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Abz-LSFMAIQ-EDDnp + H2O
Abz-LSF + MAIQ-EDDnp
-
-
-
-
?
Ac-Ala-Ala-(4-nitro)Phe-Ala-Ala + H2O
?
-
-
-
-
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala + H2O
Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
KAIEF p-nitrophenylalanine-RL + H2O
KAIEF + p-nitrophenylalanine-RL
-
-
-
?
KLIEF p-nitrophenylalanine-RL + H2O
KLIEF + p-nitrophenylalanine-RL
-
-
-
?
KPAEF p-nitrophenylalanine-RL + H2O
KPAEF + p-nitrophenylalanine-RL
-
-
-
?
KPALF p-nitrophenylalanine-RL + H2O
KPALF + p-nitrophenylalanine-RL
-
-
-
?
KPDEF p-nitrophenylalanine-RL + H2O
KPDEF + p-nitrophenylalanine-RL
-
-
-
?
KPIAF p-nitrophenylalanine-RL + H2O
KPIAF + p-nitrophenylalanine-RL
-
-
-
?
KPIDF p-nitrophenylalanine-RL + H2O
KPIDF + p-nitrophenylalanine-RL
-
-
-
?
KPIEF p-nitrophenylalanine-RL + H2O
KPIEF + p-nitrophenylalanine-RL
-
-
-
?
KPILF p-nitrophenylalanine-RL + H2O
KPILF + p-nitrophenylalanine-RL
-
-
-
?
KPISF p-nitrophenylalanine-RL + H2O
KPISF + p-nitrophenylalanine-RL
-
-
-
?
KPLEF p-nitrophenylalanine-RL + H2O
KPLEF + p-nitrophenylalanine-RL
-
-
-
?
KPREF p-nitrophenylalanine-RL + H2O
KPREF + p-nitrophenylalanine-RL
-
-
-
?
KPRRPYILKRGSYYY + H2O
KPRRPYIL + KRGSYYY
-
synthetic neurotensin-like peptide, cleavage site specificity
-
-
?
KPSEF p-nitrophenylalanine-RL + H2O
KPSEF + p-nitrophenylalanine-RL
-
-
-
?
KPVSY(4-NO2-F)RL + H2O
?
-
-
-
-
?
KPVSY(NO2)FRL + H2O
?
-
-
-
?
KSIEF p-nitrophenylalanine-RL + H2O
KSIEF + p-nitrophenylalanine-RL
-
-
-
?
L-Orn-L-Leu-D-Phe-L-Pro-L-Val-OH + H2O
L-Orn + L-Val + L-Leu-D-Phe-L-Pro-OH
-
open chain of gramicidin S that is prepared by the treatment of gramicidin S with Bacillus subtilis alkaline protease
-
?
Lys-Pro-Ala-Lys-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ala-Lys-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
milk powder + H2O
?
-
-
-
-
?
Na-Polyglutamate + H2O
Glu + Glu-Glu + unknown compound
-
-
-
?
oxidized insulin B chain + H2O
?
-
-
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
Polylysine-HCl + H2O
Lys-Lys + Lys-Lys-Lys + higher oligolysine
-
-
-
?
Z-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Z-Ala-Ala-Lys + Ala-Ala-Ala
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
-
i.e. insulin B chain, cleavage site specificity
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
L-Phe + VNQH + LCGSH + L-Leu + L-Val + L-Glu + L-Ala + L-Leu + L-Tyr + LVCG + ERG + L-Phe + L-Phe + YTPKA
-
i.e. insulin B chain, cleavage site specificity
-
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
primarily the Leu15-Tyr16 bond and the Tyr16-Leu17 bond is hydrolyzed, additional cleavage of the bonds Ala14-Leu15 and Phe24-Phe25
-
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
splits at twelve sites, preferentially Leu-Val, Tyr-Leu and Phe-Phe
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
bovine insulin
-
?
Oxidized insulin B-chain + H2O
Proteolytically cleaved oxidized insulin B-chain
-
-
-
?
Peptides + H2O
?
-
in these examples the term -+- depicts the points of cleavage: Lys-+-Tyr-+-Glu-OH, benzyloxycarbonyl-Glu-+-Tyr-OH, benzyloxycarbonyl-Phe-+-Tyr-OH, benzyloxycarbonyl-Leu-+-Tyr-OH, Gly-Glu-+-Tyr-OH, benzyloxycarbonyl-Glu-+-Tyr-OH, Leu-Tyr-OH, Glu-Tyr-OH, benzyloxycarbonyl-Gly-+-Phe-OH, benzyloxycarbonyl-Glu-+-Phe-OH, Leu-Gly-+-Phe-OHGlu-Gly-+-Phe-OH, Leu-Phe-OH
-
-
?
Peptides + H2O
?
-
obtained from oxidized B-chain of insulin
-
-
?
Peptides + H2O
?
-
specificity towards the tetradecapeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
-
-
?
Peptides + H2O
?
-
role of the Asp77 in facilitating the cleavage of oligopeptide substrates with lysine in P1
-
-
?
additional information
?
-
-
the coagulant activity of the peptidase is higher than the proteolytic activity and there is a preference for aromatic, basic, and nonpolar amino acids, particularly methionine, with specific cleavage of the peptide bond between phenylalanine and methionine
-
-
?
additional information
?
-
-
milk clotting activity
-
-
?
additional information
?
-
-
trypsinogen activation
-
-
?
additional information
?
-
-
the enzyme shows milk clotting activity with skim milk as substrate
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
additional information
?
-
-
milk clotting activity
-
-
?
additional information
?
-
-
peptide bonds susceptible to the action of the enzyme posess mainly bulky amino acids
-
-
?
additional information
?
-
-
trypsinogen activation (at pH 3.4)
-
-
?
additional information
?
-
-
trypsinogen activation
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
additional information
?
-
-
very broad substrate specificity, overview
-
-
?
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1,2-epoxy-3-(4-nitrophenoxy)propane
Ac-NA-Nva-3-hydroxy 4-amino 6-methyl heptanoic acid-Nva-NA-amide
-
-
Ac-NA-Nva-3-hydroxy 4-amino 6-methyl heptanoyl-Nva-NA-amide
-
-
Ac-NA-Val-3-hydroxy 4-amino 6-methyl heptanoic acid-2-aminobutanoyl-NA-amide
-
-
Ac-NA-Val-3-hydroxy 4-amino 6-methyl heptanoyl-Abu-NA-amide
-
-
acetylpepstatin
-
Streptomyces pepsin inhibitor
Al3+
-
16% residual activity at 10 mM
Ba2+
-
about 64 residual activity at 10 mM
Ca2+
-
about 44% residual activity at 10 mM
Co2+
-
0.3% residual activity at 10 mM; about 36% residual activity at 10 mM
CTAB
-
in the presence of CTAB, 20 and 10 % relative activities are maintained at concentrations of 0.1% (w/v) and 1% (w/v), respectively
Diazoacetyl-DL-norleucine methyl ester
dithiothreitol
-
the peptidase shows residual activities of 50 and 40% following incubation with 100 or 150 mM dithiothreitol, respectively
guanidine
-
the enzyme maintains approximately 70 and 60% of proteolytic activity at 100 and 150 mM guanidine, respectively
K+
-
about 56% residual activity at 10 mM
Mg2+
-
about 36% residual activity at 10 mM
Mn2+
-
about 36% residual activity at 10 mM
Peptide inhibitor
-
sequence: D-His-Pro-Phe-His-Phe(Psi)[CH2-NH]Phe-Val-Tyr
-
Piper hispidum essential oil
-
less than 10% residual activity at 0.048 mg/ml
-
Piper sp. essential oil
-
less than 30% residual activity at 0.048 mg/ml
-
Piper tmarginatum essential oil
-
less than 50% residual activity at 0.048 mg/ml
-
Piper tuberculatum essential oil
-
less than 10% residual activity at 0.048 mg/ml
-
SDS
-
the peptidase maintains approximately 50 % of activity in the presence of 0.02 % (w/v) SDS andloses nearly all activity during incubation with 0.08 % (w/v) SDS
Triton X-100
-
approximately 60% residual activity at 0.2 % (v/v) Triton X-100
Tween 20
-
approximately 60% residual activity at 0.2 % (v/v) Tween 20
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
amino acid sequence around the 1,2-epoxy-3-(4-nitrophenoxy)propane-reactive residues
Diazoacetyl-DL-norleucine methyl ester
-
-
Diazoacetyl-DL-norleucine methyl ester
-
Cu2+ essential for this reaction
Diazoacetyl-DL-norleucine methyl ester
-
Cu2+ essential for this reaction; rate of reaction of this inhibitor with the enzyme is decreased in the presence of pepstatin; the rate of inactivation accelerates with increasing concentration of Cu2+
Diazoacetyl-DL-norleucine methyl ester
-
Cu2+ essential for this reaction
Diazoacetyl-DL-norleucine methyl ester
-
-
pepstatin
-
A
pepstatin
-
93% inhibition at 0.02 mM, 73% at 0.01 mM
pepstatin A
-
40% residual activity at 0.2 mM
pepstatin A
-
less than 5% residual activity at 10 mM
additional information
-
not inhibited by urea
-
additional information
-
not: p-bromophenacyl bromide
-
additional information
-
development of petidomimetic inhibitors
-
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Adenoma
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Alzheimer Disease
Molecular Docking and 3D Qsar Studies of C000000956 as a Potent Inhibitor of Bace-1.
Alzheimer Disease
Multiple e-Pharmacophore Modeling Combined with High-Throughput Virtual Screening and Docking to Identify Potential Inhibitors of ?-Secretase(BACE1).
Alzheimer Disease
Overview of pepsin-like aspartic peptidases.
Arthritis, Rheumatoid
Lysosomal peptidases and glycosidases in rheumatoid arthritis.
Asthma
Recognition of Fungal Protease Activities Induces Cellular Activation and Eosinophil-Derived Neurotoxin Release in Human Eosinophils.
Breast Neoplasms
Overview of pepsin-like aspartic peptidases.
Breast Neoplasms
Ribozyme-targeting procathepsin D and its effect on invasion and growth of breast cancer cells: an implication in breast cancer therapy.
Carcinoma
Diagnostic and Prognostic Role of Immunohistochemical Expression of Napsin-A Aspartic Peptidase in Clear Cell and Papillary Renal Cell Carcinoma: A Study Including 233 Primary and Metastatic Cases.
Carcinoma
Novel biomarker candidates for the diagnosis of ovarian clear cell carcinoma.
Carcinoma, Renal Cell
Diagnostic and Prognostic Role of Immunohistochemical Expression of Napsin-A Aspartic Peptidase in Clear Cell and Papillary Renal Cell Carcinoma: A Study Including 233 Primary and Metastatic Cases.
cathepsin l deficiency
Epidermal differentiation: the role of proteases and their inhibitors.
Chagas Disease
Aspartic Peptidases of Human Pathogenic Trypanosomatids: Perspectives and Trends for Chemotherapy.
Chagas Disease
Decoding the anti-Trypanosoma cruzi action of HIV peptidase inhibitors using epimastigotes as a model.
Chromoblastomycosis
Fonsecaea pedrosoi Sclerotic Cells: Secretion of Aspartic-Type Peptidase and Susceptibility to Peptidase Inhibitors.
Coinfection
Decoding the anti-Trypanosoma cruzi action of HIV peptidase inhibitors using epimastigotes as a model.
Colitis
Chlorogenic Acid Suppresses miR-155 and Ameliorates Ulcerative Colitis through the NF-?B/NLRP3 Inflammasome Pathway.
Colonic Neoplasms
Increased expression of cathepsin D is required for L1-mediated colon cancer progression.
Colorectal Neoplasms
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Insulin Resistance
Altered amyloid precursor protein processing regulates glucose uptake and oxidation in cultured rodent myotubes.
Leishmaniasis
Aspartic Peptidases of Human Pathogenic Trypanosomatids: Perspectives and Trends for Chemotherapy.
Neoplasms
A novel aspartate protease gene, ALP56, is related to morphological features of colorectal adenomas.
Neoplasms
Complex modulation of peptidolytic activity of cathepsin D by sphingolipids.
Neoplasms
Novel biomarker candidates for the diagnosis of ovarian clear cell carcinoma.
Neoplasms
Ribozyme-targeting procathepsin D and its effect on invasion and growth of breast cancer cells: an implication in breast cancer therapy.
Neoplasms
Therapeutic potential of HIV protease-activable CASP3.
Netherton Syndrome
Epidermal differentiation: the role of proteases and their inhibitors.
Opportunistic Infections
The Widespread Anti-Protozoal Action of HIV Aspartic Peptidase Inhibitors: Focus on Plasmodium spp., Leishmania spp. and Trypanosoma cruzi.
Papillon-Lefevre Disease
Epidermal differentiation: the role of proteases and their inhibitors.
Stomach Ulcer
Overview of pepsin-like aspartic peptidases.
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0.036
Abz-LSFMAIQ-EDDnp
-
at pH 5.5 and 50°C
0.23 - 1.1
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala
0.006 - 0.269
KAIEF p-nitrophenylalanine-RL
0.007 - 0.139
KLIEF p-nitrophenylalanine-RL
0.008 - 0.089
KPAEF p-nitrophenylalanine-RL
0.004 - 0.013
KPALF p-nitrophenylalanine-RL
0.01 - 0.065
KPDEF p-nitrophenylalanine-RL
0.006 - 0.157
KPIAF p-nitrophenylalanine-RL
0.003 - 0.211
KPIDF p-nitrophenylalanine-RL
0.002 - 0.057
KPIEF p-nitrophenylalanine-RL
0.006 - 0.056
KPILF p-nitrophenylalanine-RL
0.003 - 0.047
KPISF p-nitrophenylalanine-RL
0.004 - 0.101
KPLEF p-nitrophenylalanine-RL
0.008
KPREF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.007 - 0.108
KPSEF p-nitrophenylalanine-RL
0.0034
KPVSY(4-NO2-F)RL
-
-
0.0034
KPVSY(NO2)FRL
-
pH 7.4, 37°C
0.009 - 0.21
KSIEF p-nitrophenylalanine-RL
0.23
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala
-
pH 6.0
1.1
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala
-
pH 2.0
0.006
KAIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.269
KAIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.007
KLIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.139
KLIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.008
KPAEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.089
KPAEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.004
KPALF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.013
KPALF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.01
KPDEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.065
KPDEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.006
KPIAF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.157
KPIAF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.003
KPIDF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.211
KPIDF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.002
KPIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.057
KPIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.006
KPILF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.056
KPILF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.003
KPISF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.047
KPISF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.004
KPLEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.101
KPLEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.007
KPSEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.108
KPSEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.009
KSIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
0.21
KSIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 46
KAIEF p-nitrophenylalanine-RL
5 - 38
KLIEF p-nitrophenylalanine-RL
21 - 22
KPAEF p-nitrophenylalanine-RL
9 - 13
KPALF p-nitrophenylalanine-RL
3 - 8
KPDEF p-nitrophenylalanine-RL
3 - 17
KPIAF p-nitrophenylalanine-RL
0.77 - 6.08
KPIDF p-nitrophenylalanine-RL
6 - 41
KPIEF p-nitrophenylalanine-RL
0.23 - 3
KPILF p-nitrophenylalanine-RL
3 - 4
KPISF p-nitrophenylalanine-RL
7
KPLEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, wild-type and chimeric enzyme
18
KPREF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
6 - 7
KPSEF p-nitrophenylalanine-RL
55
KPVSY(NO2)FRL
-
pH 7.4, 37°C
1.8 - 13
KSIEF p-nitrophenylalanine-RL
5
KAIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
46
KAIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
5
KLIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
38
KLIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
21
KPAEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
22
KPAEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
9
KPALF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
13
KPALF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
3
KPDEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
8
KPDEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
3
KPIAF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
17
KPIAF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.77
KPIDF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
5
KPIDF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
6.08
KPIDF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
6
KPIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
41
KPIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
0.23
KPILF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
3
KPILF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
3
KPISF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
4
KPISF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
6
KPSEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
7
KPSEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
1.8
KSIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C
13
KSIEF p-nitrophenylalanine-RL
-
pH 3.0, 37°C, chimeric enzyme
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Majima, E.; Oda, K.; Murao, S.; Ichishima, E.
Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate
Agric. Biol. Chem.
52
787-793
1988
Rhizopus sp.
-
brenda
Takahashi, K.; Chang, W.J.
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin
J. Biochem.
80
497-506
1976
Rhizopus microsporus var. chinensis
brenda
Hofmann, T.; Hodges, R.S.; James, M.N.G.
Effect of pH on the activities of penicillopepsin and Rhizopus pepsin and a proposal for the productive substrate binding mode in penicillopepsin
Biochemistry
23
635-643
1984
Rhizopus sp.
brenda
Tsuru, D.; Hattori, A.; Tsuji, H.; Yamamoto, T.; Fukumoto, J.
Mold proteases. II. Substrate specificity of acid protease of Rhizopus chinensis
Agric. Biol. Chem.
33
1419-1426
1969
Rhizopus microsporus var. chinensis
-
brenda
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