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Literature summary for 1.8.4.2 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)

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
DsbG gene
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from periplasm Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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