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EC Number pH Optimum Minimum pH Optimum Maximum Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.1-999 - PDI has a greater relative impact on isomerization reactions and consequently the structure-forming step in oxidative folding at pH 7, as opposed to pH’s 8 and 9 694981
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.12.5 - assay at with substrate AppA, DsbC 662333
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.14.5 - assay at with substrate Agp mutant, DsbC 662333
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.16.5 - assay at 680153
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.16.5 - pH optimum for the reductase activity of recombinant PDI 714929
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.16.5 - R120Q mutant shows 59% of wild-type activity at pH 7.5 652930
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.16.5 - substrate NRCSQGSCWN 652425
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.17 - - 747860
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.17 - assay at 661292, 663327, 679702, 680708, 680746
Display the word mapDisplay the reaction diagram Show all sequences 5.3.4.17 - assay at, oxidoreductase and isomerase activity 661641
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