms Comment Organism
1.8.4.16 DsbD
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
1.8.4.16 metabolism the enzyme accepts electrons from cytoplasmic thioredoxin and shuttles these electrons via a well-defined cascade through the membrane-spanning region and into the periplasm Escherichia coli