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Literature summary extracted from

  • Guilhot, C.; Jander, G.; Martin, N.; Beckwith, J.
    Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA (1995), Proc. Natl. Acad. Sci. USA, 92, 9895-9899 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.5.9 inner membrane
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.5.9 additional information Escherichia coli reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein ?
-
-
1.8.5.9 [DsbA protein] with reduced L-cysteine residues + a quinone Escherichia coli overall reaction [DsbA protein] carrying a disulfide bond + a quinol
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.5.9 additional information reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein Escherichia coli ?
-
-
1.8.5.9 [DsbA protein] with reduced L-cysteine residues + a quinone overall reaction Escherichia coli [DsbA protein] carrying a disulfide bond + a quinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.5.9 DsbB
-
 Escherichia coli