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Information on EC 1.8.4.16 - thioredoxin:protein disulfide reductase

for references in articles please use BRENDA:EC1.8.4.16
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IUBMB 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.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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a [protein] with reduced L-cysteine residues
+
thioredoxin disulfide
=
a [protein] carrying a disulfide bond
+
thioredoxin
a [protein] with reduced L-cysteine residues
+
=
a [protein] carrying a disulfide bond
+
Synonyms
dipZ, DsbD, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
(1b)
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a [DsbD protein] with reduced L-cysteine residues + thioredoxin disulfide = a [DsbD protein] carrying a disulfide bond + thioredoxin
show the reaction diagram
(1a)
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a [protein] with reduced L-cysteine residues + thioredoxin disulfide = a [protein] carrying a disulfide bond + thioredoxin
show the reaction diagram
overall reaction
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