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<< < Results 11 - 17 of 17
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48E78H/D164N site-directed mutagenesis, replacement of the catalytic residues of kumamolisin-As with those of subtilisin, disruption of the catalytic triad, the mutant shows 0.0001% of the wild-type turnover -, 664913
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48E78Q/D164N site-directed mutagenesis, completely inactive mutant which stays unprocessed -, 664913
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48more mutational analysis of the Ser278 residue reveals that the mutant loses both auto-processing activity and proteolytic activity -, 651795
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48S278A an inactive pro-kumamolisin mutant, the catalytic domain of the mutant exhibits a virtually identical structure compared to the active enzyme -, 731647
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48S278A site-directed mutagenesis, no autoactivation of the proform, inactive mutant -, 665094
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48S278A the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitzo)Phe-Arg-Leu is reduced to 0.5% of the native enzyme -, 653914
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.B48W129A the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 3.8% of the native enzyme -, 653914
<< < Results 11 - 17 of 17