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EC 1.8.4.16 Details
EC number
1.8.4.16
Accepted name
thioredoxin:protein disulfide reductase
Reaction
a [protein] with reduced L-cysteine residues + thioredoxin disulfide = a [protein] carrying a disulfide bond + thioredoxin (overall reaction);;(1a) a [DsbD protein] with reduced L-cysteine residues + thioredoxin disulfide = a [DsbD protein] carrying a disulfide bond + thioredoxin;;(1b) 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
Other name(s)
dsbD (gene name), dipZ (gene name)
Systematic name
thioredoxin:protein disulfide oxidoreductase (dithiol-forming)
Comment
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.
History
created 2019
EC Tree
3.6.1.4 created 1961, deleted 1965
3.6.1.32 created 1984, deleted 2000
3.6.1.33 created 1984, deleted 2000
3.6.1.34 created 1984, deleted 2000
3.6.1.35 created 1984, deleted 2000
3.6.1.36 created 1984, deleted 2000
3.6.1.37 created 1984, deleted 2000
3.6.1.38 created 1984, deleted 2000
3.6.1.46 created 2000, deleted 2003
3.6.1.47 created 2000, deleted 2003
3.6.1.48 created 2000, deleted 200
3.6.1.49 created 2000, deleted 2003
3.6.1.50 created 2000, deleted 2003
3.6.1.51 created 2000, deleted 2003