The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: protein dithiol oxidoreductase (disulfide-forming)
Reaction: a [DsbA protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [DsbA protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond
Other name(s): dsbA (gene name)
Systematic name: protein dithiol:[DsbA protein] oxidoreductase (protein disulfide-forming)
Comments: DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-negative bacteria that promotes protein disulfide bond formation. DsbA contains a redox active disulfide bond that is catalytically transferred via disulfide exchange to a diverse range of newly translocated protein substrates. The protein is restored to the oxidized state by EC, protein dithiol:quinone oxidoreductase DsbB.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Bardwell, J.C., McGovern, K. and Beckwith, J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581–589. [PMID: 1934062]
2.  Akiyama, Y., Kamitani, S., Kusukawa, N. and Ito, K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J. Biol. Chem. 267 (1992) 22440–22445. [PMID: 1429594]
3.  Zapun, A., Bardwell, J.C. and Creighton, T.E. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32 (1993) 5083–5092. [PMID: 8494885]
4.  Bader, M., Muse, W., Zander, T. and Bardwell, J. Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273 (1998) 10302–10307. [PMID: 9553083]
5.  Guddat, L.W., Bardwell, J.C. and Martin, J.L. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Structure 6 (1998) 757–767. [PMID: 9655827]
6.  Kadokura, H., Tian, H., Zander, T., Bardwell, J.C. and Beckwith, J. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 303 (2004) 534–537. [PMID: 14739460]
[EC created 2019]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald