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Literature summary for 1.8.5.9 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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DsbB
-
Escherichia coli