ExplorEnz: EC 1.8.4.16

Your query returned 1 entry. Printable version

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 [thioredoxin:protein disulfide reductase] with reduced L-cysteine residues + thioredoxin disulfide = a [thioredoxin:protein disulfide reductase] carrying a disulfide bond + thioredoxin
(1b) a [thioredoxin:protein disulfide reductase] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [thioredoxin:protein disulfide reductase] 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:

The DsbD protein is found in Gram-negative bacteria and transfers electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG, reducing disulfide bonds in the target proteins to dithiols. NrdH redoxins, which are found in Gram-positive bacteria, catalyse a similar reaction.

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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12925743]
6.	Rozhkova, A. and Glockshuber, R. Thermodynamic aspects of DsbD-mediated electron transport. J. Mol. Biol. 380 (2008) 783–788. [DOI] [PMID: 18571669]
7.	Si, M.R., Zhang, L., Yang, Z.F., Xu, Y.X., Liu, Y.B., Jiang, C.Y., Wang, Y., Shen, X.H. and Liu, S.J. NrdH Redoxin enhances resistance to multiple oxidative stresses by acting as a peroxidase cofactor in Corynebacterium glutamicum. Appl. Environ. Microbiol. 80 (2014) 1750–1762. [DOI] [PMID: 24375145]

[EC 1.8.4.16 created 2019, modified 2023]