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Results 1 - 10 of 11 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7D114A mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7D114A mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7D165A very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7E191A very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7E209A inactive mutant enzyme 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7H81R mutation restores the conventional cysteine-switch in the prodomain but fails to induce the cysteine-swich activation 652254
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7K189E calcium-independent high invasiveness is observed in the K189E mutant MDA-MB-231 cell line 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7K189E mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7K189E mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively 684968
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.B7more exchanging residues 88-123 of secretory MMP-7 with the same region in MMP-26 causes localization of this MMP-7 construct to the ER 755387
Results 1 - 10 of 11 > >>