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Literature summary extracted from

  • Katzen, F.; Beckwith, J.
    Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD (2003), Proc. Natl. Acad. Sci. USA, 100, 10471-10476 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.16 membrane
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 Escherichia coli 16020
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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
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.16 Escherichia coli
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-
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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 electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme Escherichia coli ?
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Synonyms

EC Number Synonyms Comment Organism
1.8.4.16 DsbD
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 Escherichia coli