3.4.21.9: enteropeptidase
This is an abbreviated version!
For detailed information about enteropeptidase, go to the full flat file.
Word Map on EC 3.4.21.9
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3.4.21.9
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trypsinogen
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pancreatic
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duodenal
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thioredoxin
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pancreas
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zymogen
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mucosa
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brush
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juice
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refolding
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chymotrypsin
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trypsin-like
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autoactivation
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ni-nta
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sucrase
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agrin
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lactase
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proenzyme
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trx
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chymotrypsinogen
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polyhistidine
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disaccharidase
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scorpion
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pet-32a
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intraductal
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cerulein
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glycodeoxycholic
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tag-free
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biotechnology
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molecular biology
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synthesis
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analysis
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medicine
- 3.4.21.9
- trypsinogen
- pancreatic
- duodenal
- thioredoxin
- pancreas
- zymogen
- mucosa
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brush
- juice
-
refolding
- chymotrypsin
-
trypsin-like
-
autoactivation
-
ni-nta
- sucrase
- agrin
- lactase
- proenzyme
- trx
- chymotrypsinogen
- polyhistidine
- disaccharidase
- scorpion
-
pet-32a
-
intraductal
- cerulein
-
glycodeoxycholic
-
tag-free
- biotechnology
- molecular biology
- synthesis
- analysis
- medicine
Reaction
Activation of trypsinogen by selective cleavage of Lys6-/-Ile bond =
Synonyms
BEK, BEP, bovine enterokinase light chain, bovine enteropeptidase, Chinese bovine enterokinase, Chinese northern yellow bovine enterokinase catalytic subunit, EC 3.4.4.8, EK, EKL, EKL-His6, EKLC, enterokinase, enterokinase light chain, enteropeptidase, enteropeptidase light chain, EP 118-1035, EP-1, EPL, HEK, HEP, human enteropeptidase, L-BEP, L-HEK, L-HEP, native enterokinase, natural enteropeptidase, peptidase, entero-, porcine enterokinase, PRSS7, recombinant bovine enterokinase catalytic subunit protein, recombinant enterokinase light chain, recombinant His-tagged enterokinase light chain, rEKL, rEKL/His, sBEKLC, TMPRSS15
ECTree
3.4.21.9 enteropeptidaseAdvanced search results
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Application on EC 3.4.21.9 - enteropeptidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biotechnology
medicine
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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
molecular biology
synthesis
additional information
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utility of enterokinase light chain as a site-specific cleavage enzyme is hampered by sporadic cleavage at other sites than the canonical D4K recognition sequence
analysis
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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
analysis
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enteropeptidase activity is influenced by accessibility of the target site and by downstream sequences
biotechnology
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EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation
biotechnology
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purification of 6.8 mg bioactive enzyme from 1l fermentation broth
biotechnology
study presents a simple and cost-effective procedure for a large-scale production
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
molecular biology
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the enzyme is used for cleavage of the N-terminal part of recombinant human interferon-alpha2a (IFN-alpha2a) and IFN-alpha2b, expressed in Escherichia coli strains strains BL21 and BL21 (DE3), for production of the protein without the N-terminal methionine residue
molecular biology
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the high degree of specificity exhibited by enteropeptidase makes it a suitable reagent for cleaving recombinant proteins to remove affinity or other tags. However often unwanted cleavages elsewhere in the protein occur during cleavage of fusions when high amount of enzyme is required
molecular biology
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the high degree of specificity exhibited by enteropeptidase makes it a suitable reagent for cleaving recombinant proteins to remove affinity or other tags. However often unwanted cleavages elsewhere in the protein occur during cleavage of fusions when high amount of enzyme is required
molecular biology
the high specificity of the target site makes enterokinase an ideal tool for cleaving fusion proteins at defined cleavage sites
synthesis
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the enzyme may be useful in amino acid sequence studies for the production of large fragents. The enzyme may also be useful in DNA-recombinant studies in releasing the desired polypeptide chain from neighboring sequences
synthesis
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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
synthesis
the enzyme can be used for cleavage of fusion proteins due to its high specific activity
synthesis
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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
