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Literature summary extracted from

  • Tapley, T.L.; Eichner, T.; Gleiter, S.; Ballou, D.P.; Bardwell, J.C.
    Kinetic characterization of the disulfide bond-forming enzyme DsbB (2007), J. Biol. Chem., 282, 10263-10271.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.3.4.1 DsbA disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbA must be reoxidized by an electron acceptor, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.4.1 additional information
-
 additional information kinetics and kinetic mechanism of DsbB, overview Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 membrane integral, the catalytic reaction takes place on the periplasmic side, PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 additional information Escherichia coli DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Escherichia coli
-
 gene dsbB
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.4.1 catalyses the rearrangement of -S-S- bonds in proteins reaction mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 additional information DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview Escherichia coli ?
-
 ?
5.3.4.1 additional information kinetic cycle of DsbB, thew enzyme uses a tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2, overview Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 disulfide bond-forming enzyme
-
 Escherichia coli
5.3.4.1 DsbB
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.4.1 7
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
5.3.4.1 ubiquinone tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview Escherichia coli