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Information on EC 3.4.22.1 - cathepsin B and Organism(s) Homo sapiens and UniProt Accession P07858
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3.4.22.1 cathepsin BSpecify your search results
Word Map
- 3.4.22.1
- cathepsins
- lysosomal
- proteinases
- papain
- collagen
- metastasis
- pancreatic
- cystatins
-
procathepsin
- upa
-
exopeptidase
- food industry
- myofibrillar
- mansoni
- schistosoma
-
lc3-ii
- calpains
-
permeabilization
- zymogen
-
intralysosomal
- leupeptin
- peptidase
-
hyperamylasemia
- pharmacology
-
papain-like
- diagnostics
- biotechnology
- collagenase
-
antibody-drug
-
autophagy-lysosome
- pepstatin
-
acinar
- ficin
- plasminogen
- caspase-1
- proenzyme
- legumain
-
autophagosomes
- elastase
- caerulein
-
caerulein-induced
- molecular biology
-
dipeptidyl
-
fluorogenic
- inflammasome
- endosomes
-
pro-il-1
-
supramaximal
-
l-like
-
b-mediated
- fasciola
- mu-calpain
- medicine
- trypsinogen
- hepatica
- drug development
-
collagenolytic
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
Synonyms
cathepsin b, cathepsin-b, cysteine cathepsin, devdase, cat b, cathepsin b1, cathb, cath b, smcb1, cath-b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cathepsin B
-
APP secretase
-
-
-
-
CatB
-
-
cathepsin B1
-
-
-
-
cathepsin II
-
-
-
-
additional information
additional information
the enzyme belongs to the group of cysteine proteases
additional information
-
cathepsin B belongs to the family of lysosomal cysteine proteases
additional information
-
cathepsin B belongs to the lysosomal cysteine protease subgroup of the cathepsin family
additional information
-
cathepsin B is a cysteine peptidase of the papain family
additional information
-
cathespsin B belongs to the papain-family of cysteine proteases
additional information
-
the cysteine cathepsin B belongs to the papain family C1A
additional information
-
the enzyme belongs to the cysteine proteases of the papain family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
kinetics
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
cathepsin B possesses a long and narrow substrate-binding active site cleft with catalytic residue Cys, the surfaces of the S1 and S1' subsites are negatively charged due to presence of Glu122 and Glu194, the occluding loop of residue 105-125 is a structural feature containing the two positively charged His residues, His110 and His111, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9047-22-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH + H2O
?
exopeptidase activity
-
-
?
Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp + H2O
Abz-Ala-Phe-Arg + Ser-Ala-X-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp, with X is Asn > Tyr, His, Leu, Trp > Ser, Phe, Pro Lys > Asp, Ala
-
-
?
Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-Ala-Phe-Arg + Ser-X-Arg-Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp, with X is Asn > Trp, Tyr, Ala > Ser, Phe > His, Lys > Asp, Leu, Pro
-
-
?
Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-Ala-X-Ala-Phe-Arg + Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp, with X is Leu, Tyr > Phe, Ala, Ser, Pro > His, Lys > Asn, Asp
-
-
?
Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp + H2O
Abz-Ala-X-Arg + Ser-Ala-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp, with X is Phe, Leu > Arg > Ala > Pro
-
-
?
Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-X-Ala-Phe-Arg + Ser-Ala-Gln-EDDnp
kcat/Km for Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp, with X is Leu, Phe, Trp > Ser, Asn, Asp, Ala > Tyr, His, Lys
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
endopeptidase activity
-
-
?
benzyloxycarbonyl-phenylalanyl-arginyl-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
37°C, 1 mM DTT, 1 mM EDTA, pH 6.0
-
-
?
Cbz-FR-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
37°C, pH 6.0, 200 mM NaCl, 1 mM EDTA, 5 nM DTT
-
-
?
Dnp-Gly-Phe-Arg-Trp-X-OH + H2O
Dnp-Gly-Phe + Arg-Trp-X-OH
kcat/Km for Dnp-Gly-Phe-Arg-Trp-X-OH, with X is Phe > Tyr, Ile > Leu > Cval > Arg > Lys, Pro > Gln, Ser > Asp, Glu, Ala
-
-
?
Dnp-Gly-Phe-Arg-X-Trp-OH + H2O
Dnp-Gly-Phe + Arg-X-Trp-OH
kcat/Km for Dnp-Gly-Phe-Arg-X-Trp-OH, with X is Phe > Ser > Leu > Ala > Ile > Tyr, Val > Gln > Lys > Gly > His, Asp > Arg > Glu
-
-
?
Dnp-Gly-Phe-X-Phe-Trp-OH + H2O
Dnp-Gly-Phe-X + Phe-Trp-OH
kcat/Km for Dnp-Gly-Phe-X-Phe-Trp-OH, with X is Arg > Lys > Phe > Leu > Val > His, Gln > Ser > Gly Ala > Glu > Tyr > Ile, Asp
-
-
?
Dnp-Gly-X-Arg-Phe-Trp-OH + H2O
Dnp-Gly-X-Arg + Phe-Trp-OH
kcat/Km for Dnp-Gly-X-Arg-Phe-Trp-OH, with X is Phe > Tyr > Lys > Val > Ala > Ile > Ser, Pro > His > Leu > Arg > Asp, Glu
-
-
?
herpes simplex virus type 1 origin binding protein + H2O
herpes simplex virus type 1 origin binding protein 1
53 kDa protein
50 kDa protein
-
?
N-CBZ-L-Arg-L-Arg-7-amido- 4-methylcoumarin + H2O
N-CBZ-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-CBZ-Arg-Arg 7-amido-4-methylcoumarin + H2O
Nalpha-CBZ-Arg-Arg + 7-amino-4-methylcoumarin
1 mM DTT
-
-
?
trypsinogen + H2O
trypsin + ?
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
-
?
trypsinogen activation peptide + H2O
?
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
1 mM DTT, 2 mM EDTA, pH 6.8, 37°C, activity varied from 0.013 to 3.4 U/mg protein in normal tissue and from 0.007 to 20.0 U/mg protein in cancer tissue
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-(Nepsilon-2,4-dinitrophenyl)Lys + H2O
2-aminobenzoyl-Gly-Ile-Val-Arg + Ala-(Nepsilon-2,4-dinitrophenyl)Lys
-
an exoproteolytic substrate
-
-
?
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH + H2O
?
-
exopeptidase activity
-
-
?
5-amino-1-(phenylsulfonyl)-1H-pyrazol-3-yl thiophene-2-carboxylate + H2O
5-amino-1-(phenylsulfonyl)-1,2-dihydro-3H-pyrazol-3-one + thiophene-2-carbaldehyde
-
-
-
-
?
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl pyridine-4-carboxylate + H2O
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1,2-dihydro-3H-pyrazol-3-one + pyridine-4-carbaldehyde
-
-
-
-
?
6-maleimidocaproic acid-L-Arg-Arg-Ala-Leu-Ala-Leu-Ala-camptothecin + H2O
?
-
-
major cleavage products are L-Leu-Ala-Leu-Ala-camptothecin, L-Ala-Leu-Ala-camptothecin, L-Leu-Ala-camptothecin, and camptothecin
-
?
6-maleimidocaproic acid-L-Arg-Arg-Ala-Leu-Ala-Leu-doxorubicin + H2O
?
-
-
major cleavage products are L-Leu-Ala-Leu-doxorubicin, L-Leu-doxorubicin, and doxorubicin
-
?
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-P-OH + H2O
?
-
-
-
-
?
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-W-OH + H2O
?
-
-
-
-
?
Abz-FRA-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH + H2O
?
-
-
-
-
?
Abz-FRF-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH + H2O
?
-
-
-
-
?
Ac-Arg-Arg-4-methyl-7-amidocoumarin + H2O
Ac-Arg-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Ac-His-Pro-Val-Lys-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
Ac-His-Pro-Val-Lys + 7-amino-3-carbamoyl-4-methylcoumarin
-
assay at pH 5.5, 37°C
-
-
?
acetyl-Arg-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-F-R-4-methylcoumarin-7-amide + H2O
acetyl-F-R + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
amyloid precursor protein C-terminal fragment + H2O
?
-
cathepsin B degraded C-terminal fragments regardless of phosphorylation
-
-
?
antiprotease secretory leucoprotease inhibitor + H2O
cleaved SLP1 protein
-
i.e. SLP1 protein, cleavage between residues Thr67 and Tyr68
-
?
benzoyl-L-3-pyridyl-Ala-l-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-3-pyridyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminocyclohexy-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminomethyl-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminomethyl-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-guanidine-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-guanidine-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-piperidinyl-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-piperidinyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-His-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-N-dimethyl-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-N-dimethyl-His-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
benzyloxycarbonyl-FR-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
Boc-Asp-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Boc-Asp-Pro-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumarin-7-amide + H2O
Boc-L-Leu-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
pH-dependence of reaction
-
?
Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin + H2O
Boc-Val-Leu-Lys + 4-methyl-7-aminocoumarin
-
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin hydrochloride + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin hydrochloride
-
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
CBZ-Arg-Arg-7-amido-4-methylcoumarin + H2O
CBZ-Arg-Arg + 7-amino-4-methylcoumarin
-
endopeptidase activity
-
-
?
Cbz-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Cbz-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
chemokine (C-C motif) ligand 20 + H2O
CCL20 1-66 isoform + ?
-
CCL20 is also known as liver- and activation-regulated chemokine (LARC), MIP-3alpha, or exodus-1
cathepsin B specifically cleaves off four C-terminally located amino acids and generates a CCL20 1-66 isoform with full functional activity
-
?
epsilon-aminocaproic acid-L-Leu-Gly-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-Gly + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)serine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)serine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)threonine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)threonine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-methyl)-tyrosine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-methyl)-tyrosine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(S-benzyl)cysteine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(S-benzyl)cysteine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-Phe-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-R-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-R + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine-4-methyl-7-coumarylamide + H2O
N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine + 4-methyl-7-coumarylamine
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-arginyl-L-arginyl-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
substrate of mature cathepsin B, also procathepsin B is catalytically active on the synthetic substrate but to a lower extent. The unfolded proenzymeis inactive
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg 7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg-beta-naphthylamide + H2O
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg + beta-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Val-Ile-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Val-Ile-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-carbobenzoxy-L-lysine 4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
-
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-benzoyl-Val-Lys-Lys-Arg-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-Gly-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-Gly-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide + H2O
?
-
-
-
?
phenylacetyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
phenylacetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Tos-Gly-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Tos-Gly-Pro-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Z-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
Z-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-L-Phe-L-Arg 7-amido-4-methylcoumarin + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate of Na-CP-3
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
an endoproteolytic substrate
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
-
albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B and in tumor homogenates of MDA-MB 435 tumor cells from in vitro culture transplanted subcutaneously into the left flank region of mice, overview
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
-
albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B
-
-
?
Proteins + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha
-
-
?
additional information
?
-
enzyme prefers dipeptidyl pathway over monopeptidyl carboxypeptidase pathway
-
?
additional information
?
-
enzyme prefers large aromatic residues at S2' subsite and the exopeptidase activity prefers aromatic side chains in P2' position
-
?
additional information
?
-
-
enzyme prefers large aromatic residues at S2' subsite and the exopeptidase activity prefers aromatic side chains in P2' position
-
?
additional information
?
-
cathepsin B can partially process the 48000 Da intermediate into 34000 Da mature cathepsin D
-
-
?
additional information
?
-
-
cathepsin B can partially process the 48000 Da intermediate into 34000 Da mature cathepsin D
-
-
?
additional information
?
-
no reaction with procarboxypeptidase and proelastase
-
-
?
additional information
?
-
-
no reaction with procarboxypeptidase and proelastase
-
-
?
additional information
?
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
active site mapping with peptidic substrates and inhibitors
-
-
?
additional information
?
-
-
active site mapping with peptidic substrates and inhibitors
-
-
?
additional information
?
-
-
preference for substrate cleavage through dipeptidyl pathway, influence of substrate P2-P1 residues
-
?
additional information
?
-
-
autocatalytic activation of the inactive proenzyme
-
-
?
additional information
?
-
-
cathepsin B is an intracellular lysosomal cysteine proteinase that can degrade extracellular components including collagen and protein turnover in the lysosomal system. Cathepsin B plays an important role in the resolution of organic matrix, a final step in bone resorption. It is also known to play an important role in the initiation and perpetuation of inflammatory processes
-
-
?
additional information
?
-
-
cathepsin B is expressed in cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview
-
-
?
additional information
?
-
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
?
additional information
?
-
-
cathepsin B, together with cathepsin L, urokinase-type plasminogen activator and its inhibitor PAI-1, plays an important role in colorectal cancer invasion. Correlation analysis of proteolytic enzymes in colorectal cancer, overview
-
-
?
additional information
?
-
-
cathepsin-B is a lysosomal cysteine proteasewith broad substrate specificity, which belongs to a family of 11 cysteine proteases. The enzyme is involved in tumor progression, e.g. of endometrial carcinomas
-
-
?
additional information
?
-
-
cysteine cathepsins play a critical role in the biologic activity of tumor-shed vesicles at acidic pH, but not at physiological pH, endothelial cell invasiveness is increased by tumor-shed vesicles exposed to acidic pH, overview
-
-
?
additional information
?
-
-
increased cathepsin B levels in acute and chronic lung diseases resulting from high levels of extracellular neutrophil elastase, expression of the protease can be inhibited by alpha1-antitrypsin augmentation therapy
-
-
?
additional information
?
-
-
NF-kappaB induced up-regulation of cathepsin B expression contributes to the invasive property of the 143B cells lacking mtDNA, overview. Extracellularly released cathepsin B can act alone or in concert with some matrix metalloproteinases
-
-
?
additional information
?
-
-
participation of cathepsin B in emodin-induced apoptosis in HK-2 cells, enzyme inhibition by Ca-074 causes significant attenuation the ratio of hypodiploid and apoptotic cells, partially blockage of caspase 3 activation and inhibition of reduction of cell viability induced by emodin, overview
-
-
?
additional information
?
-
-
Porphyromonas gingivalis strain 381 or its lipopolysaccharides increases the expression of cathepsin B in oral epithelial cells
-
-
?
additional information
?
-
-
regulation of cathepsin B in gingival fibroblasts involves interleukin-6 and its receptor along with the Cav-1-JNK-AP-1 pathway, overview
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of extracellular matrix and of basement membrane components leading to tumor invasion in the intestine. Expression of matrix metalloproteinase-9 and cathepsin B is correlated with lymph node metastasis in advanced gastric carcinoma, but not with patients' postoperative survival, overview. Correlation between the synthesis of cysteine and serine proteases and the potential tumor invasion
-
-
?
additional information
?
-
-
the enzyme is involved in extracellular matrix degradation in caveolae of endothelial cells during tube formation, overview. Cathepsin B regulates both pro- and anti-angiogenic factors and may be a contributor to the angiogenic switch of endothelial cells
-
-
?
additional information
?
-
-
the enzyme is involved in inflammatory processes
-
-
?
additional information
?
-
-
the enzyme plays an important role in cancer invasion and metastasis, the enzyme content is positively correlated with tumors in different tissue types
-
-
?
additional information
?
-
-
autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins
-
-
?
additional information
?
-
-
cathepsin B is a cysteine protease with both endopeptidase and exopeptidase activity
-
-
?
additional information
?
-
-
No activity with Boc-Val-Pro-Arg-4-methyl-7-amidocoumarin, Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin, and D-Val-Leu-Arg-4-methyl-7-amidocoumarin. Wild-type cathepsin B exhibits exopeptidase activity
-
-
?
additional information
?
-
-
procathepsin B shows autocatalytic processing triggered by proenzyme activity, identification of cleavage sites and initiation mechanism, overview. A multi-step process, starting with a unimolecular conformational change of the zymogen, which unmasks the active site and, in the presence of negatively charged molecules and/or surfaces, also converts the zymogen into a better substrate, followed by the bimolecular proteolytic removal of the propeptide
-
-
?
additional information
?
-
-
the assay uses a modified aminomethylcoumarin dipeptide substrate, which generates a fluorescent signal upon cleavage by cathepsin B
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
-
albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B and in tumor homogenates of MDA-MB 435 tumor cells from in vitro culture transplanted subcutaneously into the left flank region of mice, overview
-
-
?
TNF-alpha + H2O
?
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha
-
-
?
Proteins + H2O
?
-
-
-
-
?
additional information
?
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
-
autocatalytic activation of the inactive proenzyme
-
-
?
additional information
?
-
-
cathepsin B is an intracellular lysosomal cysteine proteinase that can degrade extracellular components including collagen and protein turnover in the lysosomal system. Cathepsin B plays an important role in the resolution of organic matrix, a final step in bone resorption. It is also known to play an important role in the initiation and perpetuation of inflammatory processes
-
-
?
additional information
?
-
-
cathepsin B is expressed in cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview
-
-
?
additional information
?
-
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
?
additional information
?
-
-
cathepsin B, together with cathepsin L, urokinase-type plasminogen activator and its inhibitor PAI-1, plays an important role in colorectal cancer invasion. Correlation analysis of proteolytic enzymes in colorectal cancer, overview
-
-
?
additional information
?
-
-
cathepsin-B is a lysosomal cysteine proteasewith broad substrate specificity, which belongs to a family of 11 cysteine proteases. The enzyme is involved in tumor progression, e.g. of endometrial carcinomas
-
-
?
additional information
?
-
-
cysteine cathepsins play a critical role in the biologic activity of tumor-shed vesicles at acidic pH, but not at physiological pH, endothelial cell invasiveness is increased by tumor-shed vesicles exposed to acidic pH, overview
-
-
?
additional information
?
-
-
increased cathepsin B levels in acute and chronic lung diseases resulting from high levels of extracellular neutrophil elastase, expression of the protease can be inhibited by alpha1-antitrypsin augmentation therapy
-
-
?
additional information
?
-
-
NF-kappaB induced up-regulation of cathepsin B expression contributes to the invasive property of the 143B cells lacking mtDNA, overview. Extracellularly released cathepsin B can act alone or in concert with some matrix metalloproteinases
-
-
?
additional information
?
-
-
participation of cathepsin B in emodin-induced apoptosis in HK-2 cells, enzyme inhibition by Ca-074 causes significant attenuation the ratio of hypodiploid and apoptotic cells, partially blockage of caspase 3 activation and inhibition of reduction of cell viability induced by emodin, overview
-
-
?
additional information
?
-
-
Porphyromonas gingivalis strain 381 or its lipopolysaccharides increases the expression of cathepsin B in oral epithelial cells
-
-
?
additional information
?
-
-
regulation of cathepsin B in gingival fibroblasts involves interleukin-6 and its receptor along with the Cav-1-JNK-AP-1 pathway, overview
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of extracellular matrix and of basement membrane components leading to tumor invasion in the intestine. Expression of matrix metalloproteinase-9 and cathepsin B is correlated with lymph node metastasis in advanced gastric carcinoma, but not with patients' postoperative survival, overview. Correlation between the synthesis of cysteine and serine proteases and the potential tumor invasion
-
-
?
additional information
?
-
-
the enzyme is involved in extracellular matrix degradation in caveolae of endothelial cells during tube formation, overview. Cathepsin B regulates both pro- and anti-angiogenic factors and may be a contributor to the angiogenic switch of endothelial cells
-
-
?
additional information
?
-
-
the enzyme is involved in inflammatory processes
-
-
?
additional information
?
-
-
the enzyme plays an important role in cancer invasion and metastasis, the enzyme content is positively correlated with tumors in different tissue types
-
-
?
additional information
?
-
-
autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1E,4E)-1-chloro-4-ethenyl-2-(trichloro-lambda4-tellanyl)hepta-1,4,6-trien-3-ol
-
(2R,3R)-3-(((1S)-1-[(4-carbamimidamidobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
-
(2R,3R)-3-(((1S)-3-methyl-1-[(3-methylbutoxy)carbonyl]butyl)carbamoyl)aziridine-2-carboxylic acid
-
(2S,3S)-3-(((1S)-1-[(4-([(benzyloxy)carbonyl]amino)butyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
-
(2S,3S)-3-(((1S)-1-[(4-aminobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
-
(2S,3S)-3-(((1S)-1-[(4-carbamimidamidobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
-
(2S,3S)-3-(((1S)-1-[(7-aminoheptyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
-
(2S,3S)-3-(((1S)-3-methyl-1-[(3-methylbutoxy)carbonyl]butyl)carbamoyl)aziridine-2-carboxylic acid
-
(2S,3S)-3-(((1S)-3-methyl-1-[(3-methylbutyl)carbamoyl]butyl)carbamoyl)oxirane-2-carboxylic acid
-
(2S,3S)-3-([(1S)-1-(benzylcarbamoyl)-3-methylbutyl]carbamoyl)oxirane-2-carboxylic acid
-
(2Z)-1,3-bis(2-methoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
(3E)-2-bromo-3-(bromomethylidene)-2-(4-methoxyphenyl)-1-oxa-2lambda4-telluraspiro[3.5]nonane
-
(3E)-2-chloro-3-(chloromethylidene)-2-(4-methoxyphenyl)-1-oxa-2lambda4-telluraspiro[3.5]nonane
irreversible inhibition
(3E)-2-chloro-3-(chloromethylidene)-2-(4-methoxyphenyl)-1-oxa-2lambda4-telluraspiro[3.6]decane
-
(3E)-4-chloro-3-([(2Z)-4-methoxy-1-methylidenepenta-2,4-dien-1-yl](dimethyl)-lambda4-tellanyl)-2-methylbut-3-en-2-ol
-
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-7-[(2,6-dimethylbenzoyl)oxy]-6-oxoheptan-1-aminium trifluoroacetate
-
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalany]amino)-6-oxo-7-[(2,4,6-trimethylbenzoyl)oxy]heptan-1-aminium trifluoroacetate
-
(S)-18-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodo-1H-1,2,3-triazol-1-yl)-12,19-dioxo-3,6,9-trioxa-13-azaicosan-20-yl 2,4,6-trimethylbenzoate
-
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(3-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
-
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
-
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[3-(3-iodophenyl)ureido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 0.013
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[3-(4-iodophenyl)ureido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 0.0035
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(3-iodobenzamido)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 280
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodo-1H-1,2,3-triazol-1-yl)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
-
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodobenzamido)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 310
(S)-3-[(S)-2-[(benzyloxycarbonyl)amino]-3-phenylpropanamido]-7-(6-[3-(3-iodophenyl)ureido]hexanamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
-
(S)-3-[(S)-2-[(benzyloxycarbonyl)amino]-3-phenylpropanamido]-7-(6-[3-(4-iodophenyl)ureido]hexanamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
-
1,1'-[[3-(5-nitroquinolin-8-yl)furan-2,5-diyl]dibenzene-4,1-diyl]diethanone
-
1-(dichloro[(1Z,3E,5Z)-2-chloroocta-1,3,5,7-tetraen-1-yl]-lambda4-tellanyl)-4-methoxybenzene
-
1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]-3-(ethoxycarbonyl)aziridine-2-carboxylic acid
-
1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]aziridine-2,3-dicarboxylic acid
-
3-(([(3S)-3-((N-[(4-chloro-2-fluorophenyl)carbonyl]-3-methyl-L-phenylalanyl)amino)-3-cyanopropyl]oxy)methyl)benzoic acid
IC50: 0.000002 mM
3-(([(3S)-3-cyano-3-([3-methyl-N-(phenylcarbonyl)-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
IC50: 0.0000094 mM
3-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
IC50: 0.0000018 mM
3-(N-benzyloxycarbonylphenylalanylamido)-DL-1-fluoro-2-butanone
irreversible covalent inhibitor
3-([(2R)-2-cyano-2-([3-methyl-N-(2-methyl-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000049 mM
3-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-2,3-dihydro-1H-inden-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000053 mM
3-([(2R)-2-cyano-2-([N-(1,1-dimethyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-3-methyl-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000053 mM
3-methylbutyl N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-prolinate
IC50: 0.367 mM
3-[(5S)-5-cyano-5-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)pentyl]benzoic acid
IC50: 0.000018 mM
4-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
IC50: 0.000005 mM
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-hydroxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
IC50: 0.00175 mM
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
IC50: 0.00168 mM
5,7-dihydroxy-2-(4-hydroxy-3-[7-methoxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
IC50: 0.00055 mM
5-(((2R)-2-cyano-2-[(3-methyl-N-phenyl-L-phenylalanyl)amino]ethoxy)methyl)-2-fluorobenzoic acid
IC50: 0.0000122 mM
5-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)-2-fluorobenzoic acid
IC50: 0.0000041 mM
benzyl N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-alanyl-L-phenylalaninate
IC50: 0.037 mM
benzyl N-([(2R,3R)-3-(butoxycarbonyl)oxiran-2-yl]carbonyl)-L-leucyl-L-prolinate
-
benzyl N-([(2R,3R)-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucinate
-
benzyl N-([(2R,3R)-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucyl-L-prolinate
-
benzyl N-([(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl)-L-leucyl-L-prolinate
-
benzyl N-([(2S,3S)-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucinate
-
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
IC50: 0.000044 mM
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-4-methylpentyl)carbamoyl)-2-methylpropyl]carbamate
IC50: 0.0290 mM
benzyl [(1R)-1-([1-benzyl-2-hydroxy-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
IC50: more than 0.1 mM
benzyl [(1R)-1-([2-hydroxy-1-methyl-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
IC50: 0.0229 mM
benzyl [(1R)-2-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)amino)-1-methyl-2-oxoethyl]carbamate
IC50: 0.00945 mM
benzyl [(1S)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
IC50: 0.00071 mM
benzyloxycarbonyl-L-phenylalanyl-L-phenylalanyl diazomethyl ketone
irreversible covalent inhibitor
benzyloxycarbonyl-phenylalanyl diazomethyl ketone
irreversible covalent inhibitor
ethyl (2R,3R)-3-(((1S)-1-[(4-carbamimidamidobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((1S)-3-methyl-1-[(3-methylbutyl)carbamoyl]butyl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-1-((3-fluorophenethyl)amino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-1-(hexylamino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((3-phenylpropyl)amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((4-phenylbutyl)-amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-(pentan-3-ylamino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl 1-[(2R)-2-((1S)-1-(acetyloxy)-2-[((N-[(2,4-difluorophenyl)carbonyl]-L-phenylalanyl)amino)oxy]-2-oxoethyl)pentanoyl]prolinate
IC50: 4.4 mM
L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl-L-isoleucyl-L-proline methyl ester
activity of caspase 3 is significantly reduced in Dengue virus-infected HepG2 cells treated with cathepsin B or S inhibitor. Treatment with cathepsin B inhibitor also reduces the activity of caspase 9
methyl N-([(2R,3R)-3-([(1R)-1-([(2S)-2-carboxypyrrolidin-1-yl]carbonyl)-3-methylbutyl]carbamoyl)oxiran-2-yl]carbonyl)-L-leucylglycylglycinate
-
methyl N-([(2S,3S)-3-([(1R)-1-([(2S)-2-carboxypyrrolidin-1-yl]carbonyl)-3-methylbutyl]carbamoyl)oxiran-2-yl]carbonyl)-L-leucylglycylglycinate
-
N-(((2R,3R)-3-[(1-methylethyl)carbamoyl]oxiran-2-yl)carbonyl)-L-leucyl-L-proline
-
N-(((2S,3S)-3-[(1-methylethyl)carbamoyl]oxiran-2-yl)carbonyl)-L-leucyl-L-proline
-
N-((1S)-2-[(2R,3R)-2-[(benzyloxy)carbonyl]-3-(ethoxycarbonyl)aziridin-1-yl]-1-methyl-2-oxoethyl)-Na-(tert-butoxycarbonyl)-L-phenylalaninamide
-
N-(3-carboxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
IC50: 0.300 mM
N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
IC50: 0.0026 mM
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
CA-074, 40.4% inhibition at 0.010 mM in cell lysates
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
i.e. CA074Me, inhibits the enzyme and PANC-1 cellular invasiveness, overview
N-([(2R,3R)-1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucyl-L-proline
-
N-([(2R,3R)-3-((5-amino-1-[(4-carbamimidamidobutyl)carbamoyl]pentyl)carbamoyl)oxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
N-([(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl)-L-leucyl-L-arginine
-
N-([(2R,3R)-3-([(1R)-1-([(2S)-2-carboxypyrrolidin-1-yl]carbonyl)-3-methylbutyl]carbamoyl)oxiran-2-yl]carbonyl)-L-leucylglycyl-N-(6-[((2-[6-(diethylamino)-3-(diethyliminio)-3H-xanthen-9-yl]phenyl)carbonyl)amino]hexyl)glycinamide
-
N-([(2R,3R)-3-([(1R)-1-([(2S)-2-carboxypyrrolidin-1-yl]carbonyl)-3-methylbutyl]carbamoyl)oxiran-2-yl]carbonyl)-L-leucylglycyl-N-[6-((5-[(4R)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl)amino)hexyl]glycinamide
-
N-([(2S,3S)-1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucyl-L-proline
-
N-([(2S,3S)-3-((5-amino-1-[(4-carbamimidamidobutyl)carbamoyl]pentyl)carbamoyl)oxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
N-alpha-[(benzyloxy)carbonyl]-N-[(3S)-1-[(2,6-dimethylbenzoyl)oxy]-7-[(6-[(2Z)-2-[(2E,4E)-5-(1-ethyl-3,3-dimethyl-5-sulfo-3H-indolium-2-yl)penta-2,4-dien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
N-benzyl-N,N-diethylethanaminium 2,2,2,4-tetrachloro-2,5-dihydro-2lambda6-[1,2]-oxatellurolinate complex
-
N-[(1R)-1-cyano-2-([3-(2H-tetrazol-2-yl)benzyl]oxy)ethyl]-3-methyl-Na-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalaninamide
IC50: 0.000005 mM
N-[(1S)-3-(benzyloxy)-1-cyanopropyl]-Nalpha-(diphenylacetyl)-3-methyl-L-phenylalaninamide
IC50: 0.0000102 mM
N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-proline
IC50: 0.390 mM
N-[[1-(1,3-benzothiazol-2-yl)piperidin-3-yl]methyl]-8-hydroxy-5-nitroquinoline-7-carboxamide
-
N-[[1-(1,3-benzoxazol-2-yl)piperidin-3-yl]methyl]-8-hydroxy-5-nitroquinoline-7-carboxamide
-
Na-[(benzyloxy)carbonyl]-N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-phenylalaninamide
IC50: 0.021 mM
Nalpha-(tert-butoxycarbonyl)-N-((1S)-2-[(2R,3R)-2-carboxy-3-(ethoxycarbonyl)aziridin-1-yl]-1-methyl-2-oxoethyl)-L-phenylalaninamide
-
Nalpha-[(benzyloxy)carbonyl]-N-[(2R,3S)-2-(carboxyoxy)-4-oxoazetidin-3-yl]-L-phenylalaninamide
IC50: 0.00047 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(3S,4R)-2-oxo-4-phenoxyazetidin-3-yl]-L-phenylalaninamide
IC50: 0.00043 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-4,4-dioxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
IC50: 0.00035 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
IC50: more than 0.00050 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6S)-7-oxo-4-oxa-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
IC50: 0.00176 mM
Nalpha-[(benzyloxy)carbonyl]-N-[(6R)-4-oxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
IC50: 0.0164 mM
RNA interference oligonucleotide shRNA-CTSB2
most efficient inhibition of cathepsin B at both mRNA and protein levels and results in suppressing endometrial cancer growth and development in vivo
-
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
-
-
(1S,3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 2,3,6-trideoxy-3-[([[4-([N-[6-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanoyl]-L-phenylalanyl-L-lysyl]amino)benzyl]oxy]carbonyl)amino]-a-L-lyxo-hexopyranoside
-
a Phe-Lys-para-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin
(2(1H)-pyridinethionato-kappaS2)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
-
-
(3E)-2-bromo-3-(bromomethylidene)-2-(4-methoxyphenyl)-1-oxa-2l4-telluraspiro[3.5]nonane
-
-
(3E)-2-chloro-3-(chloromethylidene)-2-(4-methoxyphenyl)-1-oxa-2l4-telluraspiro[3.5]nonane
-
-
(3E)-4-chloro-3-[dichloro(4-methoxyphenyl)-l4-tellanyl]-2-methylbut-3-en-2-ol
-
-
(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
-
-
(p-methoxyphenylthiolato-S)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
-
-
(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
-
-
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
best performing inhibitor is effective in cell-based in vitro models of tumor invasion, where it significantly abrogates invasion of MCF-10A neoT cells
1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
-
-
1-(dichloro[(1E)-1-chloro-3-methoxyprop-1-en-2-yl]-l4-tellanyl)-4-methoxybenzene
-
-
1-(dichloro[(Z)-2-chloro-2-phenylethenyl]-l4-tellanyl)-4-methoxybenzene
-
bis-vinylic organotellurane, can be a candidate as a starting compound to design more efficient and specific inhibitors for cathepsin B
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
-
-
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
-
-
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
-
-
2-[(6-([3'-(aminomethyl)biphenyl-3-yl]oxy)-3,5-difluoropyridin-2-yl)oxy]benzoic acid
-
-
2A2 monoclonal antibody
-
binds to the epitope EPGYSP sequence, i.e. in the nonapeptide CIAEPGYSP, that is located between amino acid residues 133-138 of cathepsin B in the proximity of the occluding loop, surface plasmon resonance analysis, overview. Binding of 2A2 monoclonal antibody to the cathepsin B/cystatin C complex causes the dissociation of cystatin C from the complex, and binding of the antibody induces a conformational change in cathepsin B, stabilizing its exopeptidase conformation and thus disabling its harmful action associated with its endopeptidase activity
-
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
-
-
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
-
-
7-epiclusianone
-
a prenylated benzophenone isolated from pericarp hexane extract of dried fruits of Rheedia brasiliensis
arsenite
-
i.e. arsenic trioxide, inhibits CatB in glioblastoma cells, 20% inhibition at 0.022 mM, 50% at 0.020 mM
biotin-NH-(CH2)6-NH-Gly-Gly-L-Leu(2S,3S)-trans-epoxysuccinyl-L-Leu-L-Pro-OH
-
selective for cathepsin B over cathepsin L
CA-074-OMe
-
blocks cysteine cathepsins in addition to CatB in in primary human antigen-presenting cells
CA074
-
high specificity, 34000fold more effective on enzyme than on cathepsin X
Cabin-1
-
i.e. LGPVTQE, peptide from human apolipoproteinA-1, 50% inhibition at 0.45 mM
Cabin-2
-
i.e. VLQSSGLYS, peptide from human immunoglobulin G gamma chain, 50% inhibition at 0.5 mM
Cabin-2(1-8)
-
i.e. VLQSSGLY, peptide from human immunoglobulin G gamma chain, 50% inhibition at 0.004 mM
Cabin-3
-
i.e. VVSVLT, peptide from human immunoglobulin G gamma chain, 50% inhibition at 0.02 mM
Cabin-4
-
i.e. LVYDAY, peptide from human transferrin, 50% inhibition at 0.0005 mM
chagasin
-
an inhibitor from Trypanosoma cruzi, Three residues from chagasin, Leu65, Gly66, and Ala67, interact with cathepsin B residues Gly74, Gly73, and Asn72, binding mode and structure of wild-type enzyme and non-glycosylated S115A and H110A/S115A cathepsin B mutants, modeling, overview
-
chloro[diphenyl[4-(2-phenyl-1,3-dioxolan-2-yl)phenyl]phosphine-kappaP]gold(I)
-
-
DCG-04
-
an E-64-type inhibitor, inhibits both mature cathepsin B and its zymogen
E-64d
-
i.e. (L-3-trans-ethoxycarbonyloxirane-2-carbonyl)-L-leucine(3-methylbutyl)amide
E64c
-
the (2S,3S)-3-(L-[N-(3-methylbutyl)amino]leucyl) side chain binds at the S1 and S3 subsites
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
-
Fmoc-Tyr-Ala-CHN2
-
FYAD, an irreversible inhibitor of cathepsin B, induces apoptosis of neuroblastoma cells but not of other tumor cells. Inhibitors that affect only one enzyme or fail to maintain inhibition of both cathepsins B and L do not induce apoptosis of these cells, overview
garciniaphenone
-
a prenylated benzophenone isolated from pericarp hexane extract of dried fruits of Rheedia brasiliensis
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
methoxy-Gly-Gly-L-Leu(2S,3S)-trans-epoxysuccinyl-L-Leu-L-Pro-OH
-
selective for cathepsin B over cathepsin L
N-benzyl-N,N-diethylethanaminium 1-trichloro-4-chloro-2,3-dihydro-2-oxatellurophene
-
-
N-[2-[(3-carboxyphenyl)methoxy]-1-(S)-cyanoethyl]-3-methyl-Nalpha-(2,4-difluorobenzoyl)-L-phenylalaninamide
-
50% inhibition at 6.8 nM, selective for cathepsin B
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
NAMI-A
-
i.e. [imidazoleH][trans-Ru(DMSO)(imidazole)Cl4], an antimetastatic compound
-
NC-2300
-
i.e. monosodium (2S,3S)-3-[[(1S)-1-isobutoxymethyl-3-methylbutyl]carbamoyl]oxirane-2-carboxylate, a cysteine cathepsin inhibitor
Os(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
-
i.e. OSPTAC
-
penetratin HP-CO-(CH2)5-NH-Gly-Gly-L-Leu(2S,3S)-trans-epoxysuccinyl-L-Leu-L-Pro-OH
-
selective for cathepsin B over cathepsin L, penetratin moiety allows penetration of cell membrane, almost complete inactivation at 300 nM, at 10 nM block of about 60% of intracellular enzyme activity
rhodamine B-NH-(CH2)6-NH-Gly-Gly-L-Leu(2S,3S)-trans-epoxysuccinyl-L-Leu-L-Pro-OH
-
selective for cathepsin B over cathepsin L
Ru(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
-
i.e. RAPTA-C
-
sodium chloro[[4,4',4''-(phosphinidyne-kappaP)tris[benzenesulfonato]]aurate]
-
-
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
-
-
triethylphosphine(2,3,4,6-tetra-O-acetyl-beta-1-D-thiopyranosato-S)gold(I)
-
auranofin
Z-Arg-Leu-Arg-alpha-aza-glycyl-Ile-Val-OMe
-
i.e. ZRLR, a highly selective cathepsin B inhibitor, cell-permeable, almost complete inhibition at 0.0001 mM
Z-Phe-Gly-NHO-Bz
-
an inhibitor of both cathepsins B and L, causes death of many cell types
[(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)Pd(1,3,5-triaza-7-phosphoadamantane)Cl]
-
-
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
-
-
[2-(mercapto-kappaS)benzoato(2-)-kappaO][2-[(2-pyridinyl-kappaN)methyl]phenyl-kappaC]Au(III)
-
-
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
i.e. DOFA, a reversible, double-headed competitive inhibitor of cathepsin B, the dioxothiazolidine head of the compound sterically hinders binding of the C-terminal residue of substrates resulting in inhibition of the exopeptidase activity of cathepsin B in a physiopathologically relevant pH range, competitive versus substrates ortho-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys-Nepsilon-2,4-dinitrophenyl-OH and carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin, structure and enzyme docking, overview
[Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phospatatricyclo[3.3.1.1]decane)Cl2]
-
-
-
[Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)2Cl]PF6
-
-
-
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl2]OTf
-
-
-
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl](OTf)PF6
-
-
-
[L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester
-
CA-074-Me, specific inhibitor
[N-(L-3-trans-propylcarbamoyl oxirane-2-carbonyl)-L-isoleucyl-L-proline]
-
specific inhibitor
[Pd2((R)-3-isopropyl-1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,1'-bis(diphenylphosphino)ferrocene)Cl2]
-
-
[Pd2((R)-3-isopropyl-1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
-
-
[Pd2((S)-3-isopropyl-1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
-
-
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,1'-bis(diphenylphosphino)ferrocene)Cl2]
-
-
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
-
-
[Ru(II)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatatricyclo[3.3.1.1]decane)Cl2]
-
-
-
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
-
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 630
CA-074
i.-e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline and its derivates, irreversible covalent inhibitor
CA074
treatment of colorectal cancer cells cells with the cathepsin B inhibitor Ca074 leads to invasiveness of human CRC cells
E64d
substituting ethyl(methyl) sulfane for 2-methylbutane (R2) of E64d improves the inhibitory activity and selectivity for cathepsin B inhibition
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
E-64, 63.2% inhibition at 0.010 mM in cell lysates
CA-074
-
a cathepsin B inhibitor significantly attenuates the ratio of hypodiploid and apoptotic cells, partially blocks caspase 3 activation and inhibits reduction of cell viability induced by emodin
CA-074
-
cathepsin B inhibitor III, i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline
CA-074-Me
-
cathepsin B inhibition decreases hepatic stellate cell proliferation and the expression of phenotypic markers of hepatic stellate cell activation, and it down-regulate alpha-smooth musle actin mRNA and protein levels in LX2 cells, overview. Reduction of CtsB and/or CtsD levels by siRNA decreases cell proliferation, compared to control siRNA-transfected LX2 cells
CA-074-Me
-
i.e. propylcarbonyl-L-trans-epoxysuccinyl-Ile-Pro-OH, enzyme binding structure at the active site cleft, modelling, overview
CA-074-Me
-
i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester
CA-074-Me
-
suppresses microglia conditioned culture medium-induced glioma cell death
CA-074Me
-
cathepsin B specific inhibitor, cathepsin B inhibitor IV, i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester
cystatin C
-
an endogenous inhibitor of cysteine cathepsins, expression patterns of cathepsin B and cystatin C
-
cystatin C
-
Porphyromonas gingivalis interrupts the interaction of cathepsin B with its inhibitor cystatin
-
additional information
concanamycin A is an indirect inhibitor by specific inhibiton of VATPase
-
additional information
-
analysis of further dipeptidyl nitriles as selective inhibitors
-
additional information
-
alpha-1-antitrypsin aerosolised augmentation abrogates neutrophil elastase-induced expression of cathepsin B in vivo and in vitro
-
additional information
-
inhibitory activities of N-cyano-tetrahydro-pyridazine derivatives, docking studies, overview
-
additional information
-
ruthenium(II)-arene compounds behave as powerful inhibitors
-
additional information
-
95-100% enzyme inhibition is required to cause neuroblastoma cell death
-
additional information
-
continuous and binary quantitative structure-activity relationship, QSAR, models to classify cathepsin B inhibition activities of small molecules, high throughput screening, detailed overview
-
additional information
-
correlation between cathepsin B inhibition and cytotoxicity for a series of palladacycles, that show in vitro activity as cytotoxic agents on A2780/S cells and also as cathepsin B inhibitors, synthesis and crystal structure of palladacycles, overview
-
additional information
-
design and synthesis of hypervalent tellurium compounds, and irreversible inhibition of cathepsins B by hypervalent tellurium compounds, e.g. organotellurium(IV) compounds, i.e. organotelluranes, that react with thiols forming mixed dichalcogenides, with a tellurium-sulfur bond. Mechanisms for two- and one-step irreversible enzyme inhibition, overview
-
additional information
-
development of cathepsin inhibitors and structure-based design of cathepsin B-specific inhibitor, binding mode at the active site and structure-activity relationship, overview. Quantitative assesment of inhibitor binding at the SN-site of cathepsin B, overview
-
additional information
-
inhibition of cathepsin B increases cell viability in the presence of imatinib
-
additional information
-
screening of pyrimidotriazine-diones and pyrazole sulfonamides as cathepsin B inhibitors, structure-function relationship, overview. Pyrimidotriazine-dione inhibitors, along with several structurally unrelated compounds, are inactive in presence of the reductant cysteine or DTT, thus the inhibitors are acting through a DTT-dependent redox cycling mechanism, rather than through direct inhibition of the enzyme
-
additional information
-
synthesis and screening of organometallic compounds of general formula [(arene)M(PTA)nXm]Y with metal M = Ru2+, Os2+, Rh3+, or Ir3+, and X = Cl or mPTA, and Y = OTf, PF6, for cytotoxicity and ability to inhibit cathepsin B in vitro, overview. Thermodynamics in solution for metal complexes adducts with N-acetyl-L-cysteine-N'-methylamide, inhibitor binding kinetics, structure-function relationship, overview
-
additional information
-
not inhibited by oryzacystatin-1 N-terminal deletion, reverse mutant 1 (T30I), reverse mutant 2 (Q97L), and reverse mutant 3 (T30I, Q97L)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
emodin
-
i.e. 1,3,8-trihydroxy-6-methylanthraquinone, emodin at apoptosis-inducing concentrations causes expression and activation of cathepsin B protein
heparin
-
at pH 8.0, heparin increases the half-life of wild type enzyme from 84 sec to 433 sec
imatinib
-
activates cathepsin B and mediates its redistribution to the cytoplasm
interleukin-6
-
IL-6, in the presence of soluble form of IL-6 receptor, sIL-6R, enhances cathepsin B expression and activity via the Cav-1-JNK-AP-1 pathway in fibroblasts of the gingiva
lipopolysaccharide
-
activates a Cat-B-dependent programmed death response in endothelial cells that is independent of both myeloid differentiation factor 88 and Toll-like receptor-associated interferon-inducing factor, is blocked by both Fas-associated death domain protein and phosphatidylinositol 3 kinase. Activates both caspase- and Cat B-dependent death pathways in presence of phosphatidylinositol 3 kinase inhibitor LY294002 or the inflammatory cytokine interferon-gamma
tumor necrosis factor-related apoptosis inducing ligand
-
an increase in the cellular amount of active 31 kDa cathepsin B is observed after tumor necrosis factor-related apoptosis inducing ligand treatment (100 ng/ml)
-
additional information
-
cell treatment with attenuated bacillus Calmette-Guerin increases enzyme expression and activity
-
additional information
-
activator buffer contains 5 mM EDTA, 10 mM DTT, pH 5.2
-
additional information
-
neutrophil elastase induces expression of cathepsin B in vivo and in vitro
-
additional information
-
Porphyromonas gingivalis strain 381 or its lipopolysaccharides increases the expression of cathepsin B 3fold in oral epithelial cells, while the expression of the cathepsin B specific inhibitor cytsatin is reduced 5fold
-
additional information
-
knockdown of cellular FLICE inhibitory protein potentiates the caspase-dependent pathway but does not activate the Cat B-dependent death response. Also knockdown of either myeloid differentiation factor 88 or Toll-like receptor-associated interferon-inducing factor expression does not affect the LPS-triggered Cat B death response in Fas-associated death domain protein-deficient human umbilical vein endothelial cells
-
additional information
-
p53-dependent lysosomal destabilization and cathepsin B activation contribute for increased sensitivity of p21-deficient cells to embelin with enhanced caspase 9 and caspase 3 activation
-
additional information
-
phagocytosis of crystalline silica induces lysosomal destabilization and subsequent release of cathepsin B into the cytoplasm, leading to NALP3 activation. Release of specific proteases such as cathepsin B seems to be causally related to inflammasome activation
-
additional information
-
pharmacological or short hairpin RNA-mediated inhibition of tyrosine kinase BCR-ABL triggers lysosomal membrane permeabilization that culminates in activation and redistribution of cathepsin B into the cytoplasm of chronic myelogenous leukemia cells, in which it triggers directly BCR-ABL degradation
-
additional information
-
the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.212
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.075
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.0177
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-P-OH
-
pH 6.0, 37°C
0.0038
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37°C
0.0179
Abz-FRA-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37°C
0.0328
Abz-FRF-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37°C
0.015
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.032
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.3
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumaryl-7-amide
-
22°C, value is quite stable in the range of pH 4.0 to pH 7.8
0.055
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin
-
pH 6.5, recombinant enzyme
1.2
Cbz-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0029
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)serine-4-methylcoumarin-7-amide
-
pH 6.0
0.0029
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)threonine-4-methylcoumarin-7-amide
-
pH 6.0
0.047
epsilon-aminocaproic acid-L-Leu-L-(O-methyl)-tyrosine-4-methylcoumarin-7-amide
-
pH 6.0
0.01
epsilon-aminocaproic acid-L-Leu-L-(S-benzyl)cysteine-4-methylcoumarin-7-amide
-
pH 6.0
0.008
o-aminobenzoic acid-L-Lys-L-Leu-Gly-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.017
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.015
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.019
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.024
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.033
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.0125
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, wild-type enzyme
0.013
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H110A
0.014
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H111A in presence of heparin
0.016
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H111A
0.043
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, wild-type enzyme in presence of heparin
0.047
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H110A in presence of heparin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
67
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
115
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp: Asn > Tyr, His, Leu, Trp > Ser, Phe, Pro Lys > Asp, Ala
additional information
Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp
-
kcat/Km for Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp: Asn > Tyr, His, Leu, Trp > Ser, Phe, Pro Lys > Asp, Ala
additional information
Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp: Asn > Trp, Tyr, Ala > Ser, Phe > His, Lys > Asp, Leu, Pro
additional information
Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp
-
kcat/Km for Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp: Asn > Trp, Tyr, Ala > Ser, Phe > His, Lys > Asp, Leu, Pro
additional information
Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala_X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp: Leu, Tyr > Phe, Ala, Ser, Pro > His, Lys > Asn, Asp
additional information
Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp
-
kcat/Km for Abz-Ala_X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp: Leu, Tyr > Phe, Ala, Ser, Pro > His, Lys > Asn, Asp
additional information
Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp: Phe, Leu > Arg > Ala > Pro
additional information
Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp
-
kcat/Km for Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp: Phe, Leu > Arg > Ala > Pro
additional information
Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp
kcat/Km for Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp: Leu, Phe, Trp > Ser, Asn, Asp, Ala > Tyr, His, Lys
additional information
Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp
-
kcat/Km for Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp: Leu, Phe, Trp > Ser, Asn, Asp, Ala > Tyr, His, Lys
additional information
Dnp-Gly-Phe-Arg-Trp-X-OH
kcat/Km for Dnp-Gly-Phe-Arg-Trp-X-OH: Phe > Tyr, Ile > Leu > Cval > Arg > Lys, Pro > Gln, Ser > Asp, Glu, Ala
additional information
Dnp-Gly-Phe-Arg-Trp-X-OH
-
kcat/Km for Dnp-Gly-Phe-Arg-Trp-X-OH: Phe > Tyr, Ile > Leu > Cval > Arg > Lys, Pro > Gln, Ser > Asp, Glu, Ala
additional information
Dnp-Gly-Phe-Arg-X-Trp-OH
kcat/Km for Dnp-Gly-Phe-Arg-X-Trp-OH: Phe > Ser > Leu > Ala > Ile > Tyr, Val > Gln > Lys > Gly > His, Asp > Arg > Glu
additional information
Dnp-Gly-Phe-Arg-X-Trp-OH
-
kcat/Km for Dnp-Gly-Phe-Arg-X-Trp-OH: Phe > Ser > Leu > Ala > Ile > Tyr, Val > Gln > Lys > Gly > His, Asp > Arg > Glu
additional information
Dnp-Gly-Phe-X-Phe-Trp-OH
kcat/Km for Dnp-Gly-Phe-X-Phe-Trp-OH: Arg > Lys > Phe > Leu > Val > His, Gln > Ser > Gly Ala > Glu > Tyr > Ile, Asp
additional information
Dnp-Gly-Phe-X-Phe-Trp-OH
-
kcat/Km for Dnp-Gly-Phe-X-Phe-Trp-OH: Arg > Lys > Phe > Leu > Val > His, Gln > Ser > Gly Ala > Glu > Tyr > Ile, Asp
additional information
Dnp-Gly-X-Arg-Phe-Trp-OH
kcat/Km for Dnp-Gly-X-Arg-Phe-Trp-OH: Phe > Tyr > Lys > Val > Ala > Ile > Ser, Pro > His > Leu > Arg > Asp, Glu
additional information
Dnp-Gly-X-Arg-Phe-Trp-OH
-
kcat/Km for Dnp-Gly-X-Arg-Phe-Trp-OH: Phe > Tyr > Lys > Val > Ala > Ile > Ser, Pro > His > Leu > Arg > Asp, Glu
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000052
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-7-[(2,6-dimethylbenzoyl)oxy]-6-oxoheptan-1-aminium trifluoroacetate
pH 6, 37°C
0.00008
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalany]amino)-6-oxo-7-[(2,4,6-trimethylbenzoyl)oxy]heptan-1-aminium trifluoroacetate
pH 6, 37°C
0.00035
(S)-18-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodo-1H-1,2,3-triazol-1-yl)-12,19-dioxo-3,6,9-trioxa-13-azaicosan-20-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.00037
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(3-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.000181
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.002
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.001
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodo-1H-1,2,3-triazol-1-yl)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.185
N-(1-cyanocyclopropyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.128
N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.00012
N-alpha-[(benzyloxy)carbonyl]-N-[(3S)-1-[(2,6-dimethylbenzoyl)oxy]-7-[(6-[(2Z)-2-[(2E,4E)-5-(1-ethyl-3,3-dimethyl-5-sulfo-3H-indolium-2-yl)penta-2,4-dien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxoheptan-3-yl]-L-phenylalaninamide
pH 6, 37°C
0.035
N-benzyl-N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.156
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.181 - 0.25
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
0.373
4-nitronaphthalen-1-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.0000876
canecystatin-1
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.00000058
canecystatin-4
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.42
di-(2-ethylhexyl)phthalate
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.64
dibutyl phthalate
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.13 - 0.132
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
0.0011
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.000064
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.0000785
oryzacystatin-1
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.0000112
oryzacystatin-1 clone A10
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.0048 - 0.0113
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
0.1675
[N-benzyl-N,N-diethylethanaminium]2 hexachloro-lambda6-tellane
-
pH 6.5, 25°C
0.181
2-methyl-5-nitroquinolin-8-ol
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.469
2-methyl-5-nitroquinolin-8-ol
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.118
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.323
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.142
8-hydroxy-5-nitroquinoline-2-carbonitrile
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.214
8-hydroxy-5-nitroquinoline-2-carbonitrile
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.19
N-(cyanomethyl)-5-nitroquinoline-8-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.24
N-(cyanomethyl)-5-nitroquinoline-8-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.16
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.201
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.182
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.185
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.181
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.25
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.019
(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.079
(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.126
([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.172
([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.005
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.426
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.034
1-(4-nitronaphthalen-1-yl)pyrrolidine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.17
1-(4-nitronaphthalen-1-yl)pyrrolidine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.032
2-bromo-4-nitronaphthalen-1-amine
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.212
2-bromo-4-nitronaphthalen-1-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.085
4-(4-nitronaphthalen-1-yl)morpholine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.289
4-(4-nitronaphthalen-1-yl)morpholine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.147
4-nitronaphthalen-1-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.217
4-nitronaphthalen-1-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.072
5,7-dinitroquinolin-8-ol
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.146
5,7-dinitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.311
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.364
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.143
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.162
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.047
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.107
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.203
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.243
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.154
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.198
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.117
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.136
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.024
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.207
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.155
8-(morpholin-4-yl)-5-nitroquinoline
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.18
8-(morpholin-4-yl)-5-nitroquinoline
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.117
8-hydroxy-5-nitroquinoline-7-carboxylic acid
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.221
8-hydroxy-5-nitroquinoline-7-carboxylic acid
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.13
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.132
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.038
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.162
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.129
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.156
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.105
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.155
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.349
N-benzyl-5-nitroquinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.364
N-benzyl-5-nitroquinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.196
N-benzyl-N-methyl-5-nitroquinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.242
N-benzyl-N-methyl-5-nitroquinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.0048
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 4.5, 25°C, competitive versus carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin
0.0067
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 4.5, 25°C, competitive versus ortho-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys-Nepsilon-2,4-dinitrophenyl-OH
0.0113
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 6.0, 25°C, competitive versus carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin
additional information
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
value above 0.01
additional information
additional information
-
kinetic mechanism of inhibition by [2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
additional information
additional information
-
second-order inactivation rate constants for cathepsin B, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000002
3-(([(3S)-3-((N-[(4-chloro-2-fluorophenyl)carbonyl]-3-methyl-L-phenylalanyl)amino)-3-cyanopropyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.000002 mM
0.0000094
3-(([(3S)-3-cyano-3-([3-methyl-N-(phenylcarbonyl)-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.0000094 mM
0.0000018
3-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.0000018 mM
0.0000049
3-([(2R)-2-cyano-2-([3-methyl-N-(2-methyl-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000049 mM
0.0000053
3-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-2,3-dihydro-1H-inden-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000053 mM
0.0000053
3-([(2R)-2-cyano-2-([N-(1,1-dimethyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-3-methyl-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000053 mM
0.367
3-methylbutyl N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-prolinate
Homo sapiens
IC50: 0.367 mM
0.000018
3-[(5S)-5-cyano-5-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)pentyl]benzoic acid
Homo sapiens
IC50: 0.000018 mM
0.000005
4-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.000005 mM
0.00175
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-hydroxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00175 mM
0.00168
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00168 mM
0.00055
5,7-dihydroxy-2-(4-hydroxy-3-[7-methoxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00055 mM
0.0000122
5-(((2R)-2-cyano-2-[(3-methyl-N-phenyl-L-phenylalanyl)amino]ethoxy)methyl)-2-fluorobenzoic acid
Homo sapiens
IC50: 0.0000122 mM
0.0000041
5-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)-2-fluorobenzoic acid
Homo sapiens
IC50: 0.0000041 mM
0.037
benzyl N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-alanyl-L-phenylalaninate
Homo sapiens
IC50: 0.037 mM
0.000044
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.000044 mM
0.029
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-4-methylpentyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.0290 mM
0.1
benzyl [(1R)-1-([1-benzyl-2-hydroxy-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: more than 0.1 mM
0.0229
benzyl [(1R)-1-([2-hydroxy-1-methyl-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.0229 mM
0.00945
benzyl [(1R)-2-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)amino)-1-methyl-2-oxoethyl]carbamate
Homo sapiens
IC50: 0.00945 mM
0.00071
benzyl [(1S)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.00071 mM
0.00002409
ethyl (2S,3S)-3-(((S)-1-((3-fluorophenethyl)amino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00000427
ethyl (2S,3S)-3-(((S)-1-(hexylamino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00000716
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((3-phenylpropyl)amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00002368
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((4-phenylbutyl)-amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00007427
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-(pentan-3-ylamino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
4.4
ethyl 1-[(2R)-2-((1S)-1-(acetyloxy)-2-[((N-[(2,4-difluorophenyl)carbonyl]-L-phenylalanyl)amino)oxy]-2-oxoethyl)pentanoyl]prolinate
Homo sapiens
IC50: 4.4 mM
0.3
N-(3-carboxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.300 mM
0.0026
N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.0026 mM
0.447
N-(3-methyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.447 mM
0.074
N-(3-phenyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.074 mM
0.000005
N-[(1R)-1-cyano-2-([3-(2H-tetrazol-2-yl)benzyl]oxy)ethyl]-3-methyl-Na-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalaninamide
Homo sapiens
IC50: 0.000005 mM
0.0000102
N-[(1S)-3-(benzyloxy)-1-cyanopropyl]-Nalpha-(diphenylacetyl)-3-methyl-L-phenylalaninamide
Homo sapiens
IC50: 0.0000102 mM
0.39
N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-proline
Homo sapiens
IC50: 0.390 mM
0.021
Na-[(benzyloxy)carbonyl]-N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-phenylalaninamide
Homo sapiens
IC50: 0.021 mM
0.00047
Nalpha-[(benzyloxy)carbonyl]-N-[(2R,3S)-2-(carboxyoxy)-4-oxoazetidin-3-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00047 mM
0.00043
Nalpha-[(benzyloxy)carbonyl]-N-[(3S,4R)-2-oxo-4-phenoxyazetidin-3-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00043 mM
0.00035
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-4,4-dioxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00035 mM
0.0005
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: more than 0.00050 mM
0.00176
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6S)-7-oxo-4-oxa-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00176 mM
0.0164
Nalpha-[(benzyloxy)carbonyl]-N-[(6R)-4-oxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.0164 mM
0.00012
(2(1H)-pyridinethionato-kappaS2)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
Homo sapiens
-
-
0.0009
(chloro)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN1] oxorhenium(V)
Homo sapiens
-
-
0.00126
(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.0886
(p-methoxyphenylthiolato-S)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.00651
(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
Homo sapiens
-
-
0.000032
1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.00011
1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.00004
1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.000032
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
Homo sapiens
-
pH 5.5, 30°C
0.000053
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
Homo sapiens
-
pH 5.5, 30°C
0.000023
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.1
2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
Homo sapiens
-
IC50 above 0.1 mM, in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.013
2-pentyl-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.1
2-phenylisothiazol-3(2H)-one
Homo sapiens
-
IC50 above 0.1 mM, in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.00126
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl furan-2-carboxylate
Homo sapiens
-
-
0.00044
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.00069
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.00175
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl furan-2-carboxylate
Homo sapiens
-
-
0.00199
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.0041
5-chloro-2-(2-chloro-4,5-dimethoxyphenethyl)isothiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.042
5-chloro-2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0073
5-chloro-2-pentyl-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.013
5-chloro-2-phenylisothiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0004
aceto[2,6-bis[(butylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
Homo sapiens
-
-
0.01346
aceto[2,6-bis[(methylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
Homo sapiens
-
-
0.00274
aceto[2,6-bis[(phenylthio-kappaS)methyl]phenyl-kappaC]-, (SP-4-3)Pd(II)
Homo sapiens
-
-
0.046
benzylamido-L-trans-epoxysuccinyl-Ile-O-benzyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000029
benzylamido-L-trans-epoxysuccinyl-Ile-Pro-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000038
CA-074-Me
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00012
CA030
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000088
chloro-[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.23
chloro[diphenyl[4-(2-phenyl-1,3-dioxolan-2-yl)phenyl]phosphine-kappaP]gold(I)
Homo sapiens
-
-
0.0028
CID 11834381
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0331
CID 11834389
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0032
CID 11834392
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.046
CID 1506381
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0071
CID 2212050
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0115
CID 286532
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0094
CID 2998380
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
CID 3236798
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0007
CID 3240114
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00044
CID 3241895
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00085
CID 3243025
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00026
CID 3243128
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0086
CID 3243168
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0184
CID 3250046
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0223
CID 3685806
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00225
CID 5293426
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0339
CID 573353
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
CID 646525
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0123
CID 646749
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000071
CID 647501
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
CID 647599
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0064
CID 648315
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00175
CID 651936
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000072
CID 653297
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.045
CID 653316
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00092
CID 653862
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
CID 654815
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0096
CID 655490
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0067
CID 658111
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0197
CID 658152
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0089
CID 658724
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.04
CID 658964
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0385
CID 660829
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000046
CID 66541
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
CID 665480
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0142
CID 714967
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0042
CID 794694
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0372
CID 971438
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00129
diaceto[2-[(2-pyridinyl-kappaN)methyl]-phenyl-kappaC]Au(III)- (SP-4-3)
Homo sapiens
-
-
0.0153
ethoxy-L-trans-epoxysuccinyl-Gly-Pro-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000023
ethoxy-L-trans-epoxysuccinyl-Ile-Ala-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
ethoxy-L-trans-epoxysuccinyl-Ile-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.024
ethoxy-L-trans-epoxysuccinyl-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00041
ethoxy-L-trans-epoxysuccinyl-Thr-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.014
ethyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0085
methyl 3-(4,5-dichloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.012
methyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.011
methyl 3-(5-chloro-4-methyl-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.011
methyl 4-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)butanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.024
methyl 6-(3-(propyldisulfanyl)acrylamido)hexanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.000046
N-phenyl-3-(propyldisulfanyl)-3-chloro-acrylamide
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.012
N-phenyl-3-(propyldisulfanyl)acrylamide
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0091
propylcarbonyl-L-trans-epoxysuccinyl-Ile-O-benzyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.068
propylcarbonyl-L-trans-epoxysuccinyl-Ile-Pro-O-methyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.353
Ru(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
Homo sapiens
-
pH 6.0, 30°C
-
0.075
sodium chloro[[4,4',4''-(phosphinidyne-kappaP)tris[benzenesulfonato]]aurate]
Homo sapiens
-
-
0.000038
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
Homo sapiens
-
pH 5.5, 30°C
0.000011
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
Homo sapiens
-
pH 5.5, 30°C
0.00018
[2-(mercapto-kappaS)benzoato(2-)-kappaO][2-[(2-pyridinyl-kappaN)methyl]phenyl-kappaC]Au(III)
Homo sapiens
-
-
0.5
[Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phospatatricyclo[3.3.1.1]decane)Cl2], [Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)2Cl]PF6
Homo sapiens
-
above, pH 6.0, 30°C
-
0.349
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl2]OTf
Homo sapiens
-
pH 6.0, 30°C
-
0.5
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl](OTf)PF6
Homo sapiens
-
above, pH 6.0, 30°C
-
0.4
[Ru(II)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatatricyclo[3.3.1.1]decane)Cl2]
Homo sapiens
-
above, pH 6.0, 30°C
-
0.14
di-(2-ethylhexyl)phthalate
Homo sapiens
-
recombinant enzyme, in Hank's balanced salt solution containing 2 mM L-cysteine, pH 7.0, at 37°C
0.38
di-(2-ethylhexyl)phthalate
Homo sapiens
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.23
dibutyl phthalate
Homo sapiens
-
recombinant enzyme, in Hank's balanced salt solution containing 2 mM L-cysteine, pH 7.0, at 37°C
0.42
dibutyl phthalate
Homo sapiens
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
additional information
additional information
Homo sapiens
-
IC50 values for cell proliferation of prenylated benzophenones from Rheedia brasiliensis, overview
-
additional information
additional information
Homo sapiens
-
IC50 values of palladacycles in cytotoxicity assay, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00042
7500
-
cathepsin B in epithelial cells infected with and induced by Porphyromonas gingivalis srain 381 lipopolysaccharides
additional information
0.00042
secreted protein in cell culture, in the presence of 0.01 mM CA-074
0.00042
secreted protein in cell culture, in the presence of 0.01 mM CA-074 Me
additional information
total cathepsin B activity and content calculated per gram of DNA are higher in Wharton's jelly than in the umbilical cord vessels
additional information
-
total cathepsin B activity and content calculated per gram of DNA are higher in Wharton's jelly than in the umbilical cord vessels
additional information
-
enzyme activity in gingival crevicular fluid of left and right sides, overview
additional information
-
activity of cathepsin B significantly increases with age
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 7.4
-
activity measurement range, vesicle-associated cathepsin B activity is increased 1300fold at acidic pH values compared to physiological pH 7.4, cathepsin B activity in cell extract is increased 33fold at pH 5.6 versus pH 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
22
37
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 5.9
-
multiple forms of cathepsin B derived peptides with pIs ranging from a pI of 5.5 to a pI of 5.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest expression in Wharton's jelly and the lowest in the umbilical cord arteries
-
tubular adenomas with low grade dysplasia and tubulovillous adenomas with high grade dysplasia
-
cathepsin B is expressed in cerebral aneurysms and aneurysmal walls, and promotes the progression of cerebral aneurysms
-
endometrial glands and epithelial cells, and also stroma
-
of a more aggressive tumor type, cathepsin B is most common in the intestinal type tumors infiltrating the whole gastric wall
-
up-regulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells resulting, at least in part, from the activation of the transcription factor NF-kappaB
-
epithelial, cathepsin B is significantly higher in patients older than compared with patients younger than 57 years of age
-
enzyme before and after canine extraction, force application reduces the enzyme activity in gingival crevicular fluid to 41.5% of maximal activity
additional information
-
from patients with alpha1-antitrypsin deficiency, pneumonia and healthy individuals
-
myeloid and plasmacytoid dendritic cells differ in their cathepsin distribution, overview
-
expression of cathepsins B, L and S gradually increases in the progression from benign astrocytoma to the malignant glioblastoma
-
the most frequent malignant brain tumor in adults, increased expression of cathepsin B compared to healthy astrocytes, immunohistochemic and expression analysis, overview
-
-
34990, 36626, 36634, 36650, 650355, 650517, 652163, 653026, 673671, 681231, 699388, 701102, 708264, 708641, 717583, 718179
-
of ovarian tumors, the levels of CatB depend on the tumor subtypes, overview. CatB levels are signifiantly higher in cystic fluid of malignant serous tumors compared to those found in benign serous tumors
-
enzyme levels in serum from patients with colorectal, gastric, hepatocellular, or pancreatic cancers and gastric epithelial dysplasia, overview
-
extracellular, secreted enzyme, the enzyme content is higher in blood from patients with pelvic inflammatory disease compared to control healthy women, overview
additional information
-
immunohistochemic expression analysis in cerebral arterial walls and aneurysms, overview
additional information
-
JNK inhibition, but not p44/42 MAPK inhibition, significantly diminishes interleukin-6/soluble form of IL-6 receptor-induced cathepsin B production
additional information
-
quantitative determination of cathepsin B tissue distribution
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of the lysosomal fraction, co-localization of active cathepsin B and its cell surface binding partners, S100A/p11 of the annexin II heterotetramer, to caveolae of human umbilical vein endothelial cells and colorectal carcinoma cells
-
phagocytosis of crystalline silica induces lysosomal destabilization and subsequent release of cathepsin B into the cytoplasm, leading to NALP3 activation
-
cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively
additional information
-
cathepsin B is secreted as an inactive precursor form, up-regulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells resulting, at least in part, from the activation of the transcription factor NF-kappaB
-
-
under certain conditions cathepsin-B may be secreted extracellularly as a pro-enzyme that requires proteolytic activation
-
-
-
36634, 678699, 680996, 695447, 696631, 698029, 699130, 699208, 699337, 707625, 707967, 707971, 708035, 708258, 708264, 708275, 708277, 708376, 708482, 708641, 709347, 709771, 709916, 710205, 710254
-
cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively
-
phagocytosis of crystalline silica induces lysosomal destabilization and subsequent release of cathepsin B into the cytoplasm, leading to NALP3 activation
additional information
Alexa Fluor 488 labeled intracellular cathepsin B is localized in vesicle-like structures in the perinuclear region of HUVECs
-
additional information
-
Alexa Fluor 488 labeled intracellular cathepsin B is localized in vesicle-like structures in the perinuclear region of HUVECs
-
additional information
-
the enzyme is secreted to blood or body fluids in patients with cancers such as leptomeningeal metastasis or hepatocellular carcinoma
-
additional information
-
imatinib mediates redistribution of cathepsin B, Iiatinib or BCR-ABL knockdown induces lysosomal membrane permeabilization that culminates in activation and redistribution of cathepsin B into the cytoplasm of chronic myelogenous leukemia cells
-
additional information
-
release of specific proteases such as cathepsin B seems to be causally related to inflammasome activation
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
physiological function
additional information
malfunction
Cathepsin B silencing by RNAi in human colorectal cancer (CRC) cells inhibits their growth in soft agar, as well as their invasion capacity, tumoral expansion, and metastatic spread in immunodeficient mice
malfunction
higher levels of the cell cycle inhibitor p27Kip1 are observed in cathepsin B-deficient tumors as well as an increase in cyclin B1
malfunction
reduced cathepsin B expression using RNA interference mimicks pharmacological inhibition of the enzyme and confirms the contribution of cathepsin B to apoptotic events induced by Dengue virus in HepG2 cells
physiological function
cathepsin B activates both caspase-9 and caspase-3
physiological function
extracellular cathepsin B is involved in cell invasion whereas intracellular cathepsin B controls tumoral properties of colorectal cancer cells
physiological function
cathepsin B can modulate autophagy processes in adipocytes
physiological function
the enzyme is involved in intracellular proteolysis within lysosomes. Increased activity and expression are strongly associated with many pathological processes, including cancers
physiological function
the enzyme is upregulated and mediates extracellular matrix degradation in colon adenocarcinoma HT29 cells overexpressing Snail (a key regulator of the extracellular matrix degradation). It is hypothesized that cathepsin B controls extracellular matrix proteolysis related to mesenchymal migration in colon cancer cells at early stages of the epithelial-to-mesenchymal transition
physiological function
the main functions are the turnover of cellular proteins, the regulation of angiogenesis, invasion, tumor proliferation and immune resistance, neurogenesis, cellular differentiation and tumor response to hypoxia. Cathepsin B plays a protective role by degrading excessive amounts of misfolded protein inside the cell. In humans, the levels of cathepsin B correlates with hippocampal-dependent memory functions and can be increased by physical exercise. The decrease in the rate of neurogenesis in Alzheimer's disease can be secondary to the accumulation of the critical Alzheimer's disease proteins, which can be induced by inhibition of cathepsin B and the consequent the lysosomal dysfunction. The expression of cathepsin B is elevated in many, but not all, cancers
malfunction
-
arsenite treatment of human glioblastoma cells induces autophagosome formation and permeabilization of mitochondria, followed by caspase 3/7-mediated apoptosis. Arsenite toxicity involves a complex interplay between autophagy and apoptosis in human glioblastoma cells and is associated with inhibition of CatB, mechanism, overview
malfunction
-
cathepsin B confers protection against cell death in clonogenic assays of CD34+ primary cells from chronic myelogenous leukemia patients
malfunction
-
cathepsin B is a major lysosomal protease, its overactivation is involved in muscular dystrophy, bone resorption, pulmonary emphysem, and tumor metastasis
malfunction
-
cathepsin B overexpression in glioblastoma is correlated with a short survival of the patient
malfunction
-
extracellular release of the lysosomal proteases, cathepsins, and their inhibitors is associated with the development and progression of several types of cancer
malfunction
-
glioblastoma and endothelial cells cross-talk, mediated by SDF-1, enhances tumour invasion and endothelial proliferation by increasing expression of cathepsins B, S, and MMP-9. Enhanced invasiveness correlates with increased expression of MMP-9 in both U87 and HMEC-1 cells, increased expression of cysteine cathepsins B and S and down-regulation of endogenous cell adhesion molecule NCAM in U-87 cells. U-87 tumour cells significantly enhance the proliferation of co-cultured endothelial cells by a mechanism involving cathepsin B, but not cathepsin S, overview. Regulation of invasion of U-87 cells involves cathepsin B, overview
malfunction
-
inhibition of cathepsin B impairs lysosomal proteolysis. FYAD, an irreversible inhibitor of cathepsin B, induces apoptosis of neuroblastoma cells but not of other tumor cells. Inhibition of cathepsin D does not rescue cells from FYAD-induced death
malfunction
-
lysosomal destabilization contributes for cell death through controlled release of lysosomal enzymes, the prominent among them being cathepsin B. p53-dependent lysosomal destabilization and cathepsin B activation contribute for increased sensitivity of p21-deficient cells to embelin with enhanced caspase 9 and caspase 3 activation, overview
malfunction
-
Microglia induce apoptosis of glioma cells via the release of NO and cathepsin B protease. Cathepsin B causes a decrease in cell survival. Cathepsin B plays a critical role in cytotoxicity in the central nervous system
malfunction
-
specific blocking cathepsin B expression suppresses apoptosis but does not affect autophagy, which suggests that cathepsin B is a molecular link between autophagy and apoptosis. Cathepsin B inhibition decreases the SPARC-induced release of cytochrome c
malfunction
-
the activity of CatB, but not of CatL or CatS, is relevant to glioblastoma invasion, role of cathepsin B in glioma invasion by in vitro 3D spheroids migration modelling of in vivo glioma growth and invasion, overview
malfunction
-
both caspase 3 activation and PARP cleavage are significantly reduced in cells lacking cathepsin B. Mitochondrial membrane permeabilization as well as the release of cytochrome C and AIF from mitochondria into cytosol induced by doxorubicin are significantly diminished in cathepsin B suppressed cells. Cell viability following doxorubicin is significantly elevated in cells with cathepsin B silencing
malfunction
-
inhibition of cathepsin B has no inhibitory effect on Notch processing
physiological function
-
autocatalytic activation of procathepsin B can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins
physiological function
-
CatB is involved in but is not essential for antigen processing
physiological function
-
cathepsin B is a molecular link between autophagy and apoptosis. Cathepsin B mediates SPARC-induced apoptosis in primitive neuroectodermal tumor, PNET, cells, overview. SPARC is secreted protein, acidic and rich in cysteine, a matrix-associated glycoprotein. Cathepsin B inhibition decreases the SPARC-induced release of cytochorome c indicating that the release is due to cathepsin B activity
physiological function
-
cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
physiological function
-
in case of inflammation of the urethra and cervix after Neisseria gonorrhoeae infection, cathepsin B is an apical controlling step in the downstream activities of NLRP3 including interleukin-1beta production, pyronecrosis, and HMGB1 release. NLRP3 mediates cell death in B-lymphocytes and THP-1 cells
physiological function
-
proteases play a major role in the invasion process with correlations between glioma grading, survival and protease expression. Cathepsin B is involved in extracellular matrix degradation in glioblastomas, and in invasion and angiogenesis, overview
physiological function
-
the endopeptidase activity of cathepsin B is associated with the degradation of the extracellular matrix proteins, which is a process required for tumor cell invasion and metastasis, the activity can be inhibited by the 2A2 monoclonal antibody
physiological function
-
TiO2-induced interleukin-1beta production depends on active cathepsin B and reactive oxygen species production
physiological function
-
cathepsin B plays a role in doxorubicin-induced cell death
physiological function
-
cathepsin B plays a role in the metabolism of amyloid precursor protein. Cathepsin B is a major CTF- and AICD-degrading enzyme with no effect on alpha- and beta-secretase activities
additional information
-
based on the use of proteinase inhibitors, cell death changes from being principally caspase-dependent to being principally cathepsin B-dependent, overview
additional information
-
cathepsin B release after imatinib-mediated lysosomal membrane permeabilization triggers tyrosine kinase BCR-ABL cleavage and elimination of chronic myelogenous leukemia cells, overview
additional information
-
increased CatB expression in malignant ovarian tumors might be balanced by a corresponding increase in inhibitor CysC, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATB_HUMAN
339
0
37822
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
-
x * 15000, form I, SDS-PAGE, x * 20000, form II, SDS-PAGE, x * 30000, form III, SDS-PAGE
20000
-
x * 15000, form I, SDS-PAGE, x * 20000, form II, SDS-PAGE, x * 30000, form III, SDS-PAGE
30000
31000
32000
-
x * 37000, procathepsin B, x * 32000, intermediate cathepsin B, x * 30000, mature enzyme, SDS-PAGE
37000
39000
-
x * 39000, enzyme precursor form, SDS-PAGE, x * 30000-31000, intermediate single-chain enzyme form, SDS-PAGE, x* 24000-25000, mature double-chain enzyme form, SDS-PAGE
30000
-
x * 37000, procathepsin B, x * 32000, intermediate cathepsin B, x * 30000, mature enzyme, SDS-PAGE
30000
-
x * 15000, form I, SDS-PAGE, x * 20000, form II, SDS-PAGE, x * 30000, form III, SDS-PAGE
31000
-
x * 31000, single chain cathepsin B, SDS-PAGE, x * 25000-26000, heavy chain of double chain cathepsin B, SDS-PAGE
37000
-
x * 37000, procathepsin B, x * 32000, intermediate cathepsin B, x * 30000, mature enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
-
x * 37000, procathepsin B, x * 32000, intermediate cathepsin B, x * 30000, mature enzyme, SDS-PAGE
?
-
x * 15000, form I, SDS-PAGE, x * 20000, form II, SDS-PAGE, x * 30000, form III, SDS-PAGE
?
-
x * 31000, single chain cathepsin B, SDS-PAGE, x * 25000-26000, heavy chain of double chain cathepsin B, SDS-PAGE
?
-
x * 39000, enzyme precursor form, SDS-PAGE, x * 30000-31000, intermediate single-chain enzyme form, SDS-PAGE, x* 24000-25000, mature double-chain enzyme form, SDS-PAGE
additional information
-
peptide mapping in 143B cells by 2D gel electrophoresis and mass spectrometry
additional information
-
three-dimensional structure of cathepsin B in comparison to other cathepsins, it possesses a long and narrow substrate-binding active site cleft with catalytic residue Cys, the surfaces of the S1 and S1' subsites are negatively charged due to presence of Glu122 and Glu194, the occluding loop of residue 105-125 is a structural feature containing the two positively charged His residues, His110 and His111, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
cathepsin B is first expressed as a 44 kDa inactive precursor which then undergoes maturation to produce a 33 kDa lysosome enzyme later converted to a final active form composed of two (24 and 5 kDa) subunits
proteolytic modification
proteolytic modification
-
of C- and of N-terminus, autocatalytic processing, precursor forms are inactive
proteolytic modification
-
autocatalytic activation of the purified proenzyme in 20 mM sodium acetate, pH 5.0, 1mM EDTA, for 5 days
proteolytic modification
-
cathepsin B is secreted as an inactive precursor form and activated by cleavage through pepsin at pH 3.5
proteolytic modification
-
cathepsin B is synthesised as a pre-pro-enzyme and the primary pathways for its normal trafficking to the lysosome utilise mannose-6-phosphate receptors. Inactive pro-cathepsin-B is processed to active single and double chain forms of cathepsin-B in the late endosomes and lysosomes, respectively. Under certain conditions cathepsin-B may be secreted extracellularly as a pro-enzyme that requires proteolytic activation
proteolytic modification
-
the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type enzyme and enzyme mutants in complex with inhibitor chagasin, hanging drop vapor diffusion method at 18°C, for crystal form I: mixing of 0.001 ml of 5 mg/ml chagasin solution with 0.002 ml of protein solution containing 3 mg/ml cathepsin B, and 0.002 ml of precipitant solution containing 0.2 M NH4H2PO4, 20% PEG 3350, pH 4.6, 2 weeks, for crystal form II: mixing of 0.001 mL of 5 mg/ml chagasin solution with 0.0015 ml of protein solution containing 3 mg/ml cathepsin B, and 0.001 ml of precipitant solution containing 0.14 M NH4F, 14% PEG 3350, pH 6.2, 1 week, X-ray diffraction structure determination and analysis at 1.8-2.7 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C29A
H110A
-
4fold decrease in pH stability compared to wild type, inhibition by heparin similar to wild type
H110A/S115A
K39A/R40A
-
site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant
L41A
-
site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant
R40A
-
site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to wild-type variant
S115A
additional information
C29A
-
stable at pH 7.5, while native enzyme irreversibly unfolds, and urea denaturation is reversible in contrast to native enzyme
H110A/S115A
-
site-directed mutagenesis, the S115A mutation eliminates an O-glycosylation site
S115A
-
site-directed mutagenesis, the S115A mutation eliminates an O-glycosylation site
additional information
-
cathepsin B gene silencing by using cathepsin B small interfering RNA, siRNA, overview
additional information
-
autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region
additional information
-
cathepsin B silencing by siRNA transfection decreases hepatic stellate cell proliferation and the expression of phenotypic markers of hepatic stellate cell activation, overview
additional information
-
downregulation of CatB by siRNA leads to 33% residual activity of CatB, but has no effect on caspase 3/7 activation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
cathepsin B loses stability and activity at pH 8.0, heparin binding prevents cathepsin B destabilization at pH 8.0
717439
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant renatured enzyme expressed in inclusion bodies in Escherichia coli
native enzyme partially from caveolae of human umbilical vein endothelial cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis by quantitative RT-PCR, expression patterns of cathepsin B and endogenous inhibitor cystatin C
-
expression analysis by realtime PCR, regulation of enzyme expression takes place at the transcriptional level, transcriptional transactivation of the NF-kappaB-responsive promoter which is higher in cells with mitochondria depleted in mtDNA
-
expression in CABA I ovarian carcinoma cells, cathepsin B expression analysis by real-time PCR
-
expression of recombinant human procathepsin B and cathepsin B in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highest expression in Wharton's jelly and the lowest in the umbilical cord arteries
the enzyme is upregulated in colon adenocarcinoma HT29 cells overexpressing Snail (a key regulator of the extracellular matrix degradation)
upregulation of cathepsin B activity and caspase-4 activation in peripheral blood mononuclear cells of patients with Systemic Inflammatory Response Syndrome or sepsis
expression of cathepsins B, L and S gradually increases in the progression from benign astrocytoma to the malignant glioblastoma
-
slibinin downregulates cathepsin B in glioblastoma contributing to reduction of invasiveness, overview
-
SPARC, i.e. secreted protein, acidic and rich in cysteine, a matrix-associated glycoprotein, expression induces autophagy, which results in the elevation of cathepsin B and subsequent mitochondria-mediated apoptosis
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after treatment with 8 M urea, mutant C29A refolds in 50 mM acetate buffer, pH 5.0, wild-type enzyme remains unfolded
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
CATB is a potent and independent prognostic marker for resectable pancreatic adenocarcinoma
drug development
medicine
molecular biology
N,N'-diBoc-dityrosine-Gly-(isoniazid)2 is a sensitive and selective assay of cathepsin B activity
diagnostics
drug development
-
cathepsin B is a target for development of efficient and specific inhibitors
medicine
pharmacology
-
the cathepsin B cleavable spacer Phe-Lys-4-aminobenzyloxycarbonyl, incorporated in an albumin-binding prodrug, is an effective way to increase the therapeutic index of doxorubicin
additional information
-
cathepsin B is a marker for malignant diseases such as colorectal cancer, diagnostic accuracy, overview
drug development
cathepsin B contributes to the neovascularization process and should be considered as a potential therapeutic target
drug development
the new organotellurium(IV)compounds are powerful inhibitors of cathepsin B, constituting promising potential anti-metastatic agents
drug development
cathepsin B could be a drug target for several pathologies, based mainly on its role in cancer progression and osteoarthritis in humans
drug development
cathepsin B is a target for anti-cancer therapy. RNA interference oligonucleotide shRNA-CTSB2 is the most efficient inhibition of cathepsin B at both mRNA and protein levels and results in suppressing endometrial cancer growth and development in vivo
medicine
cathepsin B is a target for anti-cancer therapy. RNA interference oligonucleotide shRNA-CTSB2 is the most efficient inhibition of cathepsin B at both mRNA and protein levels and results in suppressing endometrial cancer growth and development in vivo
medicine
the control of cathepsin B expression may be a target for the treatment of metabolic disorders associated to an inflammatory background
medicine
the enzyme is involved in tumour progression and represents a potential therapeutic target in cancer
diagnostics
-
cathepsin B is a biologic marker reflecting the clinical state of inflammatory disease
diagnostics
-
increased cathepsin-B expression is predictive of more aggressive tumour behaviour over time and can be regarded as an unfavourable and independent tumour marker for endometrial cancer patients with a long follow-up
diagnostics
-
cathepsin B is a possible prognostic biomarker for the aggressiveness of ovarian cancer, overview
diagnostics
-
cathepsin B is an important biomarker for the stratification of glioblastoma patients with respect to survival
medicine
-
involvement of cathepsins in the diminution of the lung antiprotease screen possibly leading to lung destruction in emphysema
medicine
-
inhibition of cathepsins B and L may provide a unique mechanism for selectively inducing death of neuroblastoma with limited toxicity to normal cells and tissues
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brzin, J.; Popovic, T.; Drobnic-Kosorok, M.; Kotnik, M.; Turk, V.
Inhibitors of cysteine proteinases from potato
Biol. Chem. Hoppe-Seyler
369
233-238
1988
Homo sapiens
Buttle, D.J.; Bonner, B.C.; Burnett, D.; Barrett, A.J.
A catalytically active high-Mr form of human cathepsin B from sputum
Biochem. J.
254
693-699
1988
Homo sapiens
Baricos, W.H.; Zhou, Y.; Mason, R.W.; Barrett, A.J.
Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane
Biochem. J.
252
301-304
1988
Homo sapiens
Simon, J.; Duffy, M.J.
Characterization of a cathepsin B-like enzyme from breast cancer
Biochem. Soc. Trans.
14
460
1986
Homo sapiens
-
Rich, D.H.; Brown, M.A.; Barrett, A.J.
Purification of cathepsin B by a new form of affinity chromatography
Biochem. J.
235
731-734
1986
Homo sapiens
Gounaris, A.D.; Slater, E.E.
Cathepsin B from human renal cortex
Biochem. J.
205
295-302
1982
Homo sapiens
Barrett, A.J.; Kirschke, H.
Cathepsin B, Cathepsin H, and cathepsin L
Methods Enzymol.
80
535-561
1981
Homo sapiens
Evans, P.; Etherington, D.J.
Characterisation of cathepsin B and collagenolytic cathepsin from human placenta
Eur. J. Biochem.
83
87-97
1978
Homo sapiens
Swanson, A.A.; Martin, B.J.; Spicer, S.S.
Human placental cathepsin B1. Isolation and some physical properties
Biochem. J.
137
223-228
1974
Homo sapiens
Musil, D.; Zucic, D.; Engh, R.A.; Mayr, I.; Huber, R.; Popovic, T.; Turk, V.; Towatari, T.; Katanuma, N.; Bode, W.
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity
EMBO J.
10
2321-2330
1991
Homo sapiens
Chan, S.J; San Segundo, B.; McCormick, M.B.; Steiner, D.
Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs
Proc. Natl. Acad. Sci. USA
83
7721-7725
1986
Homo sapiens, Mus musculus
Steed, P.M.; Lasala, D.; Liebman, J.; Wigg, A.; Clark, K.; Knap, A.K.
Characterization of recombinant human cathepsin B expressed at high levels in baculovirus
Protein Sci.
7
2033-2037
1998
Homo sapiens
Quraishi, O.; Storer, A.C.
Identification of internal autoproteolytic cleavage sites within the prosegments of recombinant procathepsin B and procathepsin S. Contribution of a plausible unimolecular autoproteolytic event for the processing of zymogens belonging to the papain family
J. Biol. Chem.
276
8118-8124
2001
Homo sapiens
Krupa, J.C.; Hasnain, S.; Nagler, D.K.; Menard, R.; Mort, J.S.
S2' substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B
Biochem. J.
361
613-619
2002
Homo sapiens (P07858), Homo sapiens
Cezari, M.H.; Puzer, L.; Juliano, M.A.; Carmona, A.K.; Juliano, L.
Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides
Biochem. J.
368
365-369
2002
Homo sapiens
Therrien, C.; Lachance, P.; Sulea, T.; Purisima, E.O.; Qi, H.; Ziomek, E.; Alvarez-Hernandez, A.; Roush, W.R.; Menard, R.
Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities
Biochemistry
40
2702-2711
2001
Homo sapiens (P07858)
Melo, R.L.; Barbosa Pozzo, R.C.; Alves, L.C.; Perissutti, E.; Caliendo, G.; Santagada, V.; Juliano, L.; Juliano, M.A.
Synthesis and hydrolysis by cathepsin B of fluorogenic substrates with the general structure benzoyl-X-ARG-MCA containing non-natural basic amino acids at position X
Biochim. Biophys. Acta
1547
82-94
2001
Homo sapiens
Menard, R.; Therrien, C.; Lachance, P.; Sulea, T.; Qi, H.; Alvarez-Hernandez, A.; Roush, W.R.
Cathepsins X and B display distinct activity profiles that can be exploited for inhibitor design
Biol. Chem.
382
839-845
2001
Homo sapiens
Schaschke, N.; Deluca, D.; Assfalg-Machleidt, I.; Hohneke, C.; Sommerhoff, C.P.; Machleidt, W.
Epoxysuccinyl peptide-derived cathepsin B inhibitors: modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin
Biol. Chem.
383
849-852
2002
Homo sapiens
Nakagomi, K.; Fujimura, A.; Maeda, H.; Sadakane, Y.; Fujii, N.; Akizawa, T.; Tanimura, T.; Hatanaka, Y.
Isolation of novel peptides, cabin-1, -2, -3, and -4, that inhibit cathepsin B from a thermolysin digest of human plasma
Biol. Pharm. Bull.
25
564-568
2002
Homo sapiens
Cathers, B.E.; Barrett, C.; Palmer, J.T.; Rydzewski, R.M.
pH Dependence of inhibitors targeting the occluding loop of cathepsin B
Bioorg. Chem.
30
264-275
2002
Homo sapiens
Song, J.; Xu, P.; Xiang, H.; Su, Z.; Storer, A.C.; Ni, F.
The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B
FEBS Lett.
475
157-162
2000
Homo sapiens
Taggart, C.C.; Lowe, G.J.; Greene, C.M.; Mulgrew, A.T.; O'Neill, S.J.; Levine, R.L.; McElvaney, N.G.
Cathepsin B, L, and S cleave and inactivate secretory leucoprotease inhibitor
J. Biol. Chem.
276
33345-33352
2001
Homo sapiens
Almeida, P.C.; Nantes, I.L.; Chagas, J.R.; Rizzi, C.C.; Faljoni-Alario, A.; Carmona, E.; Juliano, L.; Nader, H.B.; Tersariol, I.L.
Cathepsin B activity regulation. Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation
J. Biol. Chem.
276
944-951
2001
Homo sapiens
Greenspan, P.D.; Clark, K.L.; Tommasi, R.A.; Cowen, S.D.; McQuire, L.W.; Farley, D.L.; van Duzer, J.H.; Goldberg, R.L.; Zhou, H.; Du, Z.; Fitt, J.J.; Coppa, D.E.; Fang, Z.; Macchia, W.; Zhu, L.; Capparelli, M.P.; Goldstein, R.; Wigg, A.M.; Doughty, J.R.; Bohacek, R.S.; Knap, A.K.
Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design
J. Med. Chem.
44
4524-4534
2001
Homo sapiens
Del Nery, E.; Alves, L.C.; Melo, R.L.; Cesari, M.H.; Juliano, L.; Juliano, M.A.
Specificity of cathepsin B to fluorescent substrates containing benzyl side-chain-substituted amino acids at P1 subsite
J. Protein Chem.
19
33-38
2000
Homo sapiens
Nakagomi, K.; Takatsu, K.; Takagi, S.; Ebisu, H.; Sadakane, Y.; Fujii, N.; Akizawa, T.; Tanimura, T.; Hatanaka, Y.
Isolation of cathepsin B inhibitory peptides, Cabin-A1 and -A2, from a tryptic and chymotryptic hydrolysate of human serum albumin
Peptides
23
1567-1571
2002
Homo sapiens
Lindkvist, B.; Fajardo, I.; Pejler, G.; Borgstrom, A.
Cathepsin B activates human trypsinogen 1 but not proelastase 2 or procarboxypeptidase B
Pancreatology
6
224-231
2006
Homo sapiens (P07858), Homo sapiens
Cotrin, S.S.; Puzer, L.; de Souza Judice, W.A.; Juliano, L.; Carmona, A.K.; Juliano, M.A.
Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides to define substrate specificity of carboxydipeptidases: assays with human cathepsin B
Anal. Biochem.
335
244-252
2004
Homo sapiens (P07858), Homo sapiens
Pan, X.; Tan, N.; Zeng, G.; Zhang, Y.; Jia, R.
Amentoflavone and its derivatives as novel natural inhibitors of human Cathepsin B
Bioorg. Med. Chem.
13
5819-5825
2005
Homo sapiens (P07858), Homo sapiens
Cunha, R.L.; Urano, M.E.; Chagas, J.R.; Almeida, P.C.; Bincoletto, C.; Tersariol, I.L.; Comasseto, J.V.
Tellurium-based cysteine protease inhibitors: evaluation of novel organotellurium(IV) compounds as inhibitors of human cathepsin B
Bioorg. Med. Chem. Lett.
15
755-760
2005
Homo sapiens (P07858), Homo sapiens
Frlan, R.; Gobec, S.
Inhibitors of cathepsin B
Curr. Med. Chem.
13
2309-2327
2006
Homo sapiens (P07858), Homo sapiens
Troy, A.M.; Sheahan, K.; Mulcahy, H.E.; Duffy, M.J.; Hyland, J.M.; ODonoghue, D.P.
Expression of cathepsin B and L antigen and activity is associated with early colorectal cancer progression
Eur. J. Cancer
40
1610-1616
2004
Homo sapiens (P07858), Homo sapiens
Zeng, G.Z.; Pan, X.L.; Tan, N.H.; Xiong, J.; Zhang, Y.M.
Natural biflavones as novel inhibitors of cathepsin B and K
Eur. J. Med. Chem.
41
1247-1552
2006
Homo sapiens (P07858), Homo sapiens
Laurent-Matha, V.; Derocq, D.; Prebois, C.; Katunuma, N.; Liaudet-Coopman, E.
Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B
J. Biochem.
139
363-371
2006
Homo sapiens (P07858), Homo sapiens
Premzl, A.; Turk, V.; Kos, J.
Intracellular proteolytic activity of cathepsin B is associated with capillary-like tube formation by endothelial cells in vitro
J. Cell. Biochem.
97
1230-1240
2006
Homo sapiens (P07858), Homo sapiens
Wieczerzak, E.; Jankowska, E.; Rodziewicz-Motowidlo, S.; Gieldon, A.; Lagiewka, J.; Grzonka, Z.; Abrahamson, M.; Grubb, A.; Broemme, D.
Novel azapeptide inhibitors of cathepsins B and K. Structural background to increased specificity for cathepsin B
J. Pept. Res.
66 Suppl 1
1-11
2005
Homo sapiens (P07858)
Taha, T.A.; El-Alwani, M.; Hannun, Y.A.; Obeid, L.M.
Sphingosine kinase-1 is cleaved by cathepsin B in vitro: Identification of the initial cleavage sites for the protease
FEBS Lett.
580
6047-6054
2006
Homo sapiens
Schmid, B.; Chung, D.E.; Warnecke, A.; Fichtner, I.; Kratz, F.
Albumin-binding prodrugs of camptothecin and doxorubicin with an Ala-Leu-Ala-Leu-linker that are cleaved by cathepsin B: synthesis and antitumor efficacy
Bioconjug. Chem.
18
702-716
2007
Homo sapiens
Serveau-Avesque, C.; Ferrer-Di Martino, M.; Herve-Grepinet, V.; Hazouard, E.; Gauthier, F.; Diot, E.; Lalmanach, G.
Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids
Biol. Cell.
98
15-22
2006
Homo sapiens
Myers, M.C.; Napper, A.D.; Motlekar, N.; Shah, P.P.; Chiu, C.H.; Beavers, M.P.; Diamond, S.L.; Huryn, D.M.; Smith, A.B.
Identification and characterization of 3-substituted pyrazolyl esters as alternate substrates for cathepsin B: the confounding effects of DTT and cysteine in biological assays
Bioorg. Med. Chem. Lett.
17
4761-4766
2007
Homo sapiens
Hoang, V.L.; Li, Y.; Kim, S.K.
Cathepsin B inhibitory activities of phthalates isolated from a marine Pseudomonas strain
Bioorg. Med. Chem. Lett.
18
2083-2088
2008
Homo sapiens
Fujisawa, A.; Kambe, N.; Saito, M.; Nishikomori, R.; Tanizaki, H.; Kanazawa, N.; Adachi, S.; Heike, T.; Sagara, J.; Suda, T.; Nakahata, T.; Miyachi, Y.
Disease-associated mutations in CIAS1 induce cathepsin B-dependent rapid cell death of human THP-1 monocytic cells
Blood
109
2903-2911
2007
Homo sapiens
Bueth, H.; Luigi Buttigieg, P.; Ostafe, R.; Rehders, M.; Dannenmann, S.R.; Schaschke, N.; Stark, H.J.; Boukamp, P.; Brix, K.
Cathepsin B is essential for regeneration of scratch-wounded normal human epidermal keratinocytes
Eur. J. Cell Biol.
86
747-761
2007
Homo sapiens
Sandes, E.; Lodillinsky, C.; Cwirenbaum, R.; Argueelles, C.; Casabe, A.; Eijan, A.M.
Cathepsin B is involved in the apoptosis intrinsic pathway induced by Bacillus Calmette-Guerin in transitional cancer cell lines
Int. J. Mol. Med.
20
823-828
2007
Homo sapiens
Gunatilleke, S.S.; de Oliveira, C.A.; McCammon, J.A.; Barrios, A.M.
Inhibition of cathepsin B by Au(I) complexes: a kinetic and computational study
J. Biol. Inorg. Chem.
13
555-561
2008
Homo sapiens
Nagaraj, N.S.; Vigneswaran, N.; Zacharias, W.
Cathepsin B mediates TRAIL-induced apoptosis in oral cancer cells
J. Cancer Res. Clin. Oncol.
132
171-183
2006
Homo sapiens
Hasan, L.; Mazzucchelli, L.; Liebi, M.; Lis, M.; Hunger, R.E.; Tester, A.; Overall, C.M.; Wolf, M.
Function of liver activation-regulated chemokine/CC chemokine ligand 20 is differently affected by cathepsin B and cathepsin D processing
J. Immunol.
176
6512-6522
2006
Homo sapiens
Gunatilleke, S.S.; Barrios, A.M.
Tuning the Au(I)-mediated inhibition of cathepsin B through ligand substitutions
J. Inorg. Biochem.
102
555-563
2008
Homo sapiens
Link, M.A.; Silva, L.A.; Schaffer, P.A.
Cathepsin B mediates cleavage of herpes simplex virus type 1 origin binding protein (OBP) to yield OBPC-1, and cleavage is dependent upon viral DNA replication
J. Virol.
81
9175-9182
2007
Homo sapiens (P07858)
Rhee, S.H.; Kang, J.; Nahm, D.S.
Cystatins and cathepsin B during orthodontic tooth movement
Am. J. Orthod. Dentofacial. Orthop.
135
99-105
2009
Homo sapiens
Hamer, I.; Delaive, E.; Dieu, M.; Abdel-Sater, F.; Mercy, L.; Jadot, M.; Arnould, T.
Up-regulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells
Biol. Cell
101
31-41
2009
Homo sapiens
Caglic, D.; Kosec, G.; Bojic, L.; Reinheckel, T.; Turk, V.; Turk, B.
Murine and human cathepsin B exhibit similar properties: possible implications for drug discovery
Biol. Chem.
390
175-179
2009
Homo sapiens (P07858), Homo sapiens, Mus musculus (P10605), Mus musculus
Kim, S.H.; Jhon, D.J.; Song, J.H.; No, J.S.; Kang, N.S.
Effect of novel N-cyano-tetrahydro-pyridazine compounds, a class of cathepsin K inhibitors, on the bone resorptive activity of mature osteoclasts
Bioorg. Med. Chem. Lett.
18
3988-3991
2008
Homo sapiens
Herszenyi, L.; Farinati, F.; Cardin, R.; Istvan, G.; Molnar, L.D.; Hritz, I.; De Paoli, M.; Plebani, M.; Tulassay, Z.
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer
BMC Cancer
8
194
2008
Homo sapiens
Abu Ajaj, K.; Graeser, R.; Fichtner, I.; Kratz, F.
In vitro and in vivo study of an albumin-binding prodrug of doxorubicin that is cleaved by cathepsin B
Cancer Chemother. Pharmacol.
64
413-418
2009
Homo sapiens
Hwang, J.H.; Lee, S.H.; Lee, K.H.; Lee, K.Y.; Kim, H.; Ryu, J.K.; Yoon, Y.B.; Kim, Y.T.
Cathepsin B is a target of Hedgehog signaling in pancreatic cancer
Cancer Lett.
273
266-272
2009
Homo sapiens (P07858), Homo sapiens
Herszenyi, L.; Istvan, G.; Cardin, R.; De Paoli, M.; Plebani, M.; Tulassay, Z.; Farinati, F.
Serum cathepsin B and plasma urokinase-type plasminogen activator levels in gastrointestinal tract cancers
Eur. J. Cancer Prev.
17
438-445
2008
Homo sapiens
Cavallo-Medved, D.; Rudy, D.; Blum, G.; Bogyo, M.; Caglic, D.; Sloane, B.F.
Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
Exp. Cell Res.
315
1234-1246
2009
Homo sapiens
Tsai, H.T.; Wang, P.H.; Tee, Y.T.; Lin, L.Y.; Hsieh, Y.S.; Yang, S.F.
Imbalanced serum concentration between cathepsin B and cystatin C in patients with pelvic inflammatory disease
Fertil. Steril.
91
549-555
2009
Homo sapiens
Czyzewska, J.; Guzinska-Ustymowicz, K.; Kemona, A.; Bandurski, R.
The expression of matrix metalloproteinase 9 and cathepsin B in gastric carcinoma is associated with lymph node metastasis, but not with postoperative survival
Folia Histochem. Cytobiol.
46
57-64
2008
Homo sapiens
Devetzi, M.; Scorilas, A.; Tsiambas, E.; Sameni, M.; Fotiou, S.; Sloane, B.F.; Talieri, M.
Cathepsin B protein levels in endometrial cancer: Potential value as a tumour biomarker
Gynecol. Oncol.
112
531-536
2009
Homo sapiens
Redzynia, I.; Ljunggren, A.; Abrahamson, M.; Mort, J.S.; Krupa, J.C.; Jaskolski, M.; Bujacz, G.
Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B
J. Biol. Chem.
283
22815-22825
2008
Homo sapiens
Yamaguchi, T.; Naruishi, K.; Arai, H.; Nishimura, F.; Takashiba, S.
IL-6/sIL-6R enhances cathepsin B and L production via caveolin-1-mediated JNK-AP-1 pathway in human gingival fibroblasts
J. Cell. Physiol.
217
423-432
2008
Homo sapiens
Elkaim, R.; Werner, S.; Kocgozlu, L.; Tenenbaum, H.
P. gingivalis regulates the expression of cathepsin B and cystatin C
J. Dent. Res.
87
932-936
2008
Homo sapiens
Ha, S.D.; Martins, A.; Khazaie, K.; Han, J.; Chan, B.M.; Kim, S.O.
Cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
J. Immunol.
181
690-697
2008
Homo sapiens, Mus musculus, Mus musculus C57BL/6
Fricker, S.P.; Mosi, R.M.; Cameron, B.R.; Baird, I.; Zhu, Y.; Anastassov, V.; Cox, J.; Doyle, P.S.; Hansell, E.; Lau, G.; Langille, J.; Olsen, M.; Qin, L.; Skerlj, R.; Wong, R.S.; Santucci, Z.; McKerrow, J.H.
Metal compounds for the treatment of parasitic diseases
J. Inorg. Biochem.
102
1839-1845
2008
Homo sapiens
Giusti, I.; D'Ascenzo, S.; Millimaggi, D.; Taraboletti, G.; Carta, G.; Franceschini, N.; Pavan, A.; Dolo, V.
Cathepsin B mediates the pH-dependent proinvasive activity of tumor-shed microvesicles
Neoplasia
10
481-488
2008
Homo sapiens
Schenker, P.; Alfarano, P.; Kolb, P.; Caflisch, A.; Baici, A.
A double-headed cathepsin B inhibitor devoid of warhead
Protein Sci.
17
2145-2155
2008
Homo sapiens
Aoki, T.; Kataoka, H.; Ishibashi, R.; Nozaki, K.; Hashimoto, N.
Cathepsin B, K, and S are expressed in cerebral aneurysms and promote the progression of cerebral aneurysms
Stroke
39
2603-2610
2008
Homo sapiens, Rattus norvegicus
Geraghty, P.; Rogan, M.P.; Greene, C.M.; Brantly, M.L.; ONeill, S.J.; Taggart, C.C.; McElvaney, N.G.
Alpha-1-antitrypsin aerosolised augmentation abrogates neutrophil elastase-induced expression of cathepsin B and matrix metalloprotease 2 in vivo and in vitro
Thorax
63
621-626
2008
Homo sapiens
Wang, C.; Jiang, Z.; Yao, J.; Wu, X.; Sun, L.; Liu, C.; Duan, W.; Yan, M.; Sun, L.; Liu, J.; Zhang, L.
Participation of cathepsin B in emodin-induced apoptosis in HK-2 cells
Toxicol. Lett.
181
196-204
2008
Homo sapiens
Colin, C.; Voutsinos-Porche, B.; Nanni, I.; Fina, F.; Metellus, P.; Intagliata, D.; Baeza, N.; Bouvier, C.; Delfino, C.; Loundou, A.; Chinot, O.; Lah, T.; Kos, J.; Martin, P.M.; Ouafik, L.; Figarella-Branger, D.
High expression of cathepsin B and plasminogen activator inhibitor type-1 are strong predictors of survival in glioblastomas
Acta Neuropathol.
118
745-754
2009
Homo sapiens
Li, J.H.; DAlessio, A.; Pober, J.S.
Lipopolysaccharide can trigger a cathepsin B-dependent programmed death response in human endothelial cells
Am. J. Pathol.
175
1124-1135
2009
Homo sapiens
Momeny, M.; Malehmir, M.; Zakidizaji, M.; Ghasemi, R.; Ghadimi, H.; Shokrgozar, M.A.; Emami, A.H.; Nafissi, S.; Ghavamzadeh, A.; Ghaffari, S.H.
Silibinin inhibits invasive properties of human glioblastoma U87MG cells through suppression of cathepsin B and nuclear factor kappa B-mediated induction of matrix metalloproteinase 9
Anticancer Drugs
21
252-260
2010
Homo sapiens
Morishige, T.; Yoshioka, Y.; Tanabe, A.; Yao, X.; Tsunoda, S.; Tsutsumi, Y.; Mukai, Y.; Okada, N.; Nakagawa, S.
Titanium dioxide induces different levels of IL-1beta production dependent on its particle characteristics through caspase-1 activation mediated by reactive oxygen species and cathepsin B
Biochem. Biophys. Res. Commun.
392
160-165
2010
Homo sapiens
Hwang, S.Y.; Yoo, B.C.; Jung, J.W.; Oh, E.S.; Hwang, J.S.; Shin, J.A.; Kim, S.Y.; Cha, S.H.; Han, I.O.
Induction of glioma apoptosis by microglia-secreted molecules: The role of nitric oxide and cathepsin B
Biochim. Biophys. Acta
1793
1656-1668
2009
Homo sapiens, Rattus norvegicus
Cunha, R.L.; Gouvea, I.E.; Feitosa, G.P.; Alves, M.F.; Broemme, D.; Comasseto, J.V.; Tersariol, I.L.; Juliano, L.
Irreversible inhibition of human cathepsins B, L, S and K by hypervalent tellurium compounds
Biol. Chem.
390
1205-1212
2009
Homo sapiens
Pucer, A.; Castino, R.; Mirkovi?, B.; Falnoga, I.; Slejkovec, Z.; Isidoro, C.; Lah, T.T.
Differential role of cathepsins B and L in autophagy-associated cell death induced by arsenic trioxide in U87 human glioblastoma cells
Biol. Chem.
391
519-531
2010
Homo sapiens
Song, G.; Bailey, D.W.; Dunlap, K.A.; Burghardt, R.C.; Spencer, T.E.; Bazer, F.W.; Johnson, G.A.
Cathepsin B, cathepsin L, and cystatin C in the porcine uterus and placenta: potential roles in endometrial/placental remodeling and in fluid-phase transport of proteins secreted by uterine epithelia across placental areolae
Biol. Reprod.
82
854-864
2010
Homo sapiens
Li, J.; Petrassi, H.; Tumanut, C.; Masick, B.; Trussell, C.; Harris, J.
Substrate optimization for monitoring cathepsin C activity in live cells
Bioorg. Med. Chem.
17
1064-1070
2009
Homo sapiens
Kenig, S.; Alonso, M.B.; Mueller, M.M.; Lah, T.T.
Glioblastoma and endothelial cells cross-talk, mediated by SDF-1, enhances tumour invasion and endothelial proliferation by increasing expression of cathepsins B, S, and MMP-9
Cancer Lett.
289
53-61
2010
Homo sapiens
Colella, R.; Lu, G.; Glazewski, L.; Korant, B.; Matlapudi, A.; England, M.R.; Craft, C.; Frantz, C.N.; Mason, R.W.
Induction of cell death in neuroblastoma by inhibition of cathepsins B and L
Cancer Lett.
294
195-203
2010
Homo sapiens
Bhoopathi, P.; Chetty, C.; Gujrati, M.; Dinh, D.H.; Rao, J.S.; Lakka, S.
Cathepsin B facilitates autophagy-mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells
Cell Death Differ.
17
1529-1539
2010
Homo sapiens
Tomoo, K.
Development of cathepsin inhibitors and structure-based design of cathepsin B-specific inhibitor
Curr. Top. Med. Chem.
10
696-707
2010
Homo sapiens
Huryn, D.M.; Smith, A.B.
The identification, characterization and optimization of small molecule probes of cysteine proteases: experiences of the Penn center for molecular discovery with cathepsin B and cathepsin L
Curr. Top. Med. Chem.
9
1206-1216
2009
Homo sapiens
Spencer, J.; Casini, A.; Zava, O.; Rathnam, R.P.; Velhanda, S.K.; Pfeffer, M.; Callear, S.K.; Hursthouse, M.B.; Dyson, P.J.
Excellent correlation between cathepsin B inhibition and cytotoxicity for a series of palladacycles
Dalton Trans.
2009
10731-10735
2009
Bos taurus, Homo sapiens
Casini, A.; Edafe, F.; Erlandsson, M.; Gonsalvi, L.; Ciancetta, A.; Re, N.; Ienco, A.; Messori, L.; Peruzzini, M.; Dyson, P.J.
Rationalization of the inhibition activity of structurally related organometallic compounds against the drug target cathepsin B by DFT
Dalton Trans.
39
5556-5563
2010
Homo sapiens
Kolwijck, E.; Kos, J.; Obermajer, N.; Span, P.N.; Thomas, C.M.; Massuger, L.F.; Sweep, F.C.
The balance between extracellular cathepsins and cystatin C is of importance for ovarian cancer
Eur. J. Clin. Invest.
40
591-599
2010
Homo sapiens
Mirkovic, B.; Premzl, A.; Hodnik, V.; Doljak, B.; Jevnikar, Z.; Anderluh, G.; Kos, J.
Regulation of cathepsin B activity by 2A2 monoclonal antibody
FEBS J.
276
4739-4751
2009
Homo sapiens
Pungercar, J.R.; Caglic, D.; Sajid, M.; Dolinar, M.; Vasiljeva, O.; Pozgan, U.; Turk, D.; Bogyo, M.; Turk, V.; Turk, B.
Autocatalytic processing of procathepsin B is triggered by proenzyme activity
FEBS J.
276
660-668
2009
Homo sapiens
Moles, A.; Tarrats, N.; Fernandez-Checa, J.C.; Mari, M.
Cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
Hepatology
49
1297-1307
2009
Homo sapiens, Mus musculus, Mus musculus C57BL/6
Reich, M.; Wieczerzak, E.; Jankowska, E.; Palesch, D.; Boehm, B.O.; Burster, T.
Specific cathepsin B inhibitor is cell-permeable and activates presentation of TTC in primary human dendritic cells
Immunol. Lett.
123
155-159
2009
Homo sapiens
Beckham, S.A.; Piedrafita, D.; Phillips, C.I.; Samarawickrema, N.; Law, R.H.; Smooker, P.M.; Quinsey, N.S.; Irving, J.A.; Greenwood, D.; Verhelst, S.H.; Bogyo, M.; Turk, B.; Coetzer, T.H.; Wijeyewickrema, L.C.; Spithill, T.W.; Pike, R.N.
A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in the digestive tract of newly excysted juvenile parasites
Int. J. Biochem. Cell Biol.
41
1601-1612
2009
Fasciola hepatica, Homo sapiens
Kolwijck, E.; Massuger, L.F.; Thomas, C.M.; Span, P.N.; Krasovec, M.; Kos, J.; Sweep, F.C.
Cathepsins B, L and cystatin C in cyst fluid of ovarian tumors
J. Cancer Res. Clin. Oncol.
136
771-778
2010
Homo sapiens
Duncan, J.A.; Gao, X.; Huang, M.T.; OConnor, B.P.; Thomas, C.E.; Willingham, S.B.; Bergstralh, D.T.; Jarvis, G.A.; Sparling, P.F.; Ting, J.P.
Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome
J. Immunol.
182
6460-6469
2009
Homo sapiens, Mus musculus
Zhou, Z.; Wang, Y.; Bryant, S.H.
QSAR models for predicting cathepsin B inhibition by small molecules - continuous and binary QSAR models to classify cathepsin B inhibition activities of small molecules
J. Mol. Graph. Model.
28
714-727
2010
Homo sapiens
Puissant, A.; Colosetti, P.; Robert, G.; Cassuto, J.P.; Raynaud, S.; Auberger, P.
Cathepsin B release after imatinib-mediated lysosomal membrane permeabilization triggers BCR-ABL cleavage and elimination of chronic myelogenous leukemia cells
Leukemia
24
115-124
2010
Homo sapiens
Joy, B.; Sivadasan, R.; Abraham T, E.; John, M.; Sobhan, P.K.; Seervi, M.; Santhoshkumar, T.R.
Lysosomal destabilization and cathepsin B contributes for cytochrome c release and caspase activation in embelin-induced apoptosis
Mol. Carcinog.
49
324-336
2010
Homo sapiens
Gole, B.; Duran Alonso, M.B.; Dolenc, V.; Lah, T.
Post-translational regulation of cathepsin B, but not of other cysteine cathepsins, contributes to increased glioblastoma cell invasiveness in vitro
Pathol. Oncol. Res.
15
711-723
2009
Homo sapiens
Murata, R.M.; Yatsuda, R.; dos Santos, M.H.; Kohn, L.K.; Martins, F.T.; Nagem, T.J.; Alencar, S.M.; de Carvalho, J.E.; Rosalen, P.L.
Antiproliferative effect of benzophenones and their influence on cathepsin activity
Phytother. Res.
24
379-383
2010
Homo sapiens
Bien, S.; Rimmbach, C.; Neumann, H.; Niessen, J.; Reimer, E.; Ritter, C.A.; Rosskopf, D.; Cinatl, J.; Michaelis, M.; Schroeder, H.W.; Kroemer, H.K.
Doxorubicin-induced cell death requires cathepsin B in HeLa cells
Biochem. Pharmacol.
80
1466-1477
2010
Homo sapiens
Costa, M.G.; Batista, P.R.; Shida, C.S.; Robert, C.H.; Bisch, P.M.; Pascutti, P.G.
How does heparin prevent the pH inactivation of cathepsin B? Allosteric mechanism elucidated by docking and molecular dynamics
BMC Genomics
11 Suppl 5
S5
2010
Homo sapiens (P07858)
Valadares, N.F.; Dellamano, M.; Soares-Costa, A.; Henrique-Silva, F.; Garratt, R.C.
Molecular determinants of improved cathepsin B inhibition by new cystatins obtained by DNA shuffling
BMC Struct. Biol.
10
30
2010
Homo sapiens
Asai, M.; Yagishita, S.; Iwata, N.; Saido, T.C.; Ishiura, S.; Maruyama, K.
An alternative metabolic pathway of amyloid precursor protein C-terminal fragments via cathepsin B in a human neuroglioma model
FASEB J.
25
3720-3730
2011
Homo sapiens
Wisastra, R.; Ghizzoni, M.; Maarsingh, H.; Minnaard, A.J.; Haisma, H.J.; Dekker, F.J.
Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAF
Org. Biomol. Chem.
9
1817-1822
2011
Homo sapiens
Gogiel, T.; Galewska, Z.; Romanowicz, L.
Differential distribution of cathepsin B in human umbilical cord tissues
Acta Biochim. Pol.
59
679-684
2012
Homo sapiens (P07858), Homo sapiens
Kim, C.J.; Lee, D.I.; Zhang, D.; Lee, C.H.; Ahn, I.S.
New strategy for selective and sensitive assay of cathepsin B using a dityrosine-based material
Anal. Biochem.
435
166-173
2013
Homo sapiens (P07858)
Wyczalkowska-Tomasik, A.; Plczek, L.
Cathepsin B and L activity in the serum during the human aging process: cathepsin B and L in aging
Arch. Gerontol. Geriatr.
55
735-738
2012
Homo sapiens
Morchang, A.; Panaampon, J.; Suttitheptumrong, A.; Yasamut, U.; Noisakran, S.; Yenchitsomanus, P.T.; Limjindaporn, T.
Role of cathepsin B in dengue virus-mediated apoptosis
Biochem. Biophys. Res. Commun.
438
20-25
2013
Homo sapiens (P07858), Homo sapiens
Sosic, I.; Mirkovic, B.; Arenz, K.; Stefane, B.; Kos, J.; Gobec, S.
Development of new cathepsin B inhibitors: combining bioisosteric replacements and structure-based design to explore the structure-activity relationships of nitroxoline derivatives
J. Med. Chem.
56
521-533
2013
Homo sapiens
Edem, P.E.; Czorny, S.; Valliant, J.F.
Synthesis and evaluation of radioiodinated acyloxymethyl ketones as activity-based probes for cathepsin B
J. Med. Chem.
57
9564-9577
2014
Homo sapiens (P07858)
Bian, B.; Mongrain, S.; Cagnol, S.; Langlois, M.; Boulanger, J.; Bernatchez, G.; Carrier, J.; Boudreau, F.; Rivard, N.
Cathepsin B promotes colorectal tumorigenesis, cell invasion, and metastasis
Mol. Carcinog.
55
671-687
2015
Homo sapiens (P07858), Homo sapiens
Zhang, X.; Yang, X.; Wang, H.; Li, S.; Guo, K.; Jiang, D.; Xiao, J.; Liang, D.
Design, synthesis, and structure-activity relationship study of epoxysuccinyl-peptide derivatives as cathepsin B inhibitors
Biol. Pharm. Bull.
40
1240-1246
2017
Homo sapiens (P07858)
Schmitz, J.; Gilberg, E.; Loeser, R.; Bajorath, J.; Bartz, U.; Guetschow, M.
Cathepsin B Active site mapping with peptidic substrates and inhibitors
Bioorg. Med. Chem.
27
1-15
2019
Homo sapiens (P07858), Homo sapiens
Sosic, I.; Mitrovic, A.; Curic, H.; Knez, D.; Brodnik Zugelj, H.; Stefane, B.; Kos, J.; Gobec, S.
Cathepsin B inhibitors Further exploration of the nitroxoline core
Bioorg. Med. Chem. Lett.
28
1239-1247
2018
Homo sapiens (P07858), Homo sapiens
Mijanovic, O.; Brankovic, A.; Panin, A.N.; Savchuk, S.; Timashev, P.; Ulasov, I.; Lesniak, M.S.
Cathepsin B A sellsword of cancer progression
Cancer Lett.
449
207-214
2019
Homo sapiens (P07858)
Chen, N.; Ou, Z.; Zhang, W.; Zhu, X.; Li, P.; Gong, J.
Cathepsin B regulates non-canonical NLRP3 inflammasome pathway by modulating activation of caspase-11 in Kupffer cells
Cell Prolif.
51
e12487
2018
Homo sapiens (P07858), Homo sapiens, Mus musculus (P10605)
Kryczka, J.; Papiewska-Pajak, I.; Kowalska, M.A.; Boncela, J.
Cathepsin B is upregulated and mediates ECM degradation in dolon adenocarcinoma HT29 cells overexpressing snail
Cells
8
203
2019
Homo sapiens (P07858)
Araujo, T.F.; Cordeiro, A.V.; Vasconcelos, D.A.A.; Vitzel, K.F.; Silva, V.R.R.
The role of cathepsin B in autophagy during obesity A systematic review
Life Sci.
209
274-281
2018
Homo sapiens (P07858)
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