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
Advanced search results
Systematic Name
Systematic Name 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.
thioredoxin:protein disulfide oxidoreductase (dithiol-forming)
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.