ExplorEnz: EC 1.8.5.9

Your query returned 1 entry. Printable version

1.8.5.9

Accepted name:

protein dithiol:quinone oxidoreductase DsbB

Reaction:

a [DsbA protein] with reduced L-cysteine residues + a quinone = a [DsbA protein] carrying a disulfide bond + a quinol (overall reaction)
(1a) a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond = a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
(1b) a [DsbB protein] with reduced L-cysteine residues + a quinone = a [DsbB protein] carrying a disulfide bond + a quinol

Other name(s):

dsbB (gene name)

Systematic name:

protein dithiol:quinone oxidoreductase (disulfide-forming)

Comments:

DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation. The enzyme catalyses the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones. cf. EC 1.8.4.15, protein dithiol oxidoreductase (disulfide-forming).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Guilhot, C., Jander, G., Martin, N.L. and Beckwith, J. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA 92 (1995) 9895–9899. [PMID: 7568240]
2.	Kishigami, S., Kanaya, E., Kikuchi, M. and Ito, K. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270 (1995) 17072–17074. [PMID: 7615498]
3.	Kishigami, S. and Ito, K. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. Genes Cells 1 (1996) 201–208. [PMID: 9140064]
4.	Collet, J.F. and Bardwell, J.C. Oxidative protein folding in bacteria. Mol. Microbiol. 44 (2002) 1–8. [PMID: 11967064]
5.	Dutton, R.J., Boyd, D., Berkmen, M. and Beckwith, J. Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc. Natl. Acad. Sci. USA 105 (2008) 11933–11938. [PMID: 18695247]
6.	Inaba, K. Disulfide bond formation system in Escherichia coli. J. Biochem. 146 (2009) 591–597. [PMID: 19567379]

[EC 1.8.5.9 created 2019]