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proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
-
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
active site serine, catalytic triad H57, D107, and S195
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
belongs to the group of Janus-faced proteinases with dual specificity
proteolytic cleavage of polypeptides to large and stable peptides, preferential cleavage sites: Lys-, Arg-, Tyr-, Phe-, Leu-, -Pro
serine protease which has a dual specificity, i.e. both trypsin-like and chymotrypsin-like activities
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alpha-N-acetyl-Leu-Leu-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Leu-Arg + 4-nitroaniline
-
-
-
?
alpha-N-acetyl-Leu-Lys-Arg-4-nitroanilide + H2O
alpha-N-acetyl-Leu-Lys + Arg + 4-nitroaniline
-
-
-
?
alpha-N-benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
alpha-N-benzoyl-Val-Gly-Arg + 4-nitroaniline
-
-
-
?
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ala-Arg + 4-nitroaniline
-
-
-
?
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg-4-nitroanilide + H2O
alpha-N-benzyloxycarbonyl-Ala-Ala-Ile-Arg-Arg + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Phe + 4-nitroaniline
alpha-N-succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
alpha-N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Gly-Gly-Phe + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ser-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Ser-Pro-Lys + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ser-Thr-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Ser-Thr-Pro-Lys + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Thr-Pro-Lys-4-nitroanilide + H2O
alpha-N-succinyl-Thr-Pro-Lys + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
alpha-N-t-butoxycarbonyl-Gly-Phe-Arg-4-nitroanilide + H2O
N-t-butoxycarbonyl-Gly-Phe-Arg + 4-nitroaniline
-
-
-
?
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
alpha-N-tosyl-Gly-Pro-Lys + 4-nitroaniline
angiotensin II + H2O
fragments of angiotensin II
enzyme cleaves bond between residues 2-3 and 4-5
-
-
?
angiotensinogen-(1-14) + H2O
fragments of angiotensinogen-(1-14)
bovine duodenase + H2O
fragments of bovine duodenase
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
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
Escherichia coli La-protease + H2O
fragments of Escherichia coli La-protease
enzyme cleaves bond between residues 219-220 and 239-240
-
-
?
glucagon + H2O
fragments of glucagon
human gamma-interferon + H2O
fragments of human gamma-interferon
enzyme cleaves bond between residues 69-70
-
-
?
human interleukin II-(59-79) + H2O
fragments of human interleukin II-(59-79)
enzyme cleaves bond between residues 66-67
-
-
?
human proinsulin + H2O
fragments of human proinsulin
cleaved bonds, overview
-
-
?
LEEELKPLEEVLNL + H2O
LEEELKPL + EEVLNL
-
-
-
?
LVTQEVSPKIVGGS + H2O
LVTQEVSPK + IVGGS
-
-
-
?
melittin + H2O
fragments of melittin
Naja naja oxiana neurotoxin II + H2O
fragments of Naja naja oxiana neurotoxin II
enzyme cleaves bond between residues 15-16, 26-27, 44-45, and 32-33
-
-
?
polypeptide + H2O
peptides
porcine proinsulin + H2O
fragments of porcine proinsulin
protease-activated receptor-1 + H2O
?
-
-
-
?
surfagon + H2O
fragments of surfagon
enzyme cleaves bond between residues 3-4
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Thr-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
-
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
-
?
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
-
-
-
?
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
-
-
-
-
?
alpha-N-succinyl-Val-Pro-Phe-4-nitroanilide + H2O
alpha-N-succinyl-Val-Pro-Phe + 4-nitroaniline
-
-
-
?
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
alpha-N-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
alpha-N-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
alpha-N-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
angiotensinogen-(1-14) + H2O
fragments of angiotensinogen-(1-14)
-
-
-
?
angiotensinogen-(1-14) + H2O
fragments of angiotensinogen-(1-14)
enzyme cleaves bond between residues 8-9
-
-
?
bovine serum albumin + H2O
fragments of bovine serum albumin
enzyme cleaves bond between residues 27-28, 41-42, 64-65, 210-211, 223-224, 231-232, 238-239, and 409-410
-
-
?
bovine serum albumin + H2O
fragments of bovine serum albumin
enzyme cleaves the bonds Phe26-Ser27, Lys40-Leu41, Lys63-Ser64, Lys209-Ala210, Lys230-Leu231, Lys237-Val238, and Tyr409-Thr410
-
-
?
glucagon + H2O
fragments of glucagon
-
-
-
?
glucagon + H2O
fragments of glucagon
enzyme cleaves bond between residues 12-13 and 18-19
-
-
?
glucagon + H2O
fragments of glucagon
enzyme cleaves the bonds Lys12-Arg13 and Arg18-Ala19
-
-
?
melittin + H2O
fragments of melittin
-
-
-
?
melittin + H2O
fragments of melittin
enzyme cleaves bond between residues 6-7, 7-8, 9-10, and 22-23
-
-
?
melittin + H2O
fragments of melittin
leaved sites, specificity, overview
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
enzyme belongs to the serine protease subfamily
-
-
?
polypeptide + H2O
peptides
-
enzyme belongs to the serine protease subfamily
-
-
?
polypeptide + H2O
peptides
enzyme belongs to the serine protease subfamily
-
-
?
polypeptide + H2O
peptides
enzyme shows very broad substrate specificity due to absence of the SH-bridge at residues 191 and 220, chymotrypsinogen numbering, with retention of normal catalytic activity compared to other serine proteases, similar to granzyme-like proteases
-
-
?
porcine proinsulin + H2O
fragments of porcine proinsulin
enzyme cleaves bond between residues 29-30, 31-32, 32-33, 56-57, 64-65 and 66-67
-
-
?
porcine proinsulin + H2O
fragments of porcine proinsulin
enzyme cleaves the bonds Lys-29-Thr30, Arg31-Arg32, Arg32-Glu33, Leu56-Ala57, Lys64-Arg65, and Arg66-Gly67
-
-
?
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alpha-N-tosyl-L-lysine chloromethane
Bowman Birk soybean inhibitor
-
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
-
phenylmethanesulfonyl fluoride
soybean Bauman-Birk protease inhibitor
40% reduced activity in the presence of 0.6 mM
-
white ovomucoid
from chicken egg
-
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
-
alpha-N-tosyl-L-lysine chloromethane
-
alpha-N-tosyl-L-lysine chloromethane
inhibitory effect on chymotrypsin-like and trypsin-like activity
Bowman Birk soybean inhibitor
-
-
Bowman Birk soybean inhibitor
-
-
-
Bowman Birk soybean inhibitor
the enzyme binds to the antichymotrypsin site of the inhibitor
-
diisopropylphosphofluoridate
irreversible inhibition
diisopropylphosphofluoridate
complete inhibition, irreversible inhibition
Kunitz type soybean trypsin inhibitor
-
-
Kunitz type soybean trypsin inhibitor
inhibitory effect on chymotrypsin-like and trypsin-like activity
-
phenylmethanesulfonyl fluoride
-
phenylmethanesulfonyl fluoride
irreversible inhibition
phenylmethanesulfonyl fluoride
-
irreversible inhibition
Trypsin inhibitor
from bovine lungs, from Lima beans, inhibitory effect on chymotrypsin-like and trypsin-like activity
-
Trypsin inhibitor
from soybean
-
Trypsin inhibitor
from tree-thorned acacia, from kidney bean, from soybean, from Lima beans
-
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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)
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
-
brenda
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
brenda
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
brenda
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)
-
brenda
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
brenda