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
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
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Engineering
Engineering on EC 1.8.4.15 - protein dithiol oxidoreductase (disulfide-forming)
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C24S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
C21S
additional information
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-