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Literature summary extracted from

  • Cho, S.; Porat, A.; Ye, J.; Beckwith, J.
    Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility (2007), EMBO J., 26, 3509-3520 .
    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-1 Escherichia coli overall reaction a [protein] with reduced L-cysteine residues + thioredoxin-1 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-1 overall reaction Escherichia coli a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
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 ?
1.8.4.16 additional information the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma Escherichia coli ?
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Synonyms

EC Number Synonyms Comment Organism
1.8.4.16 DsbD
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 Escherichia coli