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Results 1 - 10 of 11 > >>
EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - - 29798, 662017
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - comparative proteome analysis of chloramphenicol-resistant Escherichia coli, two-dimensional electrophoresis, MALDI-TOF mass spectroscopy and Western blotting performed, differential protein expression profiles with and without chloramphenicol treatment shown, antimicrobial susceptibility tested, OmpT protease identified as critically altered protein in chloramphenicol-resistant Escherichia coli, mutant analysis performed 683820
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - effects of OmpT protease on colony-forming ability and production of fibrous protein polymers determined, involvement of OmpT protease in protein quality control within the cell discussed 683272
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - enzyme-LPS activity in endotoxin units 661616
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined 683608
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined 683608
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - strains expressing OmpT protease shown to cleave colicin E1 at the residues K84 and K95 in the N-terminal translocation domain, leading to the removal of the TolQA box essential for cytotoxicity of colicin E1, in vivo data indicating effects of OmpT protease on colicin E1 cell-killing activity shown 683605
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - structural and functional relationships for wild-type and mutated OmpT proteins investigated, relevant case of the Michaelis complex of the outer-membrane protease T (OmpT) analyzed by a hybrid molecular mechanics/coarse-grained (MM/CG) approach, structural explanation for decreased catalytic activity of the mutants S99A and H212A given 683262
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.49-999 - studies on development of a new substrate phage system, construction of a random hexapeptide library described, selection of the phage display library with OmpT protease to demonstrate application of the infectivity-modulated phage display IMOP 683352
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.4958.7 - - 29795
Results 1 - 10 of 11 > >>