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Information on EC 3.4.21.B3 - duodenase and Organism(s) Bos taurus and UniProt Accession P80219

for references in articles please use BRENDA:EC3.4.21.B3
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B3 duodenase
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This record set is specific for:
Bos taurus
UNIPROT: P80219
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
Synonyms
duodenase, dual-specificity duodenase, granzyme-like protein iii, chymotrypsin-like duodenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chymotrypsin-like duodenase
-
dual-specificity duodenase
-
duodenase
-
duodenase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
146702-80-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Leu-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Lys + Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
alpha-N-benzoyl-Val-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Phe + 4-nitroaniline
show the reaction diagram
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Gly-Gly-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Ser-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Ser-Thr-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Thr-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Thr-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
show the reaction diagram
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide + H2O
N-t-butoxycarbonyl-Gly-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
alpha-N-tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
angiotensin II + H2O
fragments of angiotensin II
show the reaction diagram
enzyme cleaves bond between residues 2-3 and 4-5
-
-
?
angiotensinogen-(1-14) + H2O
fragments of angiotensinogen-(1-14)
show the reaction diagram
bovine duodenase + H2O
fragments of bovine duodenase
show the reaction diagram
enzyme cleaves bond between residues 14-15, 17-18, 63-64, 70-71, 110-111, 138-139, 157-158, 162-163, 174-175 and 197-198
-
-
?
bovine proenteropeptidase + H2O
enteropeptidase fragments
show the reaction diagram
inactive protease substrate from bovine duodenal mucosa, recombinant 150 kDa glycoprotein
activated protease, cleaved into 2 fragments corresponding to heavy and light chain of the enteropeptidase, 130-140 kDa and 43 kDa
-
?
bovine serum albumin + H2O
fragments of bovine serum albumin
show the reaction diagram
Escherichia coli La-protease + H2O
fragments of Escherichia coli La-protease
show the reaction diagram
enzyme cleaves bond between residues 219-220 and 239-240
-
-
?
FMRF-NH2 + H2O
?
show the reaction diagram
-
-
-
?
glucagon + H2O
fragments of glucagon
show the reaction diagram
human gamma-interferon + H2O
fragments of human gamma-interferon
show the reaction diagram
enzyme cleaves bond between residues 69-70
-
-
?
human interleukin II-(59-79) + H2O
fragments of human interleukin II-(59-79)
show the reaction diagram
enzyme cleaves bond between residues 66-67
-
-
?
human proinsulin + H2O
fragments of human proinsulin
show the reaction diagram
cleaved bonds, overview
-
-
?
LEEELKPLEEVLNL + H2O
LEEELKPL + EEVLNL
show the reaction diagram
-
-
-
?
LVTQEVSPKIVGGS + H2O
LVTQEVSPK + IVGGS
show the reaction diagram
-
-
-
?
melittin + H2O
fragments of melittin
show the reaction diagram
Naja naja oxiana neurotoxin II + H2O
fragments of Naja naja oxiana neurotoxin II
show the reaction diagram
enzyme cleaves bond between residues 15-16, 26-27, 44-45, and 32-33
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
porcine proinsulin + H2O
fragments of porcine proinsulin
show the reaction diagram
protease-activated receptor-1 + H2O
?
show the reaction diagram
-
-
-
?
surfagon + H2O
fragments of surfagon
show the reaction diagram
enzyme cleaves bond between residues 3-4
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Thr-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polypeptide + H2O
peptides
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-N-tosyl-L-lysine chloromethane
Bowman Birk soybean inhibitor
-
chymostatin
-
chymotrypsin inhibitor
form I and II from potato, from kidney bean
-
diisopropylphosphofluoridate
EDTA
weak inhibition at high concentration
Human alpha1-proteinase inhibitor
suicide mechanism, regulatory effect
-
inhibitor-chymotrypsin complex
no inhibition of trypsin-like and chymotrypsin-like activity by EDTA, Ca2+, and benzamidine
-
Kunitz type soybean trypsin inhibitor
-
o-phenanthroline
weak
phenylmethanesulfonyl fluoride
soybean Bauman-Birk protease inhibitor
40% reduced activity in the presence of 0.6 mM
-
Trypsin inhibitor
-
white ovomucoid
from chicken egg
-
alpha1-antitrypsin
-
-
-
antichymotrypsin
-
-
-
antichymotrypsin P2-P3'
-
-
-
antichymotrypsin P3-P4'
-
-
-
antichymotrypsin P4-P3'
-
-
-
antichymotrypsin P6-P4'
-
-
-
Human alpha2-macroglobulin
-
complete inhibition in less than 30 s at equimolar ratio of the inhibitor and enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.4
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide
pH 8.0, 37°C
3.2
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide
pH 8.0, 37°C
0.54
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide
pH 8.0, 37°C
0.28 - 1.1
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide
0.8 - 1.3
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide
1.1
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide
pH 8.0, 37°C
0.56 - 1.1
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
1.5
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide
pH 8.0, 37°C
1
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide
pH 8.0, 37°C
0.39
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide
pH 8.0, 37°C
1.2
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide
pH 8.0, 37°C
0.2
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide
pH 8.0, 37°C
0.37
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide
pH 8.0, 25°C
0.027 - 0.042
angiotensinogen-(1-14)
0.1
FMRF-NH2
pH 8.0, 37°C <2>
1
LEEELKPLEEVLNL
pH 8.0, 37°C
0.087
LVTQEVSPKIVGGS
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide
pH 8.0, 37°C
1.2
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide
pH 8.0, 37°C
6
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide
pH 8.0, 37°C
14.4
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide
pH 8.0, 37°C
3.6 - 13.8
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide
1.2
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide
pH 8.0, 37°C
9 - 68.4
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
3.6
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide
pH 8.0, 37°C
156
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide
pH 8.0, 37°C
438
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide
pH 8.0, 37°C
33 - 168
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide
24
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide
pH 8.0, 37°C
126 - 186
angiotensinogen-(1-14)
4.2
FMRF-NH2
pH 8.0, 37°C
60
LEEELKPLEEVLNL
pH 8.0, 37°C
84
LVTQEVSPKIVGGS
pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000027 - 0.000004
Bowman Birk soybean inhibitor
pH 8.0, 25°C
-
0.0004
Bowman Birk soybean inhibitor-trypsin complex
pH 8.0, 25°C
-
0.000013
Human alpha1-proteinase inhibitor
pH 8.0, 25°C
-
0.002
Kunitz soybean trypsin inhibitor
pH 8.0, 37°C
-
0.00004
Kunitz type soybean trypsin inhibitor
pH 8.0, 25°C
-
0.000013
alpha1-antitrypsin
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.00033
antichymotrypsin P2-P3'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.0019
antichymotrypsin P3-P4'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.00043
antichymotrypsin P4-P3'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
0.033
antichymotrypsin P6-P4'
-
in 0.01 M acetate buffer, pH 4.5, at 25°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.162
purified enzyme
53
purified enzyme, substrate Ac-Leu-Lys-Arg-4-nitroanilide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
broad optimum at pH 8.0-10.5, maximum at pH 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9 - 8.2
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from pulmonary artery
Manually annotated by BRENDA team
intestinal mucosa
Manually annotated by BRENDA team
around brochioles and within alveolar septa
Manually annotated by BRENDA team
spindle or stellate-shaped, located pricipally in the lamina propria and submucosa
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDN1_BOVIN
251
0
27556
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24970
mass spectrometry
29000
gel filtration
29060
amino acid sequence determination, without sugar chain
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, protein solution: 10 mg/ml, 50 mM K/Na phosphate, pH 6.7, 1 mM NaN3, 10-14% polyethylene glycol 3350, 4C, three-dimensional structure determination by X-ray diffraction and analysis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
stable
658592
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
10 min, in solution at neutral pH, loss of 30% activity
70
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
methanol 1% v/v stabilizes the purified enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, in water stable for at least 1 year, lyophilized stable for several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at least 90% purity
CM Sepharose FF column chromatography, STI Sepharose 6B column chromatography
to homogeneity
two chromatographic steps
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in analytical protein chemistry
biotechnology
comparative evaluation of specificity of different proteases can give rise to methods employing new proteases in biotechnology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gladysheva, I.P.; Zamolodchikova, T.S.; Sokolova, E.A.; Larionova, N.I.
Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type
Biochemistry (Moscow)
64
1244-1249
1999
Bos taurus (P80219)
Manually annotated by BRENDA team
Sokolova, E.A.; Mirgorodskaya, O.A.; Roepstorff, P.; Savelyeva, N.V.; Zamolodchikova, T.S.
Comparative study of the action of bovine duodenal proteinases (duodenases) on polypeptide substrates
Biochemistry (Moscow)
66
62-67
2001
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Gladysheva, I.P.; Popykina, N.A.; Zamolodchikova, T.S.; Larionova, N.I.
Interaction between duodenase and alpha1-proteinase inhibitor
Biochemistry (Moscow)
66
682-687
2001
Bos taurus (P80219)
Manually annotated by BRENDA team
Zamolodchikova T.S.; Vorotyntseva T.I.; Antonov V.K.
Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Purification and properties
Eur. J. Biochem.
227
866-872
1995
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Zamolodchikova T.S.; Vorotyntseva T.I.; Nazimov I.V.; Grishina G.A.
Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Primary structure of the enzyme
Eur. J. Biochem.
227
873-879
1995
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Zamolodchikova, T.S.; Sokolova, E.A.; Alexandrov, S.L.; Mikhaleva, II; Prudchenko, I.A.; Morozov, I.A.; Kononenko, N.V.; Mirgorodskaya, O.A.; Da, U.; Larionova, N.I.; Pozdnev, V.F.; Ghosh, D.; Duax, W.L.; Vorotyntseva, T.I.
Subcellular localization, substrate specificity and crystallization of duodenase, a potential activator of enteropeptidase
Eur. J. Biochem.
249
612-621
1997
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Sokolova, E.A.; Starkova, N.N.; Vorotyntseva, T.I.; Zamolodchikova, T.S.
A serine protease from the bovine duodenal mucosa, chymotrypsin-like duodenase
Eur. J. Biochem.
255
501-507
1998
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Pemberton, A.D.; Zamolodchikova, T.S.; Scudamore, C.L.; Chilvers, E.R.; Miller, H.R.; Walker, T.R.
Proteolytic action of duodenase is required to induce DNA synthesis in pulmonary artery fibroblasts
Eur. J. Biochem.
269
1171-1180
2002
Bos taurus (P80219)
Manually annotated by BRENDA team
Zamolodchikova, T.S.; Sokolova, E.A.; Lu, D.; Sadler, J.E.
Activation of recombinant proenteropeptidase by duodenase
FEBS Lett.
466
295-299
2000
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Stoesser, G.; Baker, W.; van den Broek, A.; Garcia-Pastor, M.; Kanz, C.; Kulikova, T.; Leinonen, R.; Lin Q.; Lombard, V.; Lopez, R.; Mancuso, R.; Nardone, F.; Stoehr, P.; Tuli, M.A.; Tzouvara, K.; Vaughan, R.
The EMBL Nucleotide Sequence Database: major new developments
Nucleic Acids Res.
31
17-22
2003
Bos taurus (P80219)
Manually annotated by BRENDA team
Mirgorodskaya, O.; Kazanina, G.; Mirgorodskaya, E.; Vorotyntseva, T.; Zamolodchikova, T.; Alexandrov, S.
A comparative study of the specificity of melittin hydrolysis by duodenase, trypsin and plasmin
Protein Pept. Lett.
3
315-320
1996
Bos taurus (P80219)
-
Manually annotated by BRENDA team
Pletnev V.Z.; Zamolodchikova T.S.; Pangborn W.A.; Duax W.L.
Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities
Proteins
41
8-16
2000
Bos taurus (P80219), Bos taurus
Manually annotated by BRENDA team
Denisenko, O.O.; Zamolodchikova, T.S.; Popykina, N.A.; Larionova, N.I.
Interaction between human alpha2-macroglobulin and duodenase, a serine proteinase with dual specificity
Biochemistry (MOSCOW)
71
658-666
2006
Bos taurus
Manually annotated by BRENDA team
Makarova, A.M.; Zamolodchikova, T.S.; Rumsh, L.D.; Strukova, S.M.
Duodenase activates rat peritoneal mast cells via protease-activated receptors of type 1
Russ. J. Bioorg. Chem.
33
482-487
2007
Bos taurus (P80219)
-
Manually annotated by BRENDA team
Zamolodchikova, T.S.; Popykina, N.A.; Gladysheva, I.P.; Larionova, N.I.
Effect of reactive center loop structure of antichymotrypsin on inhibition of duodenase activity
Biochemistry
74
824-833
2009
Bos taurus
Manually annotated by BRENDA team