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Results 1 - 10 of 49 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C118A complete loss of activity 735550
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C141A site-directed mutagenesis, inactive mutant 733190
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C145A mutant enzyme shows 9.7% of wild-type eactivity 686659
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C145S mutant enzyme shows 6.2% of wild-type eactivity 686659
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C166A mutant catalytically inactive 209131
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C166S mutant catalytically inactive 209131
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4C249A inhibition of the mutant by ibuprofen is similar than that of wild type 655133
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4D133A inactive mutant enzyme 686659
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4D133E mutant enzyme shows 0.16% of wild-type eactivity 686659
Show all pathways known for 3.5.1.4Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.4D487N site-specific mutagenesis, the D487N mutation is located in the center of the protein, far distant from the 33-48 segment. The mutant amidase, like the wild-type enzyme, responds to changes in pH and temperature with a conformational change affecting the dimer-octamer equilibrium 711039
Results 1 - 10 of 49 > >>