EC Number |
Application |
Reference |
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3.4.21.9 | synthesis |
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 |
3.4.21.9 | analysis |
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 |
3.4.21.9 | biotechnology |
EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation |
683266 |
3.4.21.9 | analysis |
enteropeptidase activity is influenced by accessibility of the target site and by downstream sequences |
683192 |
3.4.21.9 | biotechnology |
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 |
3.4.21.9 | synthesis |
gene engineering studies on processing fusion proteins |
667758 |
3.4.21.9 | medicine |
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 |
3.4.21.9 | biotechnology |
purification of 6.8 mg bioactive enzyme from 1l fermentation broth |
683994 |
3.4.21.9 | biotechnology |
study presents a simple and cost-effective procedure for a large-scale production |
684030 |
3.4.21.9 | synthesis |
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 |