List of bacterial disulfide oxidoreductases

Bacterial thiol disulfide oxidoreductases (TDOR) are bacterial enzymes that participate in redox reactions involving cysteine residues. Along with unfolded proteins, they are secreted from bacterial cells into periplasmic spaces or extracellularly, and may have membrane anchors.[1] Some have functions in promoting processes of adhesion and biofilm development, and generally disease development.[2]

Table

Enzyme name Meaning Bacteria Catalytic site
DsbA D disulfide bond A various incl. Staphylococcus aureus CXXC[1]
DsbA D disulfide bond A Escherichia coli CPHC[3]
BdbA–D Bacillus subtilis[4][5]
MdbA Actinomyces oris, Corynebacterium diphtheriae CPHC[6]
SdbA Streptococcus gordonii[6]

References

  1. ^ a b Reardon-Robinson ME, Osipiuk J, Chang C, Wu C, Jooya N, Joachimiak A, Das A, Ton-That H (2015). "A Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces oris". Journal of Biological Chemistry. 290 (35): 21393–21405. doi:10.1074/jbc.M115.672253. PMC 4571867. PMID 26170452.
  2. ^ Comello, Vic (21 October 2015). "Studies reveal a unified approach to combating several bacterial diseases". phys.org. Retrieved 27 February 2026.
  3. ^ Bardwell JC, McGovern K, Beckwith J (1991). "Identification of a Protein Required for Disulfide Bond Formation In Vivo". Cell. 67 (3): 581–589. doi:10.1016/0092-8674(91)90532-4. PMID 1934062.
  4. ^ Meima R, Eschevins C, Fillinger S, Bolhuis A, Hamoen LW, Dorenbos R, Quax WJ, van Dijl JM, Provvedi R, Chen I, Dubnau D, Bron S (2002). "The bdbDC Operon of Bacillus subtilis Encodes Thiol-disulfide Oxidoreductases Required for Competence Development". Journal of Biological Chemistry. 277 (9): 6994–7001. doi:10.1074/jbc.M111380200. PMID 11744713.
  5. ^ Crow A, Lewin A, Hecht O, Möller MC, Moore GR, Hederstedt L, Le Brun NE (2009). "Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE". Journal of Biological Chemistry. 284 (35): 23719–23733. doi:10.1074/jbc.M109.005785. PMC 2749146. PMID 19535335.
  6. ^ a b Reardon-Robinson ME, Osipiuk J, Jooya N, Chang C, Joachimiak A, Das A, Ton-That H (2015). "A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence". Molecular Microbiology. 98 (6): 1037–1050. doi:10.1111/mmi.13172. PMC 4981772. PMID 26294390.
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