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Literature summary extracted from

  • Sevier, C.; Kadokura, H.; Tam, V.; Beckwith, J.; Fass, D.; Kaiser, C.
    The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases (2005), Protein Sci., 14, 1630-1642 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.8.5.9 R48H the mutant shows reduced affinity for ubiquinone Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.5.9 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.5.9 [DsbA protein] with reduced L-cysteine residues + ubiquinone Escherichia coli overall reaction [DsbA protein] carrying a disulfide bond + ubiquinol
-
 ?

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 [DsbA protein] with reduced L-cysteine residues + ubiquinone overall reaction Escherichia coli [DsbA protein] carrying a disulfide bond + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.5.9 DsbB
-
 Escherichia coli