EC Number   |
General Information |
Reference |
|---|
  1.8.5.9 | malfunction |
mutation in the DsbA-enzyme system results in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate |
-, 757614 |
| 1.8.5.9 | metabolism |
the enzyme facilitates the formation of disulfide bonds in periplasmic proteins but does not facilitate the formation of intramembraneous disulfides |
756716 |
| 1.8.5.9 | physiological function |
disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB |
-, 758183 |
| 1.8.5.9 | physiological function |
the enzyme is required for virulence in Burkholderia pseudomallei |
-, 756909 |
| 1.8.5.9 | physiological function |
the enzyme oxidizes DsbA for continuous protein disulfide bond formation in the cell |
756589 |
