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Literature summary extracted from

  • Van Straaten, M.; Missiakas, D.; Raina, S.; Darby, N.J.
    The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli (1998), FEBS Lett., 428, 255-258.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.2 expression from plasmid in Escherichia coli into the periplasm Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.2 periplasm DsbG protein Escherichia coli
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.4.2 25700
-
? * 25700, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.2 Escherichia coli
-
DsbG gene
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.2 recombinant enzyme from periplasm Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.2 dithiothreitol + protein disulfide
-
Escherichia coli ?
-
r
1.8.4.2 GSH + protein disulfide protein disulfide: enzyme itself Escherichia coli GSSG + protein-dithiol
-
r
1.8.4.2 additional information redox reaction between different Dsn proteins Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
1.8.4.2 ? ? * 25700, SDS-PAGE Escherichia coli