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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
-
-
?
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0.0021
A4-mutant trypsinogen
-
37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.13 nM human enteropeptidase
-
3.3
angiotensin II
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.0647 - 1.41
APFDDDDKIVGG
0.147
APFDDDDRIVGG
at 0.014-0.05 mM, holoenzyme
0.3
APFDDDGKIVGG
at 0.08-2 mM, holoenzyme
1.24
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
0.5 - 1.6
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
0.2 - 1.3
Boc-Glu(OBzl)-Ala-Arg-MCA
1.2 - 5.6
bovine trypsinogen
-
0.076 - 0.192
formyl-Ala-Phe-Arg-4-nitroanilide
0.167 - 0.28
formyl-Ala-Phe-Lys-4-nitroanilide
0.437
G5DKF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.5 - 0.6
GD4K 2-naphthylamide
-
pH 8.4, 35°C
0.025
GD4K 7-amido-4-methylcoumarin
-
pH 8.4, 35°C
0.2
GD4KNfa
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.00258 - 0.018
GD4R-4-nitroanilide
0.019 - 0.6
GDDDDK-2-naphthylamide
0.0179 - 0.276
GDDDDK-4-nitroanilide
0.75
Gly-(L-Asp)4-L-Lys-2-naphthylamide
pH and temperature not specified in the publication
1.12
Gly-Asp-ASp-Asp-Asp-2-naphthylamide
-
-
0.034 - 1.25
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
0.034 - 0.332
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide
0.108
Gly-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys-2-naphthylamide
at pH 8.0 and 37°C
0.2 - 0.525
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
0.0014 - 1.5
human cationic trypsinogen
-
4.2
LTAEEKA
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
4
MLTAEEKAA
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
596
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester +
-
37°C, pH 8.0
-
0.076
N-formyl-Ala-Phe-Arg-4-nitroanilide
-
-
0.167
N-formyl-Ala-Phe-Lys-4-nitroanilide
-
-
0.125
PrAD4KP26
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
-
1 - 10
Pro-Phe-Arg-4-methylcoumaryl-7-amide
0.2 - 1.5
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
0.12 - 0.14
thiobenzyl benzyloxy-carbonyl-L-lysinate
0.05 - 0.14
thiobenzyl benzyloxycarbonyl-L-lysinate
0.72
Val-(Ala)2-(Asp)2-Lys-Ile-Val-Gly
-
8.77
Val-(Ala)2-Asp-Ala-Lys-Ile-Val-Gly
-
1.51
Val-(Ala)3-Asp-Lys-Ile-Val-Gly
-
1.25
Val-(Asp)2-Ala-Asp-Lys-Ile-Val-Gly
-
8.31
Val-(Asp)3-Ala-Lys-Ile-Val-Gly
-
0.8
Val-(Asp)3-Glu-Lys-Ile-Val-Gly
-
0.45
Val-(Asp)4-Arg-Ile-Val-Gly
-
1.77
Val-(Asp)4-Lys-Ile-Val-Gly
-
1.01
Val-Ala-(Asp)3-Lys-Ile-Val-Gly
-
3.39
Val-Ala-Asp-Ala-Asp-Lys-Ile-Val-Gly
-
1.24
Val-Asp-(Ala)2-Asp-Lys-Ile-Val-Gly
-
21.11
Val-Asp-(Ala)3-Lys-Ile-Val-Gly
-
0.76
Val-Asp-Ala-(Asp)2-Lys-Ile-Val-Gly
-
5.57
Val-Asp-Ala-Asp-Ala-Lys-Ile-Val-Gly
-
1.6
WDDKG
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
2.1
WDDRG
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.356
Z-Ala-Ala-Arg-nitroanilide
-
-
0.234
Z-Ala-Leu-Arg-nitroanilide
-
-
0.42
Z-Ala-Met-Arg-nitroanilide
-
-
0.067
Z-Ala-Phe-Arg-nitroanilide
-
-
0.24
Z-Ala-Trp-Arg-nitroanilide
-
-
0.109
Z-Ala-Tyr-Arg-nitroanilide
-
-
0.091
Z-Gly-Pro-Arg-nitroanilide
-
-
0.1 - 0.4
Z-Phe-Arg-4-methylcoumaryl-7-amide
0.265
Z-Pro-Phe-Arg-nitroanilide
-
-
0.0647
APFDDDDKIVGG
-
EP light chain
0.353
APFDDDDKIVGG
at 0.03-0.08 mM, holoenzyme
0.907
APFDDDDKIVGG
at 0.08-2 mM, holoenzyme
1.06
APFDDDDKIVGG
at 0.1-3 mM, holoenzyme
1.41
APFDDDDKIVGG
at 0.03-0.08 mM, EP light chain
0.5
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
0.9
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
1.1
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
1.6
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
1.6
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
0.2
Boc-Glu(OBzl)-Ala-Arg-MCA
wild-type enzyme, 37°C, pH 7.4
1
Boc-Glu(OBzl)-Ala-Arg-MCA
E173A mutant, 37°C, pH 7.4
1
Boc-Glu(OBzl)-Ala-Arg-MCA
P193E mutant, 37°C, pH 7.4
1.2
Boc-Glu(OBzl)-Ala-Arg-MCA
K63R mutant, 37°C, pH 7.4
1.3
Boc-Glu(OBzl)-Ala-Arg-MCA
T105E mutant, 37°C, pH 7.4
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
-
0.076
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
0.192
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
0.167
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
0.28
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
0.16
GD4KF(NO2)G
-
50 mM Ca2+, pH 8.0, 37°C
0.16
GD4KF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.00258
GD4R-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.00629
GD4R-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.018
GD4R-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.019
GDDDDK-2-naphthylamide
-
phage-bound enteropeptidase catalytic subunit, in 25 mM Tris-HCl (pH 8.4), at 37°C
0.02
GDDDDK-2-naphthylamide
-
soluble enzyme, in 25 mM Tris-HCl (pH 8.4), at 37°C
0.3
GDDDDK-2-naphthylamide
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
0.4
GDDDDK-2-naphthylamide
mutant enzyme H24Q, at pH 8.3 and 30°C
0.5
GDDDDK-2-naphthylamide
mutant enzyme R213L, at pH 8.3 and 30°C
0.6
GDDDDK-2-naphthylamide
mutant enzyme E136Y, at pH 8.3 and 30°C
0.6
GDDDDK-2-naphthylamide
wild type enzyme, at pH 8.3 and 30°C
0.0179
GDDDDK-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.0298
GDDDDK-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.276
GDDDDK-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.034
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
0.123
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by fluorescence spectroscopy, pH not specified in the publication, at 37°C
0.141
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
0.143
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by impedance spectroscopy, pH not specified in the publication, at 37°C
0.16
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
pH 8.4, 37°C
0.17
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.0, 25°C
0.2
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
K63R mutant, 37°C, pH 7.4
0.22
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
-
0.3
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
E173A mutant, 37°C, pH 7.4
0.4
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
P193E mutant, 37°C, pH 7.4
0.4
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
T105E mutant, 37°C, pH 7.4
0.61
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
-
0.66
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K97A
0.7
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
37°C, pH 7.4
0.77
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K98A
1.25
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K96A
0.034
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide
-
in presence of 0.02 mM CaCl2
0.08
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide
-
in presence of 1mM EDTA
0.141
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide
-
in presence of 0.02 mM CaCl2
0.332
Gly-Asp-Asp-Asp-Asp-Lys-naphthylamide
-
in presence of 1mM EDTA
0.2
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
-
50 mM Ca2+, pH 8.0, 37°C
0.525
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
-
pH 8.0, 37°C
0.0014
human cationic trypsinogen
-
37 °C, 100 mM Tris-HCl pH 8.0, 1mM CaCl2, 120 nM soybean trypsin inhibitor, 0.13 nM human enteropeptidase
-
0.0072
human cationic trypsinogen
-
25 °C, 28 mM sodium succinate (pH 5.6), 10 mM CaCl2
-
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
Pro-Phe-Arg-4-methylcoumaryl-7-amide
E173A mutant, 37°C, pH 7.4
1
Pro-Phe-Arg-4-methylcoumaryl-7-amide
P193E mutant, 37°C, pH 7.4
1.1
Pro-Phe-Arg-4-methylcoumaryl-7-amide
K63R mutant, 37°C, pH 7.4
1.3
Pro-Phe-Arg-4-methylcoumaryl-7-amide
T105E mutant, 37°C, pH 7.4
10
Pro-Phe-Arg-4-methylcoumaryl-7-amide
37°C, pH 7.4
0.2
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
0.7
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
0.8
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
1.3
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
1.5
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
0.12
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
0.14
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
0.14
thiobenzyl benzyloxy-carbonyl-L-lysinate
pH 8.4, 37°C
0.05
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R99A
0.1
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme K96A
0.12
thiobenzyl benzyloxycarbonyl-L-lysinate
-
-
0.12
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R97A
0.14
thiobenzyl benzyloxycarbonyl-L-lysinate
-
-
0.14
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R98A
0.001
Trypsinogen
-
bovine guanidinated trypsinogen
0.0045
Trypsinogen
-
bovine trypsinogen
0.0056
Trypsinogen
-
pH 5.6
0.007
Trypsinogen
-
bovine trypsinogen
0.0072
Trypsinogen
-
human trypsinogen
0.07
Trypsinogen
-
bovine trypsinogen
0.165
Z-Lys-SBzl
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.172
Z-Lys-SBzl
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.19
Z-Lys-SBzl
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
0.1
Z-Phe-Arg-4-methylcoumaryl-7-amide
37°C, pH 7.4
0.1
Z-Phe-Arg-4-methylcoumaryl-7-amide
K63R mutant, 37°C, pH 7.4
0.1
Z-Phe-Arg-4-methylcoumaryl-7-amide
T105E mutant, 37°C, pH 7.4
0.2
Z-Phe-Arg-4-methylcoumaryl-7-amide
P193E mutant, 37°C, pH 7.4
0.4
Z-Phe-Arg-4-methylcoumaryl-7-amide
E173A mutant, 37°C, pH 7.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11.2
A4-mutant trypsinogen
-
37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.13 nM enteropeptidase
-
0.4
angiotensin II
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
28.4
benzoyl-Arg ethyl ester
-
-
262
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
0.36 - 1.81
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
4 - 6.9
bovine trypsinogen
-
23.5 - 26.3
formyl-Ala-Phe-Arg-4-nitroanilide
15.4 - 18.2
formyl-Ala-Phe-Lys-4-nitroanilide
24.9
GD4K 2-naphthylamide
-
pH 8.4, 35°C
64.8
GD4K 7-amido-4-methylcoumarin
-
pH 8.4, 35°C
42 - 49
GD4R-4-nitroanilide
17.8 - 115
GDDDDK-2-naphthylamide
122 - 148
GDDDDK-4-nitroanilide
520
Gly-Asp-ASp-Asp-Asp-2-naphthylamide
-
-
4.27 - 121
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
58.38
Gly-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys-2-naphthylamide
at pH 8.0 and 37°C
0.97 - 21.5
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
2.3 - 35.1
human cationic trypsinogen
-
25.17
MLTAEEKAA
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
111
N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester
-
37°C, pH 8.0
53
N2-benzoyl-L-Arg ethyl ester
-
-
2.62
PrAD4KP26
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
-
0.3 - 1.38
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
129 - 133
thiobenzyl benzyloxy-carbonyl-L-lysinate
108 - 129
thiobenzyl benzyloxycarbonyl-L-lysinate
8.1 - 12
tosyl-Arg methyl ester
12
Tosyl-Lys methyl ester
-
-
15.9
Val-(Ala)2-(Asp)2-Lys-Ile-Val-Gly
-
14.1
Val-(Ala)2-Asp-Ala-Lys-Ile-Val-Gly
-
17
Val-(Ala)3-Asp-Lys-Ile-Val-Gly
-
14.3
Val-(Asp)2-Ala-Asp-Lys-Ile-Val-Gly
-
14.6
Val-(Asp)3-Ala-Lys-Ile-Val-Gly
-
8
Val-(Asp)3-Glu-Lys-Ile-Val-Gly
-
13.6
Val-(Asp)4-Arg-Ile-Val-Gly
-
20
Val-(Asp)4-Lys-Ile-Val-Gly
-
17.8
Val-Ala-(Asp)3-Lys-Ile-Val-Gly
-
23
Val-Ala-Asp-Ala-Asp-Lys-Ile-Val-Gly
-
28.1
Val-Asp-(Ala)2-Asp-Lys-Ile-Val-Gly
-
9.1
Val-Asp-(Ala)3-Lys-Ile-Val-Gly
-
14.7
Val-Asp-Ala-(Asp)2-Lys-Ile-Val-Gly
-
10.3
Val-Asp-Ala-Asp-Ala-Lys-Ile-Val-Gly
-
0.54
WDDKG
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.68
WDDRG
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.36
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
0.56
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
0.64
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
1
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
1.81
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
4
bovine trypsinogen
-
21 °C, 50 mM sodium citrate pH 5.6, 1 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
-
23.5
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
26.3
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
15.4
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
18.2
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
0.97
G5DKF(NO2)G
-
50 mM Ca2+, pH 8.0, 37°C
0.97
G5DKF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
17.33
G5DKF(NO2)G
-
50 mM Ca2+, pH 8.0, 37°C
17.33
G5DKF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.99
GD4KF(NO2)G
-
50 mM Ca2+, pH 8.0, 37°C
0.99
GD4KF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
17.83
GD4KF(NO2)G
-
50 mM Ca2+, pH 8.0, 37°C
17.83
GD4KF(NO2)G
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.97
GD4KNfa
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
16.67
GD4KNfa
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
42
GD4R-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
45
GD4R-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
49
GD4R-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
17.8
GDDDDK-2-naphthylamide
mutant enzyme E136Y, at pH 8.3 and 30°C
26.2
GDDDDK-2-naphthylamide
mutant enzyme H24Q, at pH 8.3 and 30°C
27.9
GDDDDK-2-naphthylamide
wild type enzyme, at pH 8.3 and 30°C
28.75
GDDDDK-2-naphthylamide
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
33.02
GDDDDK-2-naphthylamide
mutant enzyme R213L, at pH 8.3 and 30°C
92
GDDDDK-2-naphthylamide
-
soluble enzyme, in 25 mM Tris-HCl (pH 8.4), at 37°C
115
GDDDDK-2-naphthylamide
-
phage-bound enteropeptidase catalytic subunit, in 25 mM Tris-HCl (pH 8.4), at 37°C
122
GDDDDK-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
135
GDDDDK-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
148
GDDDDK-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
4.27
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
-
17.1
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K96A
20.8
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.0, 25°C
24.1
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
-
25.5
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K97A
39.1
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
mutant enzyme K98A
49.3
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
98
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by fluorescence spectroscopy, pH not specified in the publication, at 37°C
115
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
pH 8.4, 37°C
118
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
121
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by impedance spectroscopy, pH not specified in the publication, at 37°C
0.97
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
-
50 mM Ca2+, pH 8.0, 37°C
16.67
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
-
50 mM Ca2+, pH 8.0, 37°C
21.5
glycyl-tetra-L-aspartyl-L-lysine beta-naphthylamide
-
pH 8.0, 37°C
2.3
human cationic trypsinogen
-
25°C, 28 mM sodium succinate (pH 5.6), 10 mM CaCl2
-
2.3
human cationic trypsinogen
-
0.00036 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm
-
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
-
35.1
human cationic trypsinogen
-
37 °C, 100 mM Tris-HCl pH 8.0, 1mM CaCl2, 120 nM soybean trypsin inhibitor, 0.13 nM enteropeptidase
-
0.07
LTAEEKA
-
pH 8.0, 37°C
0.49
LTAEEKA
-
in 0.1 M Tris-HCl buffer pH 8.0 at 37°C
0.3
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
0.34
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
0.53
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
0.6
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
1.38
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
129
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
133
thiobenzyl benzyloxy-carbonyl-L-lysinate
pH 8.4, 37°C
133
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
108
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme K96A
120
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R99A
128
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R97A
128
thiobenzyl benzyloxycarbonyl-L-lysinate
-
mutant enzyme R98A
129
thiobenzyl benzyloxycarbonyl-L-lysinate
-
-
8.1
tosyl-Arg methyl ester
-
-
12
tosyl-Arg methyl ester
-
-
0.005
Trypsinogen
-
bovine guanidinated trypsinogen
1.48
Trypsinogen
-
bovine trypsinogen
2.3
Trypsinogen
-
bovine trypsinogen
2.8
Trypsinogen
-
human trypsinogen
4.8
Trypsinogen
-
bovine trypsinogen
319
Z-Lys-SBzl
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
336
Z-Lys-SBzl
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
354
Z-Lys-SBzl
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.22 - 1.81
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
137 - 309
formyl-Ala-Phe-Arg-4-nitroanilide
55 - 109
formyl-Ala-Phe-Lys-4-nitroanilide
42
GD4K 2-naphthylamide
-
pH 8.4, 35°C
2623
GD4K 7-amido-4-methylcoumarin
-
pH 8.4, 35°C
2330 - 18900
GD4R-4-nitroanilide
29.6 - 6052
GDDDDK-2-naphthylamide
537 - 6830
GDDDDK-4-nitroanilide
347 - 3500
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
540.56
Gly-L-Asp-L-Asp-L-Asp-L-Asp-L-Lys-2-naphthylamide
at pH 8.0 and 37°C
0.23 - 2.29
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
950 - 969
thiobenzyl benzyloxy-carbonyl-L-lysinate
0.22
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
0.41
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
0.62
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
0.89
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
1.81
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
137
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
309
formyl-Ala-Phe-Arg-4-nitroanilide
-
pH 8.4, 25°C
55
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
109
formyl-Ala-Phe-Lys-4-nitroanilide
-
pH 8.4, 25°C
2330
GD4R-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
7200
GD4R-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
18900
GD4R-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
29.6
GDDDDK-2-naphthylamide
mutant enzyme E136Y, at pH 8.3 and 30°C
43.63
GDDDDK-2-naphthylamide
wild type enzyme, at pH 8.3 and 30°C
61.1
GDDDDK-2-naphthylamide
mutant enzyme R213L, at pH 8.3 and 30°C
63.1
GDDDDK-2-naphthylamide
mutant enzyme H24Q, at pH 8.3 and 30°C
99.5
GDDDDK-2-naphthylamide
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
4600
GDDDDK-2-naphthylamide
-
soluble enzyme, in 25 mM Tris-HCl (pH 8.4), at 37°C
6052
GDDDDK-2-naphthylamide
-
phage-bound enteropeptidase catalytic subunit, in 25 mM Tris-HCl (pH 8.4), at 37°C
537
GDDDDK-4-nitroanilide
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
4530
GDDDDK-4-nitroanilide
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
6830
GDDDDK-4-nitroanilide
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
347
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
805
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by fluorescence spectroscopy, pH not specified in the publication, at 37°C
846
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
value obtained by impedance spectroscopy, pH not specified in the publication, at 37°C
3500
Gly-Asp-Asp-Asp-Asp-Lys-2-naphthylamide
-
pH 8.4, 37°C
0.23
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y, at pH 8.3 and 30°C
0.23
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 8.3 and 30°C
0.67
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme R213L, at pH 8.3 and 30°C
0.85
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme H24Q, at pH 8.3 and 30°C
2.29
t-butyloxycarbonyl-E(benzyl ester)-Ala-Arg-7-amido-4-methylcoumarin
mutant enzyme E136Y/R213L, at pH 8.3 and 30°C
950
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
969
thiobenzyl benzyloxy-carbonyl-L-lysinate
-
pH 8.4, 25°C
1770
Z-Lys-SBzl
wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
1860
Z-Lys-SBzl
mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
2150
Z-Lys-SBzl
mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C
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Bos taurus
brenda
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Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli
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25
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2002
Bos taurus
brenda
Gasparian, M.E.; Ostapchenko, V.G.; Schulga, A.A.; Dolgikh, D.A.; Kirpichnikov, M.P.
Expression, purification, and characterization of human enteropeptidase catalytic subunit in Escherichia coli
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31
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brenda
Fang, L.; Sun, Q.M.; Hua, Z.C.
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36
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Bos taurus
brenda
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
brenda
Mikhailova, A.G.; Likhareva, V.V.; Prudchenko, I.A.; Rumsh, L.D.
Effect of calcium ions on enteropeptidase catalysis
Biochemistry (Moscow)
70
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Homo sapiens
brenda
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Prokaryotic expression of Chinese bovine enterokinase catalytic subunit
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117
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Bos taurus
brenda
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The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition
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280
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Bos taurus, Homo sapiens
brenda
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108
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Bos taurus
brenda
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Preparation of recombinant thioredoxin fused N-terminal proCNP: Analysis of enterokinase cleavage products reveals new enterokinase cleavage sites
Protein Expr. Purif.
41
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2005
Sus scrofa
brenda
Gasparian, M.E.; Ostapchenko, V.G.; Dolgikh, D.A.; Kirpichnikov, M.P.
Biochemical characterization of human enteropeptidase light chain
Biochemistry (Moscow)
71
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2006
Bos taurus, Homo sapiens
brenda
Liew, O.W.; Jenny Chong, P.C.; Lim, Y.Z.; Ang, C.X.; Amy Lau, Y.C.; Yandle, T.G.; Brennan, S.O.
An SRLLR motif downstream of the scissile bond enhances enterokinase cleavage efficiency
Biochimie
89
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31
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Bos taurus
brenda
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29
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Homo sapiens
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37
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Bos taurus
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Protease specificity determination by using cellular libraries of peptide substrates (CLiPS)
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103
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Homo sapiens
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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
brenda
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The ways of realization of high specificity and efficiency of enteropeptidase
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14
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Homo sapiens, Bos taurus (Q6B4R4), Bos taurus
brenda
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Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs
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72
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Bos taurus (P98072), Sus scrofa (P98074)
brenda
Shahravan, S.H.; Qu, X.; Chan, I.S.; Shin, J.A.
Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag
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59
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synthetic construct
brenda
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Application of immobilized bovine enterokinase in repetitive fusion protein cleavage for the production of mucin 1
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4
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Bos taurus
brenda
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Specificity of the medaka enteropeptidase serine protease and its usefulness as a biotechnological tool for fusion-protein cleavage
Proc. Natl. Acad. Sci. USA
104
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Oryzias latipes (A4UWM5), Oryzias latipes
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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
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2010
Bos taurus, Homo sapiens
brenda
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Design and efficient production of bovine enterokinase light chain with higher specificity in E. coli
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Bos taurus
brenda
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A fluorogenic method for measuring enteropeptidase activity: spectral shift in the emission of GD4K-conjugated 7-amino-4-methylcoumarin
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44
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Homo sapiens
brenda
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Homo sapiens (P98073), Homo sapiens
brenda
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Development of hybrid human interferon alfa-2 strain-producers and the use of enteropeptidase for production of N-terminal methionine-free interferons
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45
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2011
Sus scrofa
brenda
Simeonov, P.; Berger-Hoffmann, R.; Hoffmann, R.; Straeter, N.; Zuchner, T.
Surface supercharged human enteropeptidase light chain shows improved solubility and refolding yield
Protein Eng. Des. Sel.
24
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Homo sapiens (P98073), Homo sapiens
brenda
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Strategy for improvement of enteropeptidase efficiency in tag removal processes
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79
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Bos taurus, Homo sapiens
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Heterogeneous catalysis on the phage surface: Display of active human enteropeptidase
Biochimie
95
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2013
Homo sapiens
brenda
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
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30
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2012
Bos taurus, Homo sapiens
brenda
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Electrochemical determination of basic biochemical properties of enzyme enterokinase
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146
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2015
Homo sapiens (P98073)
-
brenda
Prohaska, T.A.; Wahlmueller, F.C.; Furtmueller, M.; Geiger, M.
Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase
PLoS ONE
7
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2012
Homo sapiens
brenda
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
brenda
Xu, J.; Hu, S.; Wang, X.; Zhao, Z.; Zhang, X.; Wang, H.; Zhang, D.; Guo, Y.
Structure basis for the unique specificity of medaka enteropeptidase light chain
Protein Cell
5
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2014
Oryzias latipes (A4UWM5), Oryzias latipes
brenda
Smith, E.T.; Johnson, D.A.
Human enteropeptidase light chain: bioengineering of recombinants and kinetic investigations of structure and function
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22
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2013
Homo sapiens (P98073), Homo sapiens
brenda
Simeonov, P.; Zahn, M.; Straeter, N.; Zuchner, T.
Crystal structure of a supercharged variant of the human enteropeptidase light chain
Proteins
80
1907-1910
2012
Homo sapiens (P98073), Homo sapiens
brenda
Melicherova, K.; Krahulec, J.; Safranek, M.; Liskova, V.; Hopkova, D.; Szeliova, D.; Turna, J.
Optimization of the fermentation and downstream processes for human enterokinase production in Pichia pastoris
Appl. Microbiol. Biotechnol.
101
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2017
Homo sapiens (P98073), Homo sapiens
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Niu, L.; Li, J.; Ji, X.; Yang, B.
Efficient expression and purification of recombinant human enteropeptidase light chain in Escherichia coli
Braz. Arch. Biol. Technol.
58
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2015
Homo sapiens (P98073)
-
brenda
Wang, J.H.; Tang, M.Z.; Yu, X.T.; Xu, C.M.; Yang, H.M.; Tang, J.B.
Site-specific, covalent immobilization of an engineered enterokinase onto magnetic nanoparticles through transglutaminase-catalyzed bioconjugation
Colloids Surf. B Biointerfaces
177
506-511
2019
Bos taurus
brenda
Hayashi, H.; Kubo, Y.; Izumida, M.; Takahashi, E.; Kido, H.; Sato, K.; Yamaya, M.; Nishimura, H.; Nakayama, K.; Matsuyama, T.
Enterokinase enhances influenza A virus infection by activating trypsinogen in human cell lines
Front. Cell. Infect. Microbiol.
8
91
2018
Homo sapiens (P98073), Homo sapiens
brenda