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Results 1 - 10 of 17 > >>
EC Number Protein Variants Commentary Reference
Display the reaction diagram Show all sequences 1.8.5.9C104S inactive 756872
Display the reaction diagram Show all sequences 1.8.5.9C130S inactive 756717
Display the reaction diagram Show all sequences 1.8.5.9C41A/C44A the mutant has two cysteine residues at Cys104 and Cys130 compared to the wild type enzyme with Cys41, Cys44, Cys104 and Cys130 757146
Display the reaction diagram Show all sequences 1.8.5.9C41S/C44S/C102S/C130S inactive -, 756909
Display the reaction diagram Show all sequences 1.8.5.9more 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 -, 758183
Display the reaction diagram Show all sequences 1.8.5.9R118H missense mutation -, 756909
Display the reaction diagram Show all sequences 1.8.5.9R48A the mutant shows strongly reduced DsbA protein oxidation activity 758211
Display the reaction diagram Show all sequences 1.8.5.9R48H the mutant shows reduced activity compared to the wild type enzyme 756585
Display the reaction diagram Show all sequences 1.8.5.9R48H the mutant shows reduced affinity for ubiquinone 758288
Display the reaction diagram Show all sequences 1.8.5.9R48H the mutant shows strongly reduced DsbA protein oxidation activity 758211
Results 1 - 10 of 17 > >>