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Results 1 - 10 of 18 > >>
EC Number Application Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9synthesis a huge number of therapeutic proteins such as antibodies, coagulation factors, growth hormones or vaccines are produced as fusion proteins. To obtain the therapeutic protein in its monomeric, active form, the fusion partner has to be removed either by chemical or enzymatic cleavage. Enterokinase is a very attractive tool for the in vitro cleavage of fusion proteins 707812
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9analysis cellular libraries of peptide substrates, CLiPS, are used to study substrate specificities, fluorescent reporter substrates on the surface of Escherichia coli as N-terminal conjugates are used as whole-cell protease activity assays 684000
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9biotechnology EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation 683266
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9analysis enteropeptidase activity is influenced by accessibility of the target site and by downstream sequences 683192
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9biotechnology enteropeptidase is a serine protease used in different biotechnological applications. For many applications the smaller light chain can be used to avoid the expression of the rather large holoenzyme 718352
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9synthesis gene engineering studies on processing fusion proteins 667758
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9medicine human TRAIL is a candidate for clinical application in cancer therapy, activity is lost in some forms of recombinant TRAIL, refolding of thioredoxin/TRAIL and cleavage by enteropeptidase yield a biological active anticancer agent 683279
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9biotechnology purification of 6.8 mg bioactive enzyme from 1l fermentation broth 683994
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9biotechnology study presents a simple and cost-effective procedure for a large-scale production 684030
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.9synthesis the cleavage immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence allows regeneration of native amino-terminal residues of recombinant proteins, e.g. removal of the thioredoxin and polyhistidine fusion partners from proteins of intrest 95583
Results 1 - 10 of 18 > >>