1.8.4.16: thioredoxin:protein disulfide reductase
This is an abbreviated version!
For detailed information about thioredoxin:protein disulfide reductase, go to the full flat file.
Word Map on EC 1.8.4.16
-
1.8.4.16
-
chaperone
-
methanothermobacter
-
pdi-like
-
extremophiles
-
thermoautotrophicum
-
gssg
-
testis-specific
-
pdilt
-
mercuric
-
agrobacterium-mediated
-
nipponbare
-
non-protein
-
phytochelatins
-
non-classical
- 1.8.4.16
- chaperone
- methanothermobacter
-
pdi-like
-
extremophiles
- thermoautotrophicum
- gssg
-
testis-specific
- pdilt
-
mercuric
-
agrobacterium-mediated
-
nipponbare
-
non-protein
- phytochelatins
-
non-classical
Reaction
Synonyms
CcdA, dipZ, disulfide bond reductase, disulfide isomerase-like protein, DsbD, DsbDalpha, NmDsbD
ECTree
1.8.4.16 thioredoxin:protein disulfide reductaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.8.4.16 - thioredoxin:protein disulfide reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin-1
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
CQQGFDGTQNSCK peptide containing amide-coupled tetraazacyclododecane-1,4,7,10-tetraacetic acid + GSSG
?
-
-
-
-
?
insulin + dithiothreitol
reduced insulin + oxidized dithiothreitol
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[DsbE protein] carrying a disulfide bond + thioredoxin
[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[HelX protein] carrying a disulfide bond + thioredoxin
[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[protein DsbC] carrying a disulfide bond + thioredoxin
[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbE] carrying a disulfide bond + thioredoxin
[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbG] carrying a disulfide bond + thioredoxin
[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
-
-
?
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
?
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
additional information
?
-
-
electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme
-
-
-
additional information
?
-
the enzyme does not catalyze the reduction of the disulfide of the thioredoxin-like oxidant DsbA
-
-
-
additional information
?
-
-
the enzyme includes three domains, each containing a pair of cysteine residues that perform a series of disulfide exchange reactions. In the first step, the transmembrane domain accepts electrons from thioredoxin in the cytoplasm; these are then transferred to the periplasmic C-terminal domain and finally to the N-terminal domain, which is also located in the periplasm
-
-
-
additional information
?
-
-
the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma
-
-
-
additional information
?
-
the enzyme transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment
-
-
-
additional information
?
-
-
the enzyme transports electrons without using a metabolite or a cofactor
-
-
-
additional information
?
-
-
the periplasmic protein TrbB relies on the enzyme from Escherichia coli for maintenance of its C-X-X-C redox active site motif which is responsible for its enzymatic activity
-
-
-
