1.8.5.9: protein dithiol:quinone oxidoreductase DsbB
This is an abbreviated version!
For detailed information about protein dithiol:quinone oxidoreductase DsbB, go to the full flat file.
Reaction
Synonyms
C. trachomatis disulfide bond protein B, CtDsbB, disulfide bond formation protein B, disulfide bond oxidoreductase B, disulfide bond protein B, disulfide-bond formation protein B, DsbB, membrane protein disulfide bond protein B, Rv2968c, thiol:disulfide oxidoreductase, VKOR homolog
ECTree
1.8.5.9 protein dithiol:quinone oxidoreductase DsbBAdvanced search results
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Engineering on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C41A/C44A
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the mutant has two cysteine residues at Cys104 and Cys130 compared to the wild type enzyme with Cys41, Cys44, Cys104 and Cys130
R48H
Y46P/E47P
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the mutant shows strongly reduced DsbA protein oxidation activity
additional information
additional information
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construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
-
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
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