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A4-mutant trypsinogen + H2O
?
-
-
-
-
?
AAVERW-streptavidin-R-phycoerythrin conjugate + H2O
AAVERW + streptavidin-R-phycoerythrin conjugate
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
AhR6-C/EBP
?
-
hybrid of the AhR basic region and C/EBP leucine zipper. Reaction under standard conditions (at 37°C in 50 mM Tris buffer, pH 7.6) is rapid and somewhat nonspecific. After just 15 min incubation, 82% of the protein has been cleaved at multiple sites, prolonged incubation causes further degradation of cleavage products
-
-
?
alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
alpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
APFDDDDRIVGG + H2O
?
-
-
-
?
APFDDDGKIVGG + H2O
?
N-terminal dodecapeptides of human pancreatitis-associated mutant variant of trypsinogen
-
-
?
APFDDDGRIVGG + H2O
?
N-terminal dodecapeptides of human cationic tryosinogen
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
benzyl-L-Arg-2-naphthylamide + H2O
?
benzyloxycarbonyl-L-alanine-X-L-arginine-p-nitroanilide + H2O
p-nitroaniline + benzyloxycarbonyl-L-alanine-X-L-arginine
-
Z-Ala-X-Arg-pNA
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Boc-Glu(OBzl)-Ala-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Glu(OBzl)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
bovine trypsinogen + H2O
?
-
-
-
-
?
DDDK-SA-PE + H2O
DDDK + SA-PE
-
Asp-Asp-Asp-Asp-Lys-fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
DDRRAG-SA-PE + H2O
DDRRAG + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
DRARVW-SA-PE + H2O
DRARVW + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
egg white lysozyme + H2O
?
-
egg white lysozyme from hen
-
-
?
EYDRQL-SA-PE + H2O
EYDRQL + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
formyl-Ala-Phe-Arg-4-nitroanilide + H2O
4-nitroaniline + formyl-Ala-Phe-Arg
-
-
-
-
?
formyl-Ala-Phe-Arg-4-nitroanilide + H2O
?
formyl-Ala-Phe-Lys-4-nitroanilide + H2O
4-nitroaniline + formyl-Ala-Phe-Lys
-
-
-
-
?
formyl-Ala-Phe-Lys-4-nitroanilide + H2O
?
fusion protein Trx/hEGF + H2O
?
the fusion protein Trx/hEGF contains an inter-domain enteropeptidase recognition site
-
?
fusion protein Trx/hIL-13 + H2O
?
the fusion protein Trx/hIL-13 contains an inter-domain enteropeptidase recognition site
-
?
GD4K 2-naphthylamide + H2O
?
-
-
-
-
?
GD4K 7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
GD4KNfa + H2O
?
-
-
-
-
?
GD4R-4-nitroanilide + H2O
?
-
-
-
?
GDDDDK-2-naphthylamide + H2O
GDDDDK + 2-naphthylamine
GDDDDK-4-nitroanilide + H2O
GDDDDK + 4-nitroaniline
-
-
-
?
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-2-naphthylamide + H2O
Gly-Asp-ASp-Asp-Asp + 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-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
-
-
-
-
?
Gly-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys-2-naphthylamide + H2O
Gly-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys + 2-naphthylamine
-
-
-
?
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide + H2O
glycyl-tetra-L-aspartyl-L-lysine + beta-naphthylamine
-
-
-
-
?
GST-GFPuv + H2O
GST + GFPuv
harboring an EK site between GST and the green fluorescent protein GFPuv
-
-
?
GST-vasostatin fusion protein + H2O
?
-
-
-
-
?
human cationic trypsinogen + H2O
?
human thioredoxin fused human NT-proCNP(1-50) + H2O
cleavage products of human thioredoxin fused human NT-proCNP(1-50)
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
interferon-alpha2a + H2O
?
-
recombinantly expressed substrate
-
-
?
interferon-alpha2b + H2O
?
-
recombinantly expressed substrate
-
-
?
LTAEEKAAV + H2O
?
-
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
-
?
MHGERM-SA-PE + H2O
MHGERM + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
MLTAEEKAA + H2O
?
-
Hb 1-9
-
-
?
MSGERM-SA-PE + H2O
MSGERM + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
MUC1-IgG Fc + H2O
MUC1 + IgG Fc
-
fusion protein
-
-
?
mucin 1-IgG2a Fc + H2O
mucin 1 + ?
-
cleavage of the mucin fusion protein
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + benzylmercaptane
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
N-alpha-benzyloxycarbonyl-L-lysine + phenylmethanethiol
-
-
-
-
?
N2-benzoyl-L-Arg ethyl ester + H2O
?
-
-
-
-
?
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
-
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pro-Phe-Arg
-
-
-
?
protein C inhibitor + H2O
?
-
-
-
-
?
S-alkylated soybean trypsin inhibitor + H2O
?
-
limited proteolysis
-
-
?
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
-
-
?
SERAAAG-SA-PE + H2O
SERAAAG + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
SGDRMW-SA-PE + H2O
SGDRMW + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin, exhibits a 17 fold faster cleavage time than DDDK
-
-
?
SGERMMG-SA-PE + H2O
SGERMMG + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
tert-butoxycarbonyl-Gln-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl 7-amide + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
tert-butoxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
thiobenzyl benzyloxy-carbonyl-L-lysinate + H2O
3-carboxy-4-nitrophenoxide + ?
thiobenzyl benzyloxy-carbonyl-L-lysinate + H2O
?
-
-
?
thiobenzyl benzyloxycarbonyl-L-lysinate + H2O
3-carboxy-4-nitrothiophenoxide + ?
-
Z-Lys-SBzl
-
-
?
thiobenzyl benzyloxycarbonyl-L-lysinate + H2O
?
-
-
-
-
?
thioredoxin-DDDD156K-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156K-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156RRK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156RRK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SDK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SDK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate, 9 fusion proteins are tested as substrates, addition of SRLLR residues leads to an increase in activity
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SRK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SRK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SRLK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SRLK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SRLLK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SRLLK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SRLLRK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SRLLRK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate, best substrate for enterokinase activity
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-DDDD156SSK-mouse NT-proCNP(2-40)-DDDK201SRLLR + H2O
cleavage products of thioredoxin-DDDD156SSK-mouse NT-proCNP(2-40)-DDDK201SRLLR
-
22kDA substrate
21 and 16 kDa cleavage products using the recombinant enzyme, multiple cleavage products using the native enzyme
-
?
thioredoxin-fused N-terminal pro-C-type natriuretic peptide + H2O
N-terminal pro-C-type natriuretic peptide fragment + ?
-
-
-
-
?
thioredoxin-human epidermal growth factor fusion protein + H2O
thioredoxin + human epidermal growth factor
thioredoxin-tumor necrosis factor-related apoptosis-inducing ligand fusion protein + H2O
thioredoxin + tumor necrosis factor-related apoptosis-inducing ligand
-
trx/TRAIL
enteropeptidase is used to cleave TRAIL from thioredoxin at enzyme-substrate molar ratio of 1 : 30,000
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
trypsinogen + H2O
trypsin
trypsinogen + H2O
trypsin + ?
Val-(Ala)2-(Asp)2-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-(Asp)2-Lys + Ile-Val-Gly
Val-(Ala)2-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-Asp-Ala-Lys + Ile-Val-Gly
Val-(Ala)3-Asp-Lys-Ile-Val-Gly + H2O
Val-(Ala)3-Asp-Lys + Ile-Val-Gly
Val-(Asp)2-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-(Asp)2-Ala-Asp-Lys + Ile-Val-Gly
Val-(Asp)3-Ala-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Ala-Lys + Ile-Val-Gly
Val-(Asp)3-Glu-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Glu-Lys + Ile-Val-Gly
Val-(Asp)4-Arg-Ile-Val-Gly + H2O
Val-(Asp)4-Arg + Ile-Val-Gly
Val-(Asp)4-Lys-Ile-Val-Gly + H2O
Val-(Asp)4-Lys + Ile-Val-Gly
Val-Ala-(Asp)2-Ala-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)2-Ala-Lys + Ile-Val-Gly
Val-Ala-(Asp)3-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)3-Lys + Ile-Val-Gly
Val-Ala-Asp-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-Ala-Asp-Ala-Asp-Lys + Ile-Val-Gly
Val-Asp-(Ala)2-Asp-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)2-Asp-Lys + Ile-Val-Gly
Val-Asp-(Ala)3-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)3-Lys + Ile-Val-Gly
Val-Asp-Ala-(Asp)2-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-(Asp)2-Lys + Ile-Val-Gly
Val-Asp-Ala-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-Asp-Ala-Lys + Ile-Val-Gly
Val-Asp-Asp-Asp-Asp-Lys-2-naphthylamide + H2O
?
-
-
-
-
?
VDYRFL-SA-PE + H2O
VDYRFL + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
VLDRWM-SA-PE + H2O
VLDRWM + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
VRDYRM-SA-PE + H2O
VRDYRM + SA-PE
-
peptide conjugated to fluorescent probe streptavidin-conjugated phycoerythrin
-
-
?
Z-Ala-Ala-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Ala-Ala-Arg
-
-
-
-
?
Z-Ala-Leu-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Ala-Leu-Arg
-
-
-
-
?
Z-Ala-Met-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Ala-Met-Arg
-
-
-
-
?
Z-Ala-Phe-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Ala-Phe-Arg
-
-
-
-
?
Z-Ala-Trp-Arg-p-nitroanilide + H2O
Z-Ala-Trp-Arg + 4-nitroaniline
-
-
-
-
?
Z-Ala-Tyr-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Ala-Tyr-Arg
-
-
-
-
?
Z-Gly-Pro-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Gly-Pro-Arg
-
-
-
-
?
Z-Lys-SBzl + H2O
?
-
-
-
?
Z-Phe-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Z-Phe-Arg
-
-
-
?
Z-Pro-Phe-Arg-p-nitroanilide + H2O
p-nitroaniline + Z-Pro-Phe-Arg
-
-
-
-
?
additional information
?
-
APFDDDDKIVGG + H2O
?
N-terminal dodecapeptides of human cationic trypsinogen
-
-
?
APFDDDDKIVGG + H2O
?
-
N-terminal dodecapeptides of human cationic trypsinogen
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
-
-
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
-
-
-
?
benzyl-L-Arg-2-naphthylamide + H2O
?
-
-
-
-
?
benzyl-L-Arg-2-naphthylamide + H2O
?
-
-
-
-
?
formyl-Ala-Phe-Arg-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
formyl-Ala-Phe-Arg-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
formyl-Ala-Phe-Lys-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
formyl-Ala-Phe-Lys-4-nitroanilide + H2O
?
-
a chromogenic peptide substrates
-
-
?
G5DKF(NO2)G + H2O
?
-
-
-
-
?
G5DKF(NO2)G + H2O
?
-
-
-
-
?
GD4KF(NO2)G + H2O
?
-
-
-
-
?
GD4KF(NO2)G + H2O
?
-
-
-
-
?
GDDDDK-2-naphthylamide + H2O
GDDDDK + 2-naphthylamine
-
-
-
-
?
GDDDDK-2-naphthylamide + H2O
GDDDDK + 2-naphthylamine
specific substrate
-
-
?
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-(L-Asp)4-L-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
-
-
-
?
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
-
-
?
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
-
GD4K-na
-
-
?
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
-
-
-
-
?
human cationic trypsinogen + H2O
?
-
-
-
-
?
human cationic trypsinogen + H2O
?
-
-
-
-
?
LTAEEKA + H2O
?
-
Hb 2-8
-
-
?
LTAEEKA + H2O
?
-
-
-
-
?
Nalpha-acetyltrypsinogen + H2O
Nalpha-acetylactivation peptides + trypsin
-
-
-
?
Nalpha-acetyltrypsinogen + H2O
Nalpha-acetylactivation peptides + trypsin
-
-
-
?
Nalpha-acetyltrypsinogen + H2O
Nalpha-acetylactivation peptides + trypsin
-
-
-
?
thiobenzyl benzyloxy-carbonyl-L-lysinate + H2O
3-carboxy-4-nitrophenoxide + ?
-
-
-
-
?
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
-
-
?
thioredoxin-human epidermal growth factor fusion protein + H2O
thioredoxin + human epidermal growth factor
-
Trx/hEGF
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
-
-
-
?
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
-
-
-
-
?
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
-
-
-
-
?
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
-
-
-
-
?
Trypsinogen + H2O
?
-
-
-
-
?
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
?
-
physiological activator of trypsinogen
-
-
?
Trypsinogen + H2O
?
-
-
-
-
?
Trypsinogen + H2O
?
-
enterokinase deficiency is a distinct clinical entity characterized by diarrhea, failure to thrive, hypoproteinemia, and edema. Acquired enterokinase deficiency may occur in some diffuse small bowel diseases. Steatorhea of cellac sprue may be due partly to the fact that deficiency of secretin and cholecystokinin may interfere with the action of enterokinase
-
-
?
Trypsinogen + H2O
?
-
physiological activator of trypsinogen
-
-
?
Trypsinogen + H2O
?
-
rapid activation of trypsinogen in pancreatic juice. The enzyme has a key permissive role in protein digestion and plays an essential part in the zymogen mechanism that protects the pancreas from self-destruction
-
-
?
Trypsinogen + H2O
?
-
initiation of digestive enzyme activation by converting trypsinogen into trypsin
-
-
?
Trypsinogen + H2O
?
-
-
-
-
?
Trypsinogen + H2O
?
-
physiological activator of trypsinogen
-
-
?
trypsinogen + H2O
trypsin
-
-
-
?
trypsinogen + H2O
trypsin
-
-
-
-
?
trypsinogen + H2O
trypsin
-
-
-
-
?
trypsinogen + H2O
trypsin
activation by by endoproteolytic cleavage
-
-
?
trypsinogen + H2O
trypsin
the enzyme cleaves after lysine residue if the Lys is preceded by four Asp and not followed by a Pro, and it shows high specificity of the target site. The light chain represents the catalytic enzyme subunit
-
-
?
trypsinogen + H2O
trypsin
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
specificity for the sequence (Asp)4-Lys-Ile
-
-
?
trypsinogen + H2O
trypsin + ?
-
cleaved exclusively at the Lys6-Ile7-peptide bond
-
-
?
trypsinogen + H2O
trypsin + ?
-
cleavage after the sequence DDDDK
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
human cationic trypsinogen is activated much more readily than bovine trypsinogen
-
-
?
trypsinogen + H2O
trypsin + ?
-
specificity for the sequence (Asp)4-Lys-Ile
-
-
?
trypsinogen + H2O
trypsin + ?
-
cleavage after the sequence DDDDK
-
-
?
trypsinogen + H2O
trypsin + ?
cleavage sequence DDDDK-X
-
-
?
trypsinogen + H2O
trypsin + ?
-
recognition sequence (Asp)4-Lys
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
recognition site DDDDK
-
-
?
trypsinogen + H2O
trypsin + ?
-
bovine trypsinogen
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
-
specificity for the sequence (Asp)4-Lys-Ile
-
-
?
trypsinogen + H2O
trypsin + ?
-
the specificity site of enterokinase recognizes in trypsinogen not merely the basic residue of the -Lys6-/-Ile7-bond, which is split during activation of the zymogen but also recognizes the sequence -Asp4-Lys, residues 2 to 6, which is present in all of the trypsinogens so far studied
-
-
?
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)2-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-(Asp)2-Lys + Ile-Val-Gly
107% 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)2-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-(Ala)2-Asp-Ala-Lys + Ile-Val-Gly
21.1% relative activity
-
-
?
Val-(Ala)3-Asp-Lys-Ile-Val-Gly + H2O
Val-(Ala)3-Asp-Lys + Ile-Val-Gly
75.6% relative activity
-
-
?
Val-(Ala)3-Asp-Lys-Ile-Val-Gly + H2O
Val-(Ala)3-Asp-Lys + Ile-Val-Gly
81.2% 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)2-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-(Asp)2-Ala-Asp-Lys + Ile-Val-Gly
93.1% 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-Ala-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Ala-Lys + Ile-Val-Gly
20.2% 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)3-Glu-Lys-Ile-Val-Gly + H2O
Val-(Asp)3-Glu-Lys + Ile-Val-Gly
64.9% relative activity
-
-
?
Val-(Asp)4-Arg-Ile-Val-Gly + H2O
Val-(Asp)4-Arg + Ile-Val-Gly
115.2% relative activity
-
-
?
Val-(Asp)4-Arg-Ile-Val-Gly + H2O
Val-(Asp)4-Arg + Ile-Val-Gly
128.2% relative activity
-
-
?
Val-(Asp)4-Lys-Ile-Val-Gly + H2O
Val-(Asp)4-Lys + Ile-Val-Gly
100% 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)2-Ala-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)2-Ala-Lys + Ile-Val-Gly
5.6% 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)3-Lys-Ile-Val-Gly + H2O
Val-Ala-(Asp)3-Lys + Ile-Val-Gly
123.7% 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-Ala-Asp-Ala-Asp-Lys-Ile-Val-Gly + H2O
Val-Ala-Asp-Ala-Asp-Lys + Ile-Val-Gly
35.8% 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)2-Asp-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)2-Asp-Lys + Ile-Val-Gly
95.8% 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)3-Lys-Ile-Val-Gly + H2O
Val-Asp-(Ala)3-Lys + Ile-Val-Gly
6.6% 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)2-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-(Asp)2-Lys + Ile-Val-Gly
119.7% 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
-
-
?
Val-Asp-Ala-Asp-Ala-Lys-Ile-Val-Gly + H2O
Val-Asp-Ala-Asp-Ala-Lys + Ile-Val-Gly
22.5% relative activity
-
-
?
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
?
-
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
?
-
-
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
-
-
?
additional information
?
-
-
enteropeptidase cleaves the C-terminal end of the substrate recognition sequence Asp-Asp-Asp-Asp-Lys, D4K. Usage of GD4K-conjugated 7-amino-4-methylcoumarin or GD4K-conjugated 2-naphthylamine as a fluorogenic substrates in the assay for enteropeptidase
-
-
?
additional information
?
-
-
high degree of cleavage specificity is exhibited by enteropeptidase
-
-
?
additional information
?
-
-
acidic residues at the P2, P3 and/or P4 position are especially favorable for maximal activity, but are not absolutely necessary
-
-
?
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
-
-
?