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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

Reaction

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

Synonyms

CcdA, dipZ, disulfide bond reductase, disulfide isomerase-like protein, DsbD, DsbDalpha, NmDsbD

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                1.8.4.16 thioredoxin:protein disulfide reductase

Systematic Name

Systematic Name on EC 1.8.4.16 - thioredoxin:protein disulfide reductase

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SYSTEMATIC NAME
IUBMB Comments
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.