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Literature summary for 5.3.4.1 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

Activating Compound Comment Organism Structure
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]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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gene dsbB
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Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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?
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 ?
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?

Synonyms

Synonyms Comment Organism
disulfide bond-forming enzyme
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Escherichia coli
DsbB
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Escherichia coli

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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