dsbB Antibody

1. Data find that overexpressing PspE, a periplasmic rhodanese, partially restores substantial disulphide bond formation to a dsbA strain. This activity depends on DsbC, the bacterial disulphide bond isomerase, but not on DsbB. PMID: 22809289
2. We found classes of mutants that specifically affect the apparent K(m) of DsbB for either DsbA or quinones, suggesting that quinone and DsbA may interact with different regions of the DsbB protein. PMID: 15687215
3. characterization of quinone-free forms of DsbB prepared from mutant cells unable to synthesize ubiquinone and menaquinone PMID: 16027117
4. the linker alpha-helix of the bacterial disulfide isomerase DsbC is important for the avoidance of misoxidation by DsbB PMID: 16280324
5. Arg-48 of DsbB in the alpha-helical arrangement is essential for the quinone transition PMID: 16384917
6. These observations suggest that the cytosolic loop is important to coordinate the active-site residues of DsbB and ubiquinone to allow their proper reaction cycles. PMID: 16771666
7. DsbB is converted by its specific substrate, DsbA, to a superoxidizing enzyme, capable of oxidizing this extremely oxidizing oxidase. PMID: 17110337
8. study reports sequential 13C and 15N chemical shift assignments for the majority of the residues in the transmembrane helices PMID: 18227427

Show More

Hide All

KEGG: ecj:JW5182

STRING: 316385.ECDH10B_1238