Biology:List of bacterial disulfide oxidoreductases
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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
- ↑ 1.0 1.1 "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. 2015. doi:10.1074/jbc.M115.672253. PMID 26170452.
- ↑ Comello, Vic (21 October 2015). "Studies reveal a unified approach to combating several bacterial diseases". http://phys.org/news/2015-10-reveal-approach-combating-bacterial-diseases.html.
- ↑ "Identification of a Protein Required for Disulfide Bond Formation In Vivo". Cell 67 (3): 581-589. 1991. doi:10.1016/0092-8674(91)90532-4. PMID 1934062.
- ↑ "The bdbDC Operon of Bacillus subtilis Encodes Thiol-disulfide Oxidoreductases Required for Competence Development". Journal of Biological Chemistry 277 (9): 6994-7001. 2002. doi:10.1074/jbc.M111380200. PMID 11744713.
- ↑ "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. 2009. doi:10.1074/jbc.M109.005785. PMID 19535335.
- ↑ 6.0 6.1 "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. 2015. doi:10.1111/mmi.13172. PMID 26294390.
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