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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics and kinetic mechanism of DsbB, overview | Escherichia coli |
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 | - |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene dsbB | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
catalyses the rearrangement of -S-S- bonds in proteins | reaction mechanism | Escherichia coli |
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 | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
disulfide bond-forming enzyme | - |
Escherichia coli |
DsbB | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Escherichia coli |
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 |