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1.8.4.15: protein dithiol oxidoreductase (disulfide-forming)

This is an abbreviated version!
For detailed information about protein dithiol oxidoreductase (disulfide-forming), go to the full flat file.

Reaction

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a [DsbA protein] carrying a disulfide bond
+
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a [protein] with reduced L-cysteine residues
=
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a [DsbA protein] with reduced L-cysteine residues
+
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a [protein] carrying a disulfide bond

Synonyms

C. trachomatis disulfide bond protein A, CtDsbA, disulfide oxidoreductase, DsbA, More, MSH-dependent thiol-disulfide reductase, mycothiol-dependent thiol-disulfide reductase, ncgl2478, protein dithiol oxidoreductase, SdbA, Streptococcus disulfide bond protein A, TDOR, thiol-disulfide oxidoreductase

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                EC 1.8.4.151.8.4.15 protein dithiol oxidoreductase (disulfide-forming)

Systematic Name

Systematic Name on EC 1.8.4.15 - protein dithiol oxidoreductase (disulfide-forming)

for references in articles please use BRENDA:EC1.8.4.15

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SYSTEMATIC NAME
IUBMB Comments
protein dithiol:[DsbA protein] oxidoreductase (protein disulfide-forming)
DsbA is a periplasmic thiol:disulfide oxidoreductase found in Gram-negative bacteria that promotes protein disulfide bond formation. DsbA contains a redox active disulfide bond that is catalytically transferred via disulfide exchange to a diverse range of newly translocated protein substrates. The protein is restored to the oxidized state by EC 1.8.5.9, protein dithiol:quinone oxidoreductase DsbB.