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Information on EC 3.4.21.9 - enteropeptidase and Organism(s) Bos taurus and UniProt Accession P98072
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3.4.21.9 enteropeptidaseSpecify your search results
Word Map
- 3.4.21.9
- trypsinogen
- pancreatic
- duodenal
- thioredoxin
- pancreas
- zymogen
- mucosa
-
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
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
enterokinase, enteropeptidase, human enteropeptidase, l-hep, enteropeptidase light chain, bovine enteropeptidase, enterokinase light chain, porcine enterokinase, bovine enterokinase light chain, tmprss15, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
enterokinase
enteropeptidase
peptidase, entero-
-
-
-
-
enterokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
9014-74-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Val-(Ala)2-(Asp)2-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-(Asp)2-Lys + Ile-Val-Gly
109.3% relative activity
-
-
?
Val-(Ala)2-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-Asp-Ala-Lys + Ile-Val-Gly
16.8% relative activity
-
-
?
Val-(Ala)3-Asp-Lys-Ile-Val-Gly + H2O
Val-(Ala)3-Asp-Lys + Ile-Val-Gly
75.6% relative activity
-
-
?
Val-(Asp)2-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-(Asp)2-Ala-Asp-Lys + Ile-Val-Gly
76.1% relative activity
-
-
?
Val-(Asp)3-Ala-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Ala-Lys + Ile-Val-Gly
16.3% relative activity
-
-
?
Val-(Asp)3-Glu-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Glu-Lys + Ile-Val-Gly
42.5% relative activity
-
-
?
Val-(Asp)4-Arg-Ile-Val-Gly + H2O
Val-(Asp)4-Arg + Ile-Val-Gly
115.2% relative activity
-
-
?
Val-(Asp)4-Lys-Ile-Val-Gly + H2O
Val-(Asp)4-Lys + Ile-Val-Gly
100% relative activity
-
-
?
Val-Ala-(Asp)2-Ala-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)2-Ala-Lys + Ile-Val-Gly
4.3% relative activity
-
-
?
Val-Ala-(Asp)3-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)3-Lys + Ile-Val-Gly
104.2% relative activity
-
-
?
Val-Ala-Asp-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-Ala-Asp-Ala-Asp-Lys + Ile-Val-Gly
48.1% relative activity
-
-
?
Val-Asp-(Ala)2-Asp-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)2-Asp-Lys + Ile-Val-Gly
82.6% relative activity
-
-
?
Val-Asp-(Ala)3-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)3-Lys + Ile-Val-Gly
7.1% relative activity
-
-
?
Val-Asp-Ala-(Asp)2-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-(Asp)2-Lys + Ile-Val-Gly
117.4% relative activity
-
-
?
Val-Asp-Ala-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-Asp-Ala-Lys + Ile-Val-Gly
21.1% relative activity
-
-
?
APFDDDDKIVGG + H2O
?
N-terminal dodecapeptides of human cationic trypsinogen
-
-
?
APFDDDGKIVGG + H2O
?
N-terminal dodecapeptides of human pancreatitis-associated mutant variant of trypsinogen
-
-
?
APFDDDGRIVGG + H2O
?
N-terminal dodecapeptides of human cationic tryosinogen
-
-
?
formyl-Ala-Phe-Arg-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
formyl-Ala-Phe-Lys-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
glutathione S-transferase-enterokinase + H2O
enterokinase + glutathione S-transferase
GST-EK harboring an EK site
-
-
?
Gly-(L-Asp)4-L-Lys-2-naphthylamide + H2O
Gly-(L-Asp)4-L-Lys + 2-naphthylamine
-
-
-
-
?
Gly-(L-Asp)4-L-Lys-2-naphthylamide + H2O
Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
Gly-Asp-Asp-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
-
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide + H2O
naphthylamine + Gly-Asp-Asp-Asp-Asp-Lys
-
GD4K-na
-
-
?
Gly-Gly-Asp-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
Gly-Gly-Asp-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
-
-
-
?
Gly-Gly-Gly-Asp-Asp-Lys-Ile-Val-Gly-Gly + H2O
Gly-Gly-Gly-Asp-Asp-Lys + Ile-Val-Gly-Gly
-
-
-
-
?
Gly-Gly-Gly-Gly-Asp-Lys-Ile-Val-Gly-Gly + H2O
Gly-Gly-Gly-Gly-Asp-Lys + Ile-Val-Gly-Gly
-
-
-
-
?
GST-GFPuv + H2O
GST + GFPuv
harboring an EK site between GST and the green fluorescent protein GFPuv
-
-
?
Nalpha-acetyltrypsinogen + H2O
Nalpha-acetylactivation peptides + trypsin
-
-
-
?
PrAD4KP26 + H2O
?
-
fusion protein containing a modified protein A as a carrier and recoverin as a target protein
-
-
?
S-carboxyamidomethyl derivative of bovine serum albumin + H2O
?
-
bovine serum albumin is resistant in its native state, somewhat susceptible as the S-carboxyamidomethyl derivative and highly susceptible as the S-carboxymethyl derivative
-
-
?
thiobenzyl benzyloxy-carbonyl-L-lysinate + H2O
3-carboxy-4-nitrophenoxide + ?
-
-
-
-
?
thioredoxin-human epidermal growth factor fusion protein + H2O
thioredoxin + human epidermal growth factor
-
Trx/hEGF
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
-
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
-
-
?
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
Gly-Asp-Asp-Asp-Asp-Lys + 2-naphthylamine
-
-
-
-
?
Trypsinogen + H2O
?
-
initiates activation of pancreatic hydrolases by cleaving and activating trypsinogen
-
-
?
Trypsinogen + H2O
?
-
the enzyme plays a key role in initiating the proteolytic digestion cascade in duodenum by converting trypsinogen to trypsin
-
-
?
trypsinogen + H2O
trypsin + ?
-
cleaved exclusively at the Lys6-Ile7-peptide bond
-
-
?
additional information
?
-
Val-(Asp)2-(Ala)2-Lys-Ile-Val-Gly, Val-Ala-Asp-(Ala)2-Lys-Ile-Val-Gly, Val-(Asp)4-Lys-Ile-Val-Gly, Val-(Asp)4-Ala-Ile-Val-Gly and Val-(Asp)4-Glu-Ile-Val-Gly are not hydrolyzed
-
-
?
additional information
?
-
-
the enteropeptidase heavy chain has little influence on the recognition of small peptides, but strongly influences macromolecular substrate recognition
-
-
?
additional information
?
-
-
the catalytic subunit retains the restricted specificity of intact enterokinase but the rate of activation of trypsinogen is much slower
-
-
?
additional information
?
-
-
the highly specific protease cleaves immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence
-
-
?
additional information
?
-
-
susceptible bonds are either Lys or Arg. The preceding acidic residues could be either Asp, Glu, or carboxymethyl cysteine
-
-
?
additional information
?
-
-
cleaves after Lys residues of peptidyl substrates that resemble trypsinogen activation peptides such as Val-(Asp)4-Lys
-
-
?
additional information
?
-
-
enterokinase light chain is a serine protease that recognizes Asp-Asp-Asp-Asp-Lys, D4K, sequence and cleaves the C-terminal peptide bond of the lysine residue
-
-
?
additional information
?
-
-
high degree of cleavage specificity is exhibited by enteropeptidase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enterokinase light chain is a serine protease that recognizes Asp-Asp-Asp-Asp-Lys, D4K, sequence and cleaves the C-terminal peptide bond of the lysine residue
-
-
?
Trypsinogen + H2O
?
-
initiates activation of pancreatic hydrolases by cleaving and activating trypsinogen
-
-
?
Trypsinogen + H2O
?
-
the enzyme plays a key role in initiating the proteolytic digestion cascade in duodenum by converting trypsinogen to trypsin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.75
Gly-(L-Asp)4-L-Lys-2-naphthylamide
pH and temperature not specified in the publication
1.5
human cationic trypsinogen
-
37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.45 nM enteropeptidase
-
1.2
bovine trypsinogen
-
37 °C, 25 mM Tris-HCl pH 8.4, 10 mM CaCl2, 0. 4 mM ovomucoid, 0.3 nM enteropeptidase
-
5.6
bovine trypsinogen
-
21 °C, 50 mM sodium citrate pH 5.6, 1 nM enteropeptidase
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.8
human cationic trypsinogen
-
37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.45 nM enteropeptidase
-
6.9
bovine trypsinogen
-
37 °C, 25 mM Tris-HCl pH 8.4, 10 mM CaCl2, 0. 4 mM ovomucoid, 0.3 nM enteropeptidase
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enterokinase molecule from the mucosal fluid is identical with that found previously in the mucosal cells but differs from that in the intestinal contents
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme triggers the activation of the zymogens in pancreatic juice by converting trypsinogen into trypsin
additional information
additional information
-
enterokinase shows no strict cleavage site specificity because of sporadic cleavage at other sites, which consist of acidic and basic residues
additional information
-
improved efficiency of fusion proteins cleavage by enteropeptidase by substitution of the Lys residue by Arg in specific cleavage sequence (Asp)4-Lys. 3-6fold lower amounts of the catalytic subunit of enteropeptidase is required for 95% cleavage of Trx/TRAIL and Trx/FGF-2 fusions with (Asp)4-Arg cleavage sequence in comparison to native sequence (Asp)4-Lys. Reduced amount of non-specifically cleaved peptide fragments are observed during cleavage of (Asp)4-Lys/Arg mutated fusions
additional information
-
low enzyme concentrations protect hippocampal neurons against the death caused by 0.1 mM glutamate, via a proteinase activated receptor PAR1-dependent mechanism, while High concentrations of the enzyme causes the death of neurons mainly through necrosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ENTK_BOVIN
1035
1
114887
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enteropeptidase catalytic domain to 2.3 A resolution in complex with the inhibitor Val-(Asp)4-Lys-chloromethane
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K99A
-
no cleavage of trypsinogen or Gly-(Asp)4-Lys-beta-naphthylamide and reduced rate of inhibition by Val-(Asp)4-Lys-chloromethane
Y174K/K99M
-
site-directed mutagenesis, the mutant does not form the active structure
Y174K/K99Q
-
site-directed mutagenesis, the mutantion results in a more site-specific enterokinase light chain
Y174R/K99M
-
site-directed mutagenesis, the mutant does not form the active structure
Y174R/K99Q
-
site-directed mutagenesis, the mutant does not form the active structure
additional information
additional information
-
improved efficiency of fusion proteins cleavage by enteropeptidase by substitution of the Lys residue by Arg in specific cleavage sequence (Asp)4-Lys
additional information
-
in order to produce more site-specific enterokinase light chain, EKL, several mutants are generated with substitutions at Tyr174 and Lys99 using the protein disulfide isomerase fusion system. Substitution of Tyr174 by basic residues confers higher specificity on EKL. Mutant enzyme substrate specificity and modeling, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
complete destruction of activity towards trypsinogen after 2 min, 60% loss of esterase activity after 8 min. Presence of 4 mM CaCl2 stabilizes both activities
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, enzyme immobilized onto amine-modified magnetic nanoparticles, 30 days, 10% loss of activity
-
The free enzyme has a half life of 8 days at 23°C. The immobilised enzyme has a half life of 29 days at 23°C. The immobilised and glutardialdehyde treated enzyme has a half life of 36 days at 23°C. The free enzyme has a half life of 85 days at 4°C. The immobilised enzyme has a half life of 10 month at 4°C.
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant fusion protein by osmotic shock technique and nickel affinity column chromatography
-
of the recombinant fusion protein using nickel affinity column chromatography, refolding and auto-catalytic cleavage
solubilization of inclusion bodies with 6 M guanidine-HCl, affinity chromatography on STI-agarose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as glutathione S-transferase-fusion protein, the gene is a Pro82Arg/Glu176Asp variant of the known bovine EK
expression of a 26300 Da protein containing the catalytic domain of bovine enterokinase, expression in methylotrophic yeast Pichia pastoris
-
expression of wild-type and mutant enterokinase light chain in Escherichia coli strain Rosetta (DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
molecular biology
-
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
synthesis
additional information
-
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
biotechnology
-
EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation
biotechnology
-
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
synthesis
-
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
-
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grant, D.A.W.; Hermon-Taylor, J.
Enterokinase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
143-155
1984
Bos taurus, Homo sapiens, Sus scrofa
-
Light, A.; Fonseca, P.
The preparation and properties of the catalytic subunit of bovine enterokinase
J. Biol. Chem.
259
13195-13198
1984
Bos taurus
Fonseca, P.; Light, A.
The purification and characterization of bovine enterokinase from membrane fragments in the duodenal mucosal fluid
J. Biol. Chem.
258
14516-14520
1983
Bos taurus
Light, A.; Savithri, H.S.; Liepnieks, J.J.
Specificity of bovine enterokinase toward protein substrates
Anal. Biochem.
106
199-206
1980
Bos taurus
Liepnieks, J.J.; Light, A.
The preparation and properties of bovine enterokinase
J. Biol. Chem.
254
1677-1683
1979
Bos taurus
Anderson, L.E.; Walsh, K.A.; Neurath, H.
Bovine enterokinase. Purification, specificity, and some molecular properties
Biochemistry
16
3354-3360
1977
Bos taurus
Lu, D.; Futterer, K.; Korolev, S.; Zheng, X.; Tan, K.; Waksman, G.; Sadler, J.E.
Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
J. Mol. Biol.
292
361-373
1999
Bos taurus
Lu, D.; Yua, X.; Zheng, X.; Sadler, J.E.
Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
J. Biol. Chem.
272
31293-31300
1997
Bos taurus
Light, A.; Janska, G.
Enterokinase (enteropeptidase): comparative aspects
Trends Biochem. Sci.
14
110-112
1989
Bos taurus, Homo sapiens, Sus scrofa
Vozza, L.A.; Wittwer, L.; Higgins, D.R.; Purcell, T.J.; Bergseid, M.; Collins-Racie, L.A.; LaVallie, E.R.; Hoeffler, J.P.
Production of a recombinant bovine enterokinase catalytic subunit in the methylotrophic yeast Pichia pastoris
Biotechnology
14
77-81
1996
Bos taurus
Collins-Racie, L.A.; McColgan, J.M.; Grant, K.L.; DiBlasio-Smith, A.; McCoy, J.M.; LaVallie, E.R.
Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using novel secretory fusion partner DsbA
Biotechnology
13
982-987
1995
Bos taurus
Yuan, L.D.; Hua, Z.C.
Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli
Protein Expr. Purif.
25
300-304
2002
Bos taurus
Fang, L.; Sun, Q.M.; Hua, Z.C.
Expression of recombinant chinese bovine enterokinase catalytic subunit in P. pastoris and its purification and characterization
Acta Biochim. Biophys. Sin.
36
513-517
2004
Bos taurus
Mikhailova, A.G.; Likhareva, V.V.; Vaskovsky, B.V.; Garanin, S.K.; Onoprienko, L.V.; Prudchenko, I.A.; Chikin, L.D.; Rumsh, L.D.
Study of secondary specificity of enteropeptidase in comparison with trypsin
Biochemistry (Moscow)
69
909-917
2004
Bos taurus
Huang, H.; Zhao, Y.; Yi-ru, G.
Prokaryotic expression of Chinese bovine enterokinase catalytic subunit
Chin. Med. Sci.
117
286-290
2004
Bos taurus
Nemoda, Z.; Sahin-Toth, M.
The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition
J. Biol. Chem.
280
29645-29652
2005
Bos taurus, Homo sapiens
Peng, L.; Zhong, X.; Ou, J.; Zheng, S.; Liao, J.; Wang, L.; Xu, A.
High-level secretory production of recombinant bovine enterokinase light chain by Pichia pastoris
J. Biotechnol.
108
185-192
2004
Bos taurus
Gasparian, M.E.; Ostapchenko, V.G.; Dolgikh, D.A.; Kirpichnikov, M.P.
Biochemical characterization of human enteropeptidase light chain
Biochemistry (Moscow)
71
113-119
2006
Bos taurus, Homo sapiens
Kubitzki, T.; Noll, T.; Luetz, S.
Immobilisation of bovine enterokinase and application of the immobilised enzyme in fusion protein cleavage
Bioprocess Biosyst. Eng.
31
173-182
2008
Bos taurus
Huang, L.; Ruan, H.; Gu, W.; Xu, Z.; Cen, P.; Fan, L.
Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli
Prep. Biochem. Biotechnol.
37
205-217
2007
Bos taurus
Tan, H.; Wang, J.; Zhao, Z.K.
Purification and refolding optimization of recombinant bovine enterokinase light chain overexpressed in Escherichia coli
Protein Expr. Purif.
56
40-47
2007
Bos taurus (Q6B4R4), Bos taurus
Mikhailova, A.G.; Likhareva, V.V.; Teich, N.; Rumsh, L.D.
The ways of realization of high specificity and efficiency of enteropeptidase
Protein Pept. Lett.
14
227-232
2007
Homo sapiens, Bos taurus (Q6B4R4), Bos taurus
Kim, Y.T.; Nishii, W.; Matsushima, M.; Inoue, H.; Ito, H.; Park, S.J.; Takahashi, K.
Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs
Biosci. Biotechnol. Biochem.
72
905-908
2008
Bos taurus (P98072), Sus scrofa (P98074)
Kubitzki, T.; Minoer, D.; Mackfeld, U.; Oldiges, M.; Noll, T.; Luetz, S.
Application of immobilized bovine enterokinase in repetitive fusion protein cleavage for the production of mucin 1
Biotechnol. J.
4
1610-1618
2009
Bos taurus
Makarova, A.M.; Gorbacheva, L.R.; Savinkova, I.V.; Mikhailova, A.G.; Rumsh, L.D.; Pinelis, V.G.; Strukova, S.M.
Effect of enteropeptidase on survival of cultured hippocampal neurons under conditions of glutamate toxicity
Biochemistry (Moscow)
75
1153-1159
2010
Bos taurus, Homo sapiens
Chun, H.; Joo, K.; Lee, J.; Shin, H.C.
Design and efficient production of bovine enterokinase light chain with higher specificity in E. coli
Biotechnol. Lett.
33
1227-1232
2011
Bos taurus
Gasparian, M.E.; Bychkov, M.L.; Dolgikh, D.A.; Kirpichnikov, M.P.
Strategy for improvement of enteropeptidase efficiency in tag removal processes
Protein Expr. Purif.
79
191-196
2011
Bos taurus, Homo sapiens
Ostapchenko, V.G.; Gasparian, M.E.; Kosinsky, Y.A.; Efremov, R.G.; Dolgikh, D.A.; Kirpichnikov, M.P.
Dissecting structural basis of the unique substrate selectivity of human enteropeptidase catalytic subunit
J. Biomol. Struct. Dyn.
30
62-73
2012
Bos taurus, Homo sapiens
Azhar, M.; Somashekhar, R.
Production and purification of recombinant enteropeptidase expressed in an insect-baculovirus cell system
Prep. Biochem. Biotechnol.
45
268-278
2015
Bos taurus (R4QR01), Bos taurus
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