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Literature summary for 1.8.4.16 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
Search for more literature for 1.8.4.16

Cloned(Commentary)

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
DsbD
-
 Escherichia coli

General Information

General Information Comment Organism
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