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2-aminobenzoyl-Phe-Arg-Ala-(2,4-dinitrophenyl)-epsilon-NH2-lysine + H2O
?
-
-
-
?
Abz-FRF(NO2)A + H2O
?
-
-
-
?
Abz-GIVRAK(Dnp) + H2O
?
-
-
-
?
Arg-Arg-7-amido-4-methylcoumarin + H2O
Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
CBZ-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
fibronectin + H2
?
-
-
-
?
hemoglobinase + H2O
?
-
degradation
-
-
?
human IgG + H2O
?
-
degradation
-
-
?
IEC-6 monolayer + H2O
?
enzyme hydrolyzes the extracellular matrix of rat intestine epithelial cell line IEC-6 monolayer that the intercellular space of the IEC-6 monolayer increases while the shape of the adherent cells partly rounds up
-
-
?
myristoylated-alanine-rich C-kinase + H2O
?
-
specific degradation, the enzyme degrades the protein involved in actin cytoskeleton regulation
-
-
?
myristoylated-alanine-rich C-kinase substrate + H2O
?
-
i.e. MARCKS, specific degradation
-
-
?
Nalpha-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Phe-Arg-7-amido-4-methylcoumarin + H2O
Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
protein rGSII-D88N + H2O
?
-
legume lectin
-
-
?
Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
Z-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Leu-Arg-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
additional information
?
-
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
CmSvp may contribute to insect counter-defense, in part by inhibiting CmCatB expression under normal growth conditions, but releasing the inhibition when insects are challenged by dietary protease inhibitors
-
-
?
additional information
?
-
strongly induces cathepsin B-like cysteine protease 1c transcripts when fed diet containing a soybean cysteine protease inhibitor soyacystatin N. The scN-activated and developmentally regulated CmCatB1 expression pattern suggests it may have a unique function in insect counter-defence against antinutritional factors. CmCatB1 confers inhibitor-insensitive enzymatic activity to cowpea bruchids, which is crucial for insect survival when challenged by dietary protease inhibitors
-
-
?
additional information
?
-
strongly induces cathepsin B-like cysteine protease 1c transcripts when fed diet containing a soybean cysteine protease inhibitor soyacystatin N. The scN-activated and developmentally regulated CmCatB1 expression pattern suggests it may have a unique function in insect counter-defence against antinutritional factors. CmCatB1 confers inhibitor-insensitive enzymatic activity to cowpea bruchids, which is crucial for insect survival when challenged by dietary protease inhibitors
-
-
?
additional information
?
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
?
additional information
?
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
?
additional information
?
-
-
the enzyme is involved in yolk protein degradation during embryogenesis
-
-
?
additional information
?
-
-
the enzyme is involved in lethal N-methyl-D-aspartate-induced collapse and F-actib loss of dendritic spines, sub-lethal ecitosis injury to dendrites can elicit loss or shrinkage of dendritic spines, specific enzyme inhibitors attenuate the effect, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the inhibition of antigen presentation by degrading MHC class II molecules in the parasiophorus vacuole
-
-
?
additional information
?
-
-
the enzyme does not readily hyrolyze benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin which is cleaved by cathespsin B. The substrate specificity is attributed to Gly234 at the S2 subsite of LmajcatB, which forms a larger, more hydrophobic pocket compared with mammalian cathepsin B
-
-
?
additional information
?
-
-
the enzyme is not able to cleave synthetic substrates having an Arg in position P2
-
-
?
additional information
?
-
-
the enzyme might be involved in activation of TGF-beta, a suppressive cytokine in Leishmania infection
-
-
?
additional information
?
-
-
the enzyme might be involved in activation of TGF-beta, a suppressive cytokine in Leishmania infection, the enzyme is involved in the inhibition of antigen presentation by degrading MHC class II molecules in the parasiophorus vacuole
-
-
?
additional information
?
-
collagen type IV, elastin, keratin, fibrinogen type III and myelin basic protein are degraded
-
-
?
additional information
?
-
-
collagen type IV, elastin, keratin, fibrinogen type III and myelin basic protein are degraded
-
-
?
additional information
?
-
-
no hydrolysis of benzoyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin and benzoyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
no hydrolysis of benzoyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin and benzoyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
-
-
?
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(1S,2S)-2-(((S)-1-((4-guanidinobutyl)amino)-4-methyl-1-oxopentan-2-yl)carbamoyl)cyclopropanecarboxylic acid
-
i.e. E-64
acetyl-Leu-Val-lysinal
350 nM, 37°C, pH 4.5, 1 h, 15% inhibition
CA074Me
-
specific inhibition
cathepsin L inhibitor 1
-
has a lower inhibitory effct on cathepsin B-like protease
CBZ-Phe-Gly-NHO-Bz-pMe
350 nM, 37°X, pH 4.5, 1 h, 87% inhibition
K11002
-
morpholine urea-Phe-homoPhe-vinylsulphonylphenyl
L-transepoxysuccinyl-L-leucylamido-(4-guanidino)-butane
E64
Leishmania cysteine peptidase inhibitor 1
-
N-(L-3-trans-propylcarbamoyl-oxirane-2-carbonyl)-L-Ile-L-Pro
-
CA074, irreversible inhibitor
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-Ile-Pro-OH
CA-074, irreversible inhibitor
N-(Na-carbonyl-Cpd-Gln-Ala-al)-Leu
elastatinal, irreversible inhibitor
N-trans-(epoxysuccinyl)-L-leucine 4-guanidinobutylamide
E-64, irreversible inhibitor
nicotinamide
complete inhibition at 25 mM
Z-Phe-Ala-diazomethylketone
irreversible inhibitor
Z-Phe-Phe-diazomethylketone
irreversible inhibitor
Z-Phe-Tyr(tBu)-diazomethylketone
irreversible inhibitor
ZLIII115A
-
IC50: 0.01 mM
ZLIII43A
-
IC50: 0.002 mM
CA-074
-
CA-074
a specific cathepsin B inhibitor, the membrane-permeable derivative of CA-074, impairs invasion of epithelial MDBK cells by Eimeria tenella sporozoites
CA074
-
specific inhibition of CPC
CA074
-
i.e. N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
CA074
-
specific inhibition of CPC
CA074
-
specific inhibition of CPC
CA074
350 nM, 37°C, pH 4.5, 1 h, complete inhibition
cystatin
Haemonchus contortus, GenBank accession number AF035945
-
cystatin
-
protects against Leishmania infection in vivo
-
cystatin
-
protects against Leishmania infection in vivo
-
cystatin
350 nM, 37°C, pH 4.5, 1 h, 23% inhibition
-
E-64
-
E-64
350 nM, 37°C, pH 4.5, 1 h, complete inhibition
Leishmania cysteine peptidase inhibitor 1
-
i.e. ICP, inhibitor of CPs from family C1 clan A
-
Leishmania cysteine peptidase inhibitor 1
-
i.e. ICP, inhibitor of CPs from family C1 clan A
-
Leishmania cysteine peptidase inhibitor 1
-
i.e. ICP, inhibitor of CPs from family C1 clan A
-
additional information
no significant inhibitory effects for pepstatin and PMSF
-
additional information
activity is unaffeceted by soyacystatin N
-
additional information
activity is unaffeceted by soyacystatin N
-
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24000
-
x * 24000, 2-D electrophoresis
27400
-
x * 37800, about, preproprotein, sequence calculation, x * 27400, about, mature protein, sequence calculation
28500
x * 28500, calculated for mature enzyme, x * 32000, SDS-PAGE (glycosylated)
32000
x * 28500, calculated for mature enzyme, x * 32000, SDS-PAGE (glycosylated)
35000
x * 35000, x * 45000, gelatin SDS-PAGE digestion assay
37000
-
x * 37000, recombinant detagged enzyme, SDS-PAGE
37800
-
x * 37800, about, preproprotein, sequence calculation, x * 27400, about, mature protein, sequence calculation
42000
x * 42000, recombinant zymogen, SDS-PAGE
43000
x * 43000, SDS-PAGE, predicted: 36700 Da (with pro-region and without signal peptide), 29000 Da (without pro-region)
45000
x * 35000, x * 45000, gelatin SDS-PAGE digestion assay
additional information
-
SDS-PAGE analysis of the eluted recombinant protein reveals a prominent band of 39000 Da and a minor protein of 40000 Da. These bands correspond to glycosylated forms of a 35000 Da protein, the expected size of the protease
additional information
SDS-PAGE analysis of the eluted recombinant protein reveals a prominent band of 39000 Da and a minor protein of 40000 Da. These bands correspond to glycosylated forms of a 35000 Da protein, the expected size of the protease
additional information
-
SDS-PAGE analysis of the eluted recombinant protein reveals a prominent band of 40000 Da and a minor protein of 50000 Da. These bands correspond to glycosylated forms of a 36000 Da protein, the expected size of the protease
additional information
SDS-PAGE analysis of the eluted recombinant protein reveals a prominent band of 40000 Da and a minor protein of 50000 Da. These bands correspond to glycosylated forms of a 36000 Da protein, the expected size of the protease
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Sakanari, J.A.; Nadler, S.A.; Chan, V.J.; Engel, J.C.; Leptak, C.; Bouvier J.
Leishmania major: comparison of the cathepsin L- and B-like cysteine protease genes with those of other trypanosomatids
Exp. Parasitol.
85
63-76
1997
Leishmania major (P90627)
brenda
Chan, V.J.; Selzer, P.M.; McKerrow, J.H.; Sakanari, J.A.
Expression and alteration of the S2 subsite of the Leishmania major cathepsin B-like cysteine protease
Biochem. J.
340
113-117
1999
Leishmania major
brenda
Selzer, P.M.; Chen, X.; Chan, V.J.; Cheng, M.; Kenyon, G.L.; Kuntz, I.D.; Sakanari, J.A.; Cohen, F.E.; McKerrow, J.H.
Leishmania major: molecular modeling of cysteine proteases and prediction of new nonpeptide inhibitors
Exp. Parasitol.
87
212-221
1997
Leishmania major
brenda
Zhao, X.F.; An, X.M.; Wang, J.X.; Dong, D.J.; Du, X.J.; Sueda, S.; Kondo, H.
Expression of the Helicoverpa cathepsin B-like proteinase during embryonic development
Arch. Insect Biochem. Physiol.
58
39-46
2005
Helicoverpa armigera
brenda
Mottram, J.C.; Coombs, G.H.; Alexander, J.
Cysteine peptidases as virulence factors of Leishmania
Curr. Opin. Microbiol.
7
375-381
2004
Leishmania amazonensis, Leishmania major, Leishmania mexicana
brenda
Jasmer, D.P.; Mitreva, M.D.; McCarter, J.P.
mRNA sequences for Haemonchus contortus intestinal cathepsin B-like cysteine proteases display an extreme in abundance and diversity compared with other adult mammalian parasitic nematodes
Mol. Biochem. Parasitol.
137
297-305
2004
Haemonchus contortus
brenda
Graber, S.; Maiti, S.; Halpain, S.
Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines
Neuropharmacology
47
706-713
2004
Homo sapiens
brenda
Mendoza-Palomares, C.; Biteau, N.; Giroud, C.; Coustou, V.; Coetzer, T.; Authie, E.; Boulange, A.; Baltz, T.
Molecular and biochemical characterization of a cathepsin B-like protease family unique to Trypanosoma congolense
Eukaryot. Cell
7
684-697
2008
Trypanosoma congolense, Trypanosoma congolense (B2C323)
brenda
Ahn, J.E.; Guarino, L.A.; Zhu-Salzman, K.
Seven-up facilitates insect counter-defense by suppressing cathepsin B expression
FEBS J.
274
2800-2814
2007
Callosobruchus maculatus
brenda
Koo, Y.D.; Ahn, J.E.; Salzman, R.A.; Moon, J.; Chi, Y.H.; Yun, D.J.; Lee, S.Y.; Koiwa, H.; Zhu-Salzman, K.
Functional expression of an insect cathepsin B-like counter-defence protein
Insect Mol. Biol.
17
235-245
2008
Callosobruchus maculatus (B2XVS9), Callosobruchus maculatus (Q5VJM8)
brenda
Miranda-Miranda, E.; Zamora-Ruiz, A.; Cossio-Bayugar, R.
Molecular cloning and expression of a Caenorhabditis elegans Cathepsin B-like Protease
Biotechnology
8
242-247
2009
Caenorhabditis elegans (P43510)
-
brenda
Chi, Y.H.; Koo, Y.D.; Dai, S.Y.; Ahn, J.E.; Yun, D.J.; Lee, S.Y.; Zhu-Salzman, K.
N-glycosylation at non-canonical Asn-X-Cys sequence of an insect recombinant cathepsin B-like counter-defense protein
Comp. Biochem. Physiol. B
156
40-47
2010
Callosobruchus maculatus
brenda
Doleckova, K.; Kasny, M.; Mikes, L.; Cartwright, J.; Jedelsky, P.; Schneider, E.; Dvorak, J.; Mountford, A.; Craik, C.; Horak, P.
The functional expression and characterisation of a cysteine peptidase from the invasive stage of the neuropathogenic schistosome Trichobilharzia regenti
Int. J. Parasitol.
39
201-211
2009
Trichobilharzia regenti (A7L844), Trichobilharzia regenti
brenda
Kim, J.H.; Yang, A.H.; Sohn, H.J.; Kim, D.; Song, K.J.; Shin, H.J.
Immunodominant antigens in Naegleria fowleri excretory--secretory proteins were potential pathogenic factors
Parasitol. Res.
105
1675-1681
2009
Naegleria fowleri
brenda
Kerr, I.D.; Wu, P.; Marion-Tsukamaki, R.; Mackey, Z.B.; Brinen, L.S.
Crystal Structures of TbCatB and rhodesain, potential chemotherapeutic targets and major cysteine proteases of Trypanosoma brucei
PLoS Negl. Trop. Dis.
4
e701
2010
Trypanosoma brucei
brenda
De Vries, E.; Bakker, N.; Krijgsveld, J.; Knox, D.P.; Heck, A.J.; Yatsuda, A.P.
An AC-5 cathepsin B-like protease purified from Haemonchus contortus excretory secretory products shows protective antigen potential for lambs
Vet. Res.
40
41
2009
Haemonchus contortus (Q25030), Haemonchus contortus
brenda
Thul, S.; Khan, F.; Khanuja, S.
Cathepsin B-like protease from chili pepper revealed by in silico approach
Plant OMICS
4
120-125
2011
Capsicum frutescens, Nicotiana rustica (Q40413)
-
brenda
Ni, F.; Wang, Y.; Zhang, J.; Yu, L.; Fang, W.; Luo, D.
Cathepsin B-like and hemoglobin-type cysteine proteases: stage-specific gene expression in Angiostrongy cantonensis
Exp. Parasitol.
131
433-441
2012
Angiostrongylus cantonensis (E5KEA9), Angiostrongylus cantonensis (E5KEB0)
brenda
Unciti-Broceta, J.D.; Maceira, J.; Morales, S.; Garcia-Perez, A.; Munoz-Torres, M.E.; Garcia-Salcedo, J.A.
Nicotinamide inhibits the lysosomal cathepsin B-like protease and kills African trypanosomes
J. Biol. Chem.
288
10548-10557
2013
Trypanosoma brucei (Q6R7Z5), Trypanosoma brucei
brenda
Cheng, M.; Yang, X.; Li, Z.; He, H.; Qu, Z.; He, A.; Wu, Z.; Zhan, X.
Cloning and characterization of a novel cathepsin B-like cysteine proteinase from Angiostrongylus cantonensis
Parasitol. Res.
110
2413-2422
2012
Angiostrongylus cantonensis
brenda
Rieux, A.; Gras, S.; Lecaille, F.; Niepceron, A.; Katrib, M.; Smith, N.C.; Lalmanach, G.; Brossier, F.
Eimeripain, a cathepsin B-like cysteine protease, expressed throughout sporulation of the apicomplexan parasite Eimeria tenella
PLoS ONE
7
e31914
2012
Eimeria tenella (G9IBU6), Eimeria tenella
brenda
Porodko, A.; Cirnski, A.; Petrov, D.; Raab, T.; Paireder, M.; Mayer, B.; Maresch, D.; Nika, L.; Biniossek, M.L.; Gallois, P.; Schilling, O.; Oostenbrink, C.; Novinec, M.; Mach, L.
The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities
Biol. Chem.
399
1223-1235
2018
Arabidopsis thaliana (Q93VC9), Arabidopsis thaliana (Q94K85)
brenda
Long, Y.; Cao, B.; Yu, L.; Tukayo, M.; Feng, C.; Wang, Y.; Luo, D.
Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration
Parasite
22
37
2015
Angiostrongylus cantonensis (E5KEA9), Angiostrongylus cantonensis
brenda
Ferrara, T.F.; Schneider, V.K.; Kishi, L.T.; Carmona, A.K.; Alves, M.F.; Belasque-Junior, J.; Rosa, J.C.; Hunter, W.B.; Henrique-Silva, F.; Soares-Costa, A.
Characterization of a recombinant cathepsin B-like cysteine peptidase from Diaphorina citri Kuwayama (Hemiptera Liviidae) A putative target for control of Citrus Huanglongbing
PLoS ONE
10
e0145132
2015
Diaphorina citri (A0A0U4DX43)
brenda