Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2 + H2O
?
-
fluorogenic synthetic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Ser-Ala-Phe-Leu-Ala-Phe-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide + H2O
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu + L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
due to the close proximity of a Mca-donor and a Dnp-acceptor, near complete intramolecular quenching effect is achieved in the substrate's intact state. After the proteolytic cleavage of the hydrophobic motif, both Mca and Dnp are further apart, resulting in bright fluorescence
substrate shows a 265fold difference in the net fluorescence signals between cathepsins E and D. This cathepsin E selectivity is established by having Leu-Pro residues at the scissile peptide bond
-
?
Acetyl-substance P + H2O
?
-
-
-
-
?
Acetyl-substance P(2-11) + H2O
?
-
-
-
-
?
Acetyl-substance P(3-11) + H2O
?
-
-
-
-
?
acidic fibroblast growth factor + H2O
?
-
-
-
-
?
Acidic fibroblast growth factor fragment 102-111 + H2O
His-Ala-Glu-Lys-His-Trp-Phe + Val-Gly-Leu
antigens presented by MHC class II molecules + H2O
?
-
-
-
?
Arg-modified substance P + H2O
?
-
-
-
-
?
Basic fibroblast growth factor fragment 106-120 + H2O
?
Bovine gamma-globulin + H2O
Hydrolyzed bovine gamma-globulin
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
casein + H2O
hydrolyzed casein
Cholecystokinin 8 + H2O
Asp-Tyr-Met-Gly-Trp + Met-Asp-Phe-NH2
Cytochrome c + H2O
Hydrolyzed cytochrome c
-
pH 5, at 2.5% (dimeric enzyme) or 2.3% (monomeric enzyme) the rate of hemoglobin hydrolysis
-
?
DED-[5-[(2-aminoethyl)amino]naphthalene-1-sulfonyl]-KPILFFRLGK-[4-(4-dimethylaminophenylazo)benzoic acid] + H2O
?
-
-
-
-
?
dynorphin A + H2O
hydrolyzed dynorphin A
Egg albumin + H2O
Hydrolyzed egg albumin
Eledoisin + H2O
Pyro-Glu-Pro-Ser-Lys-Asp-Ala-Phe + Ile-Gly-Leu-Met-NH2
glucagon + ATP + H2O
hydrolyzed glucagon + ?
-
is digested at pH 4.0 but not at pH 7.4
-
-
?
Hemoglobin + H2O
?
-
denatured
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
Human beta-endorphin + H2O
Hydrolyzed human beta-endorphin
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
Human endothelin precursor big ET-2 + H2O
Human endothelin precursor ET-2 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-3 + H2O
Huamn endothelin precursor ET-3 + respective C-terminal fragment
-
cleavage site: Trp-Ile
-
?
Human gamma-globulin + H2O
Hydrolyzed human gamma-globulin
-
pH 5, at 0.5% (dimeric enzyme) or 0.6% (monomeric enzyme) the rate of hemoglobin hydrolysis
-
?
Human renin substrate + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Val-Ile-His
Immunoglobulin + H2O
?
-
least active gastric protease for this substrate
-
-
?
Kassinin + H2O
Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe + Val-Gly-Leu-Met-NH2
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
Membrane proteins + H2O
?
-
-
-
-
?
MOCAc-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(DnP)-D-Arg-NH2 + H2O
?
-
-
-
?
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
-
-
-
?
MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(DNP)-D-Arg-NH2 + H2O
hydrolyzed MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(DNP)-D-Arg-NH2
-
-
-
-
?
N-succinyl-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-4-methyl-7-coumaryl-amide + H2O
?
-
-
-
?
Neurokinin A + H2O
His-Lys-Thr-Asp-Ser-Phe + Val-Gly-Leu-Met-NH2
neurotensin + H2O
hydrolyzed neurotensin
-
no cleavage at pH 7.4
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
Porcine renin substrate + H2O
Acetyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Leu-Val-Tyr-Ser
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Thr-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
Reduced and carboxymethylated bovine pancreatic ribonuclease A + H2O
Hydrolyzed bovine pancreatic RCm ribonuclease A
-
-
-
?
reduced carboxymethylated(RCm-)ribonuclease A + H2O
?
-
-
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
Substance P(1-9) + H2O
?
-
-
-
-
?
Substance P(2-11) + H2O
?
-
-
-
-
?
Substance P(3-11) + H2O
?
-
-
-
-
?
Substance P(4-11) + H2O
?
-
-
-
-
?
[His10]-substance P + H2O
?
-
-
-
-
?
[Tyr8]-substance P + H2O
?
-
-
-
-
?
additional information
?
-
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe + Phe-Arg-Leu-Lys(dinitrophenyl)-D-Arg-NH2
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
most sensitive and selective substrate for cathepsin E. This substrate might represent a useful tool for monitoring and accurately quantifying cathepsin E, even in crude enzyme preparations
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 + H2O
?
-
most sensitive and selective substrate for cathepsin E. This substrate might represent a useful tool for monitoring and accurately quantifying cathepsin E, even in crude enzyme preparations
-
-
?
Acidic fibroblast growth factor fragment 102-111 + H2O
His-Ala-Glu-Lys-His-Trp-Phe + Val-Gly-Leu
-
i.e. His-Ala-Glu-Lys-His-Trp-Phe-Val-Gly-Leu or acidic FGF 102-111
-
?
Acidic fibroblast growth factor fragment 102-111 + H2O
His-Ala-Glu-Lys-His-Trp-Phe + Val-Gly-Leu
-
i.e. His-Ala-Glu-Lys-His-Trp-Phe-Val-Gly-Leu or acidic FGF 102-111
-
?
Basic fibroblast growth factor fragment 106-120 + H2O
?
-
i.e. Tyr-Arg-Ser-Arg-Lys-Tyr-Ser-Ser-Trp-Tyr-Val-Ala-Leu-Lys-Arg or basic FGF 106-120, major cleavage site: Tyr-Val, minor site: Trp-Tyr
-
-
?
Basic fibroblast growth factor fragment 106-120 + H2O
?
-
i.e. Tyr-Arg-Ser-Arg-Lys-Tyr-Ser-Ser-Trp-Tyr-Val-Ala-Leu-Lys-Arg or basic FGF 106-120, major cleavage site: Tyr-Val, minor site: Trp-Tyr
-
-
?
big ET-1 + H2O
?
-
-
-
-
?
big ET-1 + H2O
?
-
-
-
-
?
Bovine gamma-globulin + H2O
Hydrolyzed bovine gamma-globulin
-
-
-
-
?
Bovine gamma-globulin + H2O
Hydrolyzed bovine gamma-globulin
-
pH 2.5, at 2.3% the rate of hemoglobin hydrolysis
-
?
Bovine gamma-globulin + H2O
Hydrolyzed bovine gamma-globulin
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
pH 5, at 3.6% (dimeric enzyme) or 4.1% (monomeric enzyme) the rate of hemoglobin hydrolysis
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
pH 2.5 at 14% the rate of hemoglobin hydrolysis
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
pH 5, at 9.1% (dimeric enzyme) or 8.9% (monomeric enzyme) the rate of hemoglobin hydrolysis
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
at pH 5.5
-
-
?
casein + H2O
hydrolyzed casein
-
at 2.3% the rate of hemoglobin hydrolysis
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
Cholecystokinin 8 + H2O
Asp-Tyr-Met-Gly-Trp + Met-Asp-Phe-NH2
-
i.e. Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2, cleavage site: Trp-Met
-
?
Cholecystokinin 8 + H2O
Asp-Tyr-Met-Gly-Trp + Met-Asp-Phe-NH2
-
i.e. Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2, cleavage site: Trp-Met
-
?
dynorphin A + H2O
hydrolyzed dynorphin A
-
cleavage site: Phe4-Leu5
-
?
dynorphin A + H2O
hydrolyzed dynorphin A
-
no cleavage at pH 7.4
-
-
?
dynorphin A + H2O
hydrolyzed dynorphin A
-
cleavage site: Phe4-Leu5
-
?
Egg albumin + H2O
Hydrolyzed egg albumin
-
pH 5, at 1% (dimeric enzyme) or 1.1% (monomeric enzyme) the rate of hemoglobin hydrolysis
-
?
Egg albumin + H2O
Hydrolyzed egg albumin
-
i.e. ovalbumin
-
?
Eledoisin + H2O
Pyro-Glu-Pro-Ser-Lys-Asp-Ala-Phe + Ile-Gly-Leu-Met-NH2
-
i.e. pyro-Glu-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2, cleavage site: Phe-Ile
-
?
Eledoisin + H2O
Pyro-Glu-Pro-Ser-Lys-Asp-Ala-Phe + Ile-Gly-Leu-Met-NH2
-
i.e. pyro-Glu-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2, cleavage site: Phe-Ile
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
preferred substrate
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
at pH 2 the two catalytically active subunits have the same activity vs. hemoglobin, but at pH 5 they have a slightly higher activity than the enzyme dimer
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
acid denatured form
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
bovine
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
preferred substrate
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
acid denatured form
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
bovine
-
-
?
Human beta-endorphin + H2O
Hydrolyzed human beta-endorphin
-
major cleavage site: Leu17-Phe18, minor site: Thr16-Leu17
-
?
Human beta-endorphin + H2O
Hydrolyzed human beta-endorphin
-
major cleavage site: Leu17-Phe18, minor site: Thr16-Leu17
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human endothelin precursor big ET-1 + H2O
Human endothelin precursor ET-1 + respective C-terminal fragment
-
cleavage site: Trp-Val
-
?
Human renin substrate + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Val-Ile-His
-
i.e. angiotensinogen fragment 1-13 or Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His, cleavage site: Leu-Val
-
?
Human renin substrate + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Val-Ile-His
-
i.e. angiotensinogen fragment 1-13 or Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His, cleavage site: Leu-Val
-
?
Kassinin + H2O
Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe + Val-Gly-Leu-Met-NH2
-
i.e. Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2, cleavage site: Phe-Val
-
?
Kassinin + H2O
Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe + Val-Gly-Leu-Met-NH2
-
i.e. Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2, cleavage site: Phe-Val
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide, less suitable peptide substrate than substance P or other tachykinins
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide, less suitable peptide substrate than substance P or other tachykinins
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
pH 7.4
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
no activation by ATP
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide, less suitable peptide substrate than substance P or other tachykinins
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide, less suitable peptide substrate than substance P or other tachykinins
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
i.e. RS-6
-
-
?
Neurokinin A + H2O
His-Lys-Thr-Asp-Ser-Phe + Val-Gly-Leu-Met-NH2
-
i.e. His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2, cleavage site: Phe-Val
-
?
Neurokinin A + H2O
His-Lys-Thr-Asp-Ser-Phe + Val-Gly-Leu-Met-NH2
-
i.e. His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2, cleavage site: Phe-Val
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
no activation by ATP
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage specificity changes significantly with pH, e.g. cleaves Glu13-Ala14 only at pH 7.4
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage sites
-
-
?
Porcine renin substrate + H2O
Acetyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Leu-Val-Tyr-Ser
-
i.e. angiotensinogen fragment 1-14 acetate salt or acetyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, cleavage site: Leu-Leu
-
?
Porcine renin substrate + H2O
Acetyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Leu-Val-Tyr-Ser
-
i.e. angiotensinogen fragment 1-14 acetate salt or acetyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, cleavage site: Leu-Leu
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
-
?
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Pro-Thr-Ile-Phe + (4-nitro)Phe-Arg-Leu
-
synthetic chromogenic peptide
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, best peptide substrate, cleavage site: Phe-Phe
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, best peptide substrate, cleavage site: Phe-Phe
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, best peptide substrate, cleavage site: Phe-Phe
-
?
Substance P + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe + Phe-Gly-Leu-Met-NH2
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, best peptide substrate, cleavage site: Phe-Phe
-
?
Tachykinins + H2O
?
-
-
-
-
?
Tachykinins + H2O
?
-
-
-
-
?
Tachykinins + H2O
?
-
-
-
-
?
Tachykinins + H2O
?
-
-
-
-
?
additional information
?
-
-
no hydrolysis of synthetic peptides corresponding to residues His16-His27 and His16-Ser38 in the big ET-1 sequence
-
-
?
additional information
?
-
-
milk-clotting activity is twice as high as that of pepsinogen and gastricin
-
-
?
additional information
?
-
-
degradation of protein antigens, crucial step in the initiation of a T-cell mediated immune response
-
?
additional information
?
-
-
cathepsin E has an important role in the class II MHC Ag processing pathway within dendritic cells
-
-
?
additional information
?
-
-
cathepsin E has an important role in the class II MHC Ag processing pathway within dendritic cells
-
-
?
additional information
?
-
-
cathepsin E is located in mast-cell secretory granules in complex with heparin proteoglycans, and has a role in processing of procarboxypeptidase A into active protease
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
1,2-epoxy-3-(p-nitrophenoxy)propane
alpha2-Macroglobulin
-
at pH 5.5, RNAse as substrate, at a molar ratio of enzyme/inhibitor of 0.5:1 to 2:1, above a ratio of 2:1 the excess enzyme is not inhibited, structural changes in alpha2-macroglobulin upon complex formation, no inhibition with oxidized insulin B-chain as substrate
-
Ascaris pepsin inhibitor
-
CCACCAACACAACTAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 4.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAACAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 31.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAACGAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 14.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCACCACCACAATAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCATCACTACAACAAAACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCATAGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 22.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCATAGTGCTCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 6.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCCCACCACAACCCTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 37.6% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
CCCCCACCACAACCCTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 33.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
DGCCIIINGGRPPTVFFRVKDYKHHDDK
-
Diazoacetyl-DL-norleucine methyl ester
GGSCSSCLGGRPPTIFFRLKDYKDDDDK
-
grassystatin A
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin B
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
grassystatin C
-
potent cathepsin E inhibitor, shows selectivity for cathepsin E over cathepsin D
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Phe-Arg-Glu
Protein inhibitor from Ascaris lumbricoides
-
SCIGIIDSGGRPPTIFFRAEGLQR
-
TCCATAAGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.2% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGAATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 26.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGATTCACTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGCTCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 24.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGGTCACTCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 18.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATAGGTATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 17.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 15.4% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGAGCTCACTCATCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 27.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGAGCTCACTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 11.5% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TCCCCGGTGCTCACTTATCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 19.3% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TGCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 40.8% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TTCATATGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 23.0% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
TTCATCGGGATCACTCCCTCCAC
-
inhibitory part, additionally the molecule has the conserved sequence GATCTCACTCCTTCGCAGTATTCGCGAGCC at its 5'-side, 29.7% inhibition (2 nM inhibitor /2 nM cathepsin E)
-
YCGGLLPLGGRPPTIFFRLKDYKGDDDK
-
(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
-
i.e. H-77, with reduced isostere as replacement of the-CO-NH- of the peptide bond
(D)-His-Pro-Phe-His-Leu-PSI(CH2-NH)-Leu-Val-Tyr
-
i.e. H-77, with reduced isostere as replacement of the-CO-NH- of the peptide bond
1,2-epoxy-3-(p-nitrophenoxy)propane
-
ir
1,2-epoxy-3-(p-nitrophenoxy)propane
-
ir
1,2-epoxy-3-(p-nitrophenoxy)propane
-
ir
1,2-epoxy-3-(p-nitrophenoxy)propane
-
ir
Ascaris pepsin inhibitor
-
-
-
Ascaris pepsin inhibitor
-
-
-
Ascaris pepsin inhibitor
-
-
-
Diazoacetyl-DL-norleucine methyl ester
-
ir
Diazoacetyl-DL-norleucine methyl ester
-
ir
Diazoacetyl-DL-norleucine methyl ester
-
ir
Diazoacetyl-DL-norleucine methyl ester
-
ir
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
-
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
i.e. L-363,564, hemoglobin as substrate
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
-
N-tert-Butoxycarbonyl-His-Pro-Phe-His-4-amino-3-hydroxy-6-methylheptanoic acid-Leu-Phe-NH2
-
-
N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
-
i.e. H-261, with reduced isostere as replacement of the -CO-NH- of the peptide bond
N-tert-Butoxycarbonyl-His-Pro-Phe-His-Leu-PSI(CHOH-CH2)-Val-Ile-His
-
i.e. H-261, with reduced isostere as replacement of the -CO-NH- of the peptide bond
PepA-penetratin
-
efficient cell-permeable aspartic protease inhibitor
-
PepA-penetratin
-
efficient cell-permeable aspartic protease inhibitor
-
pepstatin
-
-
pepstatin
-
as substrate, incubation at pH 7.4 restores; at pH 3 and 5.5, not at pH 7.4
pepstatin
-
as substrate, incubation at pH 7.4 restores; at pH 3 and 5.5, not at pH 7.4; oxidized insulin B-chain
pepstatin
-
also inhibits conversion of procathepsin E to cathepsin E
pepstatin A
-
-
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
-
i.e. H-297, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
-
hemoglobin as substrate
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
-
-
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Nle-Arg-Leu
-
i.e. H-297, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Phe-Arg-Glu
-
i.e. H-256, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Pro-Thr-Glu-Phe-PSI(CH2-NH)-Phe-Arg-Glu
-
i.e. H-256, with reduced isostere as replacement of the -CO-NH- of the peptide bond
Protein inhibitor from Ascaris lumbricoides
-
MW 17000
-
Protein inhibitor from Ascaris lumbricoides
-
MW 17000
-
Protein inhibitor from Ascaris lumbricoides
-
MW 17000
-
Protein inhibitor from Ascaris lumbricoides
-
MW 17000
-
Tripeptide analogs
-
-
-
additional information
-
iodoaceteic acid, EDTA, phosphoramidon on proteolysis of membrane proteins; no (or little) inhibition
-
additional information
-
2-mercaptoethanol, Mg2+ or vanadate
-
additional information
-
1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4); inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
-
additional information
-
1,10-phenanthroline, diprotin A, antipain, amastatin, L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64, at pH 7.4); inhibition by PMSF, diisopropyl fluorophosphate, leupeptin
-
additional information
-
the computed three-dimensional structure of cathepsin-E and the relevant findings might provide useful insights for designing inhibitors with the desired selectivity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.55 - 11.9
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
39.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
32.2
(7-methoxycoumarin-4-yl)acetyl-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
0.52 - 20.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
1.68
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Ser-Ala-Phe-Leu-Ala-Phe-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
322.5
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide
-
pH 4.0, 27°C
26
Acetyl-substance P
-
pH 5
19
Acetyl-substance P(2-11)
-
pH 5
58
Acetyl-substance P(3-11)
-
pH 5
18
acidic fibroblast growth factor
-
pH 5
-
64
Arg-modified substance P
-
pH 5
-
135
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
pH 3.1
26 - 170
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
360
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2
-
25°C, pH 4.0
13
Porcine renin substrate
-
pH 5
5 - 132
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
27
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
pH 3.1
22
Substance P(2-11)
-
pH 5
70
Substance P(3-11)
-
pH 5
0.74
Substance P(4-11)
-
pH 5
23
[His10]-substance P
-
pH 5
40
[Tyr8]-substance P
-
pH 5
additional information
additional information
-
1.55
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant D98E
6.4
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, mutant T284S
11.9
(7-methoxycoumarin-4-yl)-acetyl-Gly-Lys-Pro-Ile-Ile-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-D-Arg-NH2
-
pH 3.5, 40°C, wild-type
0.52
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
13.58
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, wild-type cathepsin E
18.8
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, erythrocyte cathepsin E
19.4
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, erythrocyte cathepsin E
20.1
(7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2
-
40°C, pH 4.0, gastric cathepsin E
0.13
big ET-1
-
-
26
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
without ATP, pH 5.4
54
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
without ATP, pH 5
56
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 5.8
72
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 5.4
76
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
without ATP, pH 4.5
77
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 4.5 and pH 5
82
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
Cys4-Ala mutant cathepsin E, pH 3.1
115
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
-
170
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
pH 3.5
5
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
value below, with ATP, pH 7
11
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 6.6 and without ATP, pH 5
16
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 6.2
31
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 5
36
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
without ATP, pH 4.5
39
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 4.5 and pH 5.4
40
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
-
40
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
with ATP, pH 5.8
40
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
[Tyr8]-substance P, pH 5
47
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
-
47
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
without ATP, pH 5
47
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
substance P
70
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
Cys4-Ala mutant cathepsin E, pH 3.1
75
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
pH 3.5
132
Pro-Pro-Thr-Ile-Phe-(4-nitro)Phe-Arg-Leu
-
-
additional information
additional information
-
pH-dependence of kinetic constants
-
additional information
additional information
-
pH-dependence of kinetic constants
-
additional information
additional information
-
pH-dependence of kinetic constants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Lapresle, C.; Puizdar, V.; Porchon-Bertolotto, C.; Joukoff, E.; Turk, V.
Structural differences between rabbit cathepsin E and cathepsin D
Biol. Chem. Hoppe-Seyler
367
523-526
1986
Oryctolagus cuniculus
brenda
Yamamoto, K.; Ueno, E.; Uemura, H.; Kato, Y.
Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E
Biochem. Biophys. Res. Commun.
148
267-272
1987
Homo sapiens, Rattus norvegicus
brenda
Yonezawa, S.; Fujii, K.; Maejima, Y.; Tamoto, K.; Mori, Y.; Muto, N.
Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form
Arch. Biochem. Biophys.
267
176-183
1988
Rattus norvegicus
brenda
Jupp, R.A.; Richards, A.D.; Kay, J.; Dunn, B.M.; Wyckoff, J.B.; Samloff, M.; Yamamoto, K.
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E
Biochem. J.
254
895-898
1988
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Wiederanders, B.; Schaper, S.; Kirschke, H.
Isolation and some properties of a cathepsin E type proteinase from rat spleen
Biomed. Biochim. Acta
48
23-32
1989
Rattus norvegicus
brenda
Azuma, T.; Pals, G.; Mohandas, T.K.; Couvreur, J.M.; Taggert, R.T.
Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases
J. Biol. Chem.
264
16748-16753
1989
Homo sapiens
brenda
Ueno, E.; Sakai, H.; Kato, Y.; Yamamoto, K.
Activation mechanism of erythrocyte cathepsin E. evidence for the occurrence of the membrane-associated active enzyme
J. Biochem.
105
878-882
1989
Homo sapiens
brenda
Thomas, D.J.; Richards, A.D.; Jupp, R.A.; Ueno, E.; Yamamoto, K.; Samloff, I.M.; Dunn, B.M.; Kay, J.
Stabilisation of cathepsin E by ATP
FEBS Lett.
243
145-148
1989
Homo sapiens
brenda
Yonezawa, S.; Takahashi, T.; Ichinose, M.; Miki, K.; Tanaka, J.; Gasa, S.
Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme
Biochem. Biophys. Res. Commun.
166
1032-1038
1990
Rattus norvegicus
brenda
Athauda, S.B.P.; Matsuzaki, O.; Kageyama, T.; Takahashi, K.
Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E
Biochem. Biophys. Res. Commun.
168
878-885
1990
Homo sapiens
brenda
Athauda, S.B.P.; Takahashi, T.; Inoue, H.; Ichinose, M.; Takahashi, K.
Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin
FEBS Lett.
292
53-56
1991
Homo sapiens
brenda
Athauda, S.B.P.; Takahashi, T.; Kageyama, T.; Takahashi, K.
Autocatalytic processing of procathepsin E to cathepsin E and their structural differences
Biochem. Biophys. Res. Commun.
175
152-158
1991
Homo sapiens
brenda
Kageyama, T.; Ichinose, M.; Tsukada, S.; Miki, K.; Kurokawa, K.; Koiwai, O.; Tanji, M.; Yakabe, E.; Athauda, S.B.P.; Takahashi, K.
Gastric procathepsin E and progastricsin from guinea pig. Purification, molecular cloning of cDNAs, and characterization of enzymatic properties, with special reference to procathepsin E
J. Biol. Chem.
267
16450-16459
1992
Cavia porcellus
brenda
Robinson, P.S.; Lees, W.E.; Kay, J.; Cook, N.D.
Kinetic parameters for the generation of endothelins-1,-2 and -3 by human cathepsin E
Biochem. J.
284
407-409
1992
Homo sapiens
brenda
Kageyama, T.; Ichinose, M.; Miki, K.; Moriyama, A.; Yonezawa, S.; Tanji, M.; Athauda, S.B.P.; Takahashi, K.
Isolation, characterization, and structure of procathepsin E and cathepsin E from the gastric mucosa of guinea pig
Adv. Exp. Med. Biol.
362
211-221
1995
Cavia porcellus
brenda
Kiselev, A.F.; Gul'nik, S.V.; Tarasova, N.I.
Human stomach cathepsin E action on human immunoglobulins
Adv. Exp. Med. Biol.
306
369-371
1991
Homo sapiens
brenda
Takeda-Ezaki, M.; Yamamoto, K.
Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes
Arch. Biochem. Biophys.
304
352-358
1993
Homo sapiens
brenda
Athauda, S.B.P.; Arakawa, H.; Nishigai, M.; Takahashi, T.; Takahashi, K.
Inhibition of cathepsin E by alpha 2-macroglobulin and the resulting structural changes in the inhibitor
J. Biochem.
113
526-530
1993
Homo sapiens
brenda
Tsukuba, T.; Hori, H.; Azuma, T.; Takahashi, T.; Taggart, R.T.; Akamine, A.; Ezaki, M.; Nakanishi, H.; Sakai, H.; Yamamoto, K.
Isolation and characterization of recombinant human cathepsin E expressed in Chinese hamster ovary cells
J. Biol. Chem.
268
7276-7282
1993
Homo sapiens
brenda
Hill, J.; Montgomery, D.S.; Kay, J.
Human cathepsin E produced in E. coli
FEBS Lett.
326
101-104
1993
Homo sapiens
brenda
Inokuchi, T.; Kobayashi, K.; Horiuchi, S.
Purification and characterization of cathepsin E type acid proteinase from gastric mucosa of bullfrog, Rana catesbeiana
J. Biochem.
115
76-81
1994
Lithobates catesbeianus
brenda
Kageyama, T.
Procathepsin E and cathepsin E
Methods Enzymol.
248
120-136
1995
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Iida, H.; Matsuba, T.; Yamada, M.; Azuma, T.; Suzuki, H.; Yamamoto, K.; Hori, H.
Purification and characterization of recombinant human cathepsin E
Adv. Exp. Med. Biol.
362
325-330
1995
Homo sapiens
brenda
Athauda, S.B.P.; Kageyama, T.; Takahashi, T.; Inoue, H.; Ichinose, M.; Ukai, M.; Takahashi, K.
Isolation and characterization of human gastric procathepsin E and cathepsin E
Adv. Exp. Med. Biol.
362
201-210
1995
Homo sapiens
brenda
Tsukuba, T.; Masayuki, Y.; Hori, H.; Azuma, T.; Yamamoto, K.
Comparison of biochemical properties of natural and recombinant cathepsin E
Adv. Exp. Med. Biol.
362
331-334
1995
Homo sapiens
brenda
Fowler, S.D.; Kay, J.; Dunn, B.M.; Tatnell, P.J.
Monomeric human cathepsin E
FEBS Lett.
366
72-74
1995
Homo sapiens
brenda
Okamoto, K.; Yu, H.; Misumi, Y.; Ikehara, Y.; Yamamoto, K.
Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E
Arch. Biochem. Biophys.
322
103-111
1995
Rattus norvegicus
brenda
Kageyama, T.; Takahashi, K.
A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization
J. Biochem.
87
725-735
1980
Homo sapiens
brenda
Arnold, D.; Keilholz, W.; Schild, H.; Dumrese, T.; Stevanovic, S.; Rammensee, H.G.
Substrate specificity of cathepsins D and E determined by N-terminal and C-terminal sequencing of peptide pools
Eur. J. Biochem.
249
171-179
1997
Homo sapiens
brenda
Liu, J.; Tsukuba, T.; Okamoto, K.; Ohishi, M.; Yamamoto, K.
Mutational analysis of residues in two consensus motifs in the active sites of cathepsin E
J. Biochem.
132
493-499
2002
Rattus norvegicus
brenda
Athauda, S.B.; Takahashi, K.
Distinct cleavage specificity of human cathepsin E at neutral pH with special preference for Arg-Arg bonds
Protein Pept. Lett.
9
15-22
2002
Homo sapiens
brenda
Chou, K.C.
Modeling the tertiary structure of human cathepsin-E
Biochem. Biophys. Res. Commun.
331
56-60
2005
Homo sapiens
brenda
Yasuda, Y.; Kohmura, K.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
A new selective substrate for cathepsin E based on the cleavage site sequence of alpha2-macroglobulin
Biol. Chem.
386
299-305
2005
Homo sapiens, Rattus norvegicus
brenda
Tsukuba, T.; Ikeda, S.; Okamoto, K.; Yasuda, Y.; Sakai, E.; Kadowaki, T.; Sakai, H.; Yamamoto, K.
Characterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells
FEBS J.
273
219-229
2006
Rattus norvegicus
brenda
Yasuda, Y.; Tsukuba, T.; Okamoto, K.; Kadowaki, T.; Yamamoto, K.
The role of the cathepsin E propeptide in correct folding, maturation and sorting to the endosome
J. Biochem.
138
621-630
2005
Rattus norvegicus
brenda
Henningsson, F.; Yamamoto, K.; Saftig, P.; Reinheckel, T.; Peters, C.; Knight, S.D.; Pejler, G.
A role for cathepsin E in the processing of mast-cell carboxypeptidase A
J. Cell Sci.
118
2035-2042
2005
Mus musculus
brenda
Chain, B.M.; Free, P.; Medd, P.; Swetman, C.; Tabor, A.B.; Terrazzini, N.
The expression and function of cathepsin E in dendritic cells
J. Immunol.
174
1791-1800
2005
Homo sapiens, Mus musculus
brenda
Ostermann, N.; Gerhartz, B.; Worpenberg, S.; Trappe, J.; Eder, J.
Crystal structure of an activation intermediate of cathepsin E
J. Mol. Biol.
342
889-899
2004
Homo sapiens
brenda
Cappiello, M.G.; Wu, Z.; Scott, B.B.; McGeehan, G.M.; Harrison, R.K.
Purification and characterization of recombinant human cathepsin E expressed in human kidney cell line 293
Protein Expr. Purif.
37
53-60
2004
Homo sapiens
brenda
Busquets, L.; Guillen, H.; DeFord, M.E.; Suckow, M.A.; Navari, R.M.; Castellino, F.J.; Prorok, M.
Cathepsin E is a specific marker of dysplasia in APC mouse intestine
Tumour Biol.
27
36-42
2006
Mus musculus
brenda
Page, J.L.; Strom, S.C.; Omiecinski, C.J.
Regulation of the human cathepsin E gene by the constitutive androstane receptor
Arch. Biochem. Biophys.
467
132-138
2007
Homo sapiens
brenda
Zaidi, N.; Herrmann, T.; Voelter, W.; Kalbacher, H.
Recombinant cathepsin E has no proteolytic activity at neutral pH
Biochem. Biophys. Res. Commun.
360
51-55
2007
Mus musculus
brenda
Zaidi, N.; Kalbacher, H.
Cathepsin E: a mini review
Biochem. Biophys. Res. Commun.
367
517-522
2008
Homo sapiens, Mus musculus
brenda
Shin, M.; Kadowaki, T.; Iwata, J.; Kawakubo, T.; Yamaguchi, N.; Takii, R.; Tsukuba, T.; Yamamoto, K.
Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
Biol. Chem.
388
1173-1181
2007
Homo sapiens
brenda
Kawakubo, T.; Okamoto, K.; Iwata, J.; Shin, M.; Okamoto, Y.; Yasukochi, A.; Nakayama, K.I.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
Cathepsin E prevents tumor growth and metastasis by catalyzing the proteolytic release of soluble TRAIL from tumor cell surface
Cancer Res.
67
10869-10878
2007
Mus musculus
brenda
Zaidi, N.; Herrmann, T.; Baechle, D.; Schleicher, S.; Gogel, J.; Driessen, C.; Voelter, W.; Kalbacher, H.
A new approach for distinguishing cathepsin E and D activity in antigen-processing organelles
FEBS J.
274
3138-3149
2007
Homo sapiens
brenda
Kakehashi, H.; Nishioku, T.; Tsukuba, T.; Kadowaki, T.; Nakamura, S.; Yamamoto, K.
Differential regulation of the nature and functions of dendritic cells and macrophages by cathepsin E
J. Immunol.
179
5728-5737
2007
Mus musculus
brenda
Burster, T.; Reich, M.; Zaidi, N.; Voelter, W.; Boehm, B.O.; Kalbacher, H.
Cathepsin E regulates the presentation of tetanus toxin C-fragment in PMA activated primary human B cells
Biochem. Biophys. Res. Commun.
377
1299-1303
2008
Homo sapiens (P14091), Homo sapiens
brenda
da Rocha Fragoso, R.; Lourenco, I.T.; Batista, J.A.; Oliveira-Neto, O.B.; Silva, M.C.; Rocha, T.L.; Coutinho, M.V.; Grossi-de-Sa, M.F.
Meloidogyne incognita: molecular cloning and characterization of a cDNA encoding a cathepsin D-like aspartic proteinase
Exp. Parasitol.
121
115-123
2009
Meloidogyne incognita (Q1A2Z2), Meloidogyne incognita
brenda
Tsukuba, T.; Yanagawa, M.; Okamoto, K.; Okamoto, Y.; Yasuda, Y.; Nakayama, K.I.; Kadowaki, T.; Yamamoto, K.
Impaired chemotaxis and cell adhesion due to decrease in several cell-surface receptors in cathepsin E-deficient macrophages
J. Biochem.
145
565-573
2009
Mus musculus (P70269)
brenda
Kitamura, K.; Yoshida, C.; Kinoshita, Y.; Kadowaki, T.; Takahashi, Y.; Tayama, T.; Kawakubo, T.; Naimuddin, M.; Salimullah, M.; Nemoto, N.; Hanada, K.; Husimi, Y.; Yamamoto, K.; Nishigaki, K.
Development of systemic in vitro evolution and its application to generation of peptide-aptamer-based inhibitors of cathepsin E
J. Mol. Biol.
387
1186-1198
2009
Rattus norvegicus (P16228)
brenda
Shigematsu, N.; Fukuda, T.; Yamamoto, T.; Nishioku, T.; Yamaguchi, T.; Himeno, M.; Nakayama, K.I.; Tsukuba, T.; Kadowaki, T.; Okamoto, K.; Higuchi, S.; Yamamoto, K.
Association of cathepsin E deficiency with the increased territorial aggressive response of mice
J. Neurochem.
105
1394-1404
2008
Mus musculus
brenda
Yoshida, C.; Kuniwake, A.; Naimuddin, M.; Nishigaki, K.
Molecular design guided by a local map of sequence space: DNA aptamers that inhibit cathepsin E
Oligonucleotides
18
1-8
2008
Rattus norvegicus
brenda
Caruso, M.; Moore, J.; Goodall, G.J.; Thomas, M.; Phillis, S.; Tyskin, A.; Cheetham, G.; Lerda, N.; Takahashi, H.; Ruszkiewicz, A.
Over-expression of cathepsin E and trefoil factor 1 in sessile serrated adenomas of the colorectum identified by gene expression analysis
Virchows Arch.
454
291-302
2009
Homo sapiens (P14091)
brenda
Yasukochi, A.; Kawakubo, T.; Nakamura, S.; Yamamoto, K.
Cathepsin E enhances anticancer activity of doxorubicin on human prostate cancer cells showing resistance to TRAIL-mediated apoptosis
Biol. Chem.
391
947-958
2010
Homo sapiens
brenda
Kwan, J.C.; Eksioglu, E.A.; Liu, C.; Paul, V.J.; Luesch, H.
Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation
J. Med. Chem.
52
5732-5747
2009
Homo sapiens
brenda
Abd-Elgaliel, W.R.; Tung, C.H.
Selective detection of Cathepsin E proteolytic activity
Biochim. Biophys. Acta
1800
1002-1008
2010
Homo sapiens
brenda
Cruz-Monserrate, Z.; Abd-Elgaliel, W.; Grote, T.; Deng, D.; Ji, B.; Arumugam, T.; Wang, H.; Tung, C.; Logsdon, C.
Detection of pancreatic cancer tumours and precursor lesions by cathepsin E activity in mouse models
Gut
61
1315-1322
2012
Homo sapiens
brenda
Biyani, M.; Futakami, M.; Kitamura, K.; Kawakubo, T.; Suzuki, M.; Yamamoto, K.; Nishigaki, K.
In vitro selection of cathepsin E-activity-enhancing peptide aptamers at neutral pH
Int. J. Pept.
2011
834525
2011
Rattus norvegicus
brenda
Harada, Y.; Zhang, J.; Imari, K.; Yamasaki, R.; Ni, J.; Wu, Z.; Yamamoto, K.; Kira, J.I.; Nakanishi, H.; Hayashi, Y.
Cathepsin E in neutrophils contributes to the generation of neuropathic pain in experimental autoimmune encephalomyelitis
Pain
160
2050-2062
2019
Mus musculus
brenda
Hiramatsu, S.; Watanabe, K.S.; Zeggar, S.; Asano, Y.; Miyawaki, Y.; Yamamura, Y.; Katsuyama, E.; Katsuyama, T.; Watanabe, H.; Takano-Narazaki, M.; Matsumoto, Y.; Kawabata, T.; Sada, K.E.; Wada, J.
Regulation of cathepsin E gene expression by the transcription factor Kaiso in MRL/lpr mice derived CD4+ T cells
Sci. Rep.
9
3054
2019
Mus musculus
brenda