The Enzyme Database

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EC 1.8.4.16     
Accepted name: thioredoxin:protein disulfide reductase
Reaction: a [protein] with reduced L-cysteine residues + thioredoxin disulfide = a [protein] carrying a disulfide bond + thioredoxin (overall reaction)
(1a) a [DsbD protein] with reduced L-cysteine residues + thioredoxin disulfide = a [DsbD protein] carrying a disulfide bond + thioredoxin
(1b) a [DsbD protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [DsbD protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond
Other name(s): dsbD (gene name); dipZ (gene name)
Systematic name: thioredoxin:protein disulfide oxidoreductase (dithiol-forming)
Comments: DsbD is an inner membrane protein found in Gram-negative bacteria that transfers electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG, reducing disulfide bonds in the target proteins to dithiols. DsbD consists of three domains: a periplasmic N-terminal domain, a central transmembrane domain and a periplasmic C-terminal domain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Missiakas, D., Schwager, F. and Raina, S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14 (1995) 3415–3424. [PMID: 7628442]
2.  Gordon, E.H., Page, M.D., Willis, A.C. and Ferguson, S.J. Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. Mol. Microbiol. 35 (2000) 1360–1374. [PMID: 10760137]
3.  Katzen, F. and Beckwith, J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103 (2000) 769–779. [PMID: 11114333]
4.  Goulding, C.W., Sawaya, M.R., Parseghian, A., Lim, V., Eisenberg, D. and Missiakas, D. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Biochemistry 41 (2002) 6920–6927. [PMID: 12033924]
5.  Katzen, F. and Beckwith, J. Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Proc. Natl. Acad. Sci. USA 100 (2003) 10471–10476. [PMID: 12925743]
6.  Rozhkova, A. and Glockshuber, R. Thermodynamic aspects of DsbD-mediated electron transport. J. Mol. Biol. 380 (2008) 783–788. [PMID: 18571669]
[EC 1.8.4.16 created 2019]
 
 


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