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Information on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB

for references in articles please use BRENDA:EC1.8.5.9
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IUBMB 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).
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The expected taxonomic range for this enzyme is: Rhodobacter capsulatus
Reaction Schemes
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a [DsbA protein] with reduced L-cysteine residues
+
a quinone
=
a [DsbA protein] carrying a disulfide bond
+
a quinol
a [DsbA protein] with reduced L-cysteine residues
+
=
a [DsbA protein] carrying a disulfide bond
+
Synonyms
DsbB, thiol:disulfide oxidoreductase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [DsbA protein] with reduced L-cysteine residues + a quinone = a [DsbA protein] carrying a disulfide bond + a quinol
show the reaction diagram
overall reaction
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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
show the reaction diagram
(1a)
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-
-
a [DsbB protein] with reduced L-cysteine residues + a quinone = a [DsbB protein] carrying a disulfide bond + a quinol
show the reaction diagram
(1b)
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-
-
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