Information on EC 3.4.22.1 - cathepsin B

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.22.1
-
RECOMMENDED NAME
GeneOntology No.
cathepsin B
-
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
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
show the reaction diagram
non-active site residue Gln109 and active site Cys115 play an important role in the catalytic mechanism
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
show the reaction diagram
the catalytic residue is Cys29
-
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
show the reaction diagram
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
-
-
-
-
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
APP secretase
-
-
-
-
cat B
-
-
cat B
Mus musculus BALB/c
-
-
-
CatB
-
-
CatB
Mus musculus C57BL/6
-
-
-
CatB
Trypanosoma brucei 90-13
-
-
-
Cath-B
-
-
Cath-B
-
-
cathepsin B
-
-
cathepsin B
-
cathepsin B
isoform 6
cathepsin B
isoform 5
cathepsin B
isoform 4
cathepsin B
isoform 3
cathepsin B
isoform 2
cathepsin B
isoform 1
cathepsin B
-
cathepsin B proteinase
-
-
cathepsin B-like AC-5
-
cathepsin B-like counter-defence protein
-
cathepsin B-like cysteine protease
-
cathepsin B-like cysteine protease
-
-
cathepsin B-like cysteine protease 1
-
cathepsin B-type cysteine protease
-
-
cathepsin B1
-
-
-
-
cathepsin B1
enzyme variant
cathepsin B1
-
-
cathepsin B2
enzyme variant
cathepsin II
-
-
-
-
cathepsin-B
-
-
cathepsin-B
-
-
CPB
Monocercomonoides sp.
-
-
CTSB
Mus musculus C57BL/6, Mus musculus C57BL/6J
-
-
-
cysteine cathepsin
-
-
toxopain-1
-
-
additional information
cathepsin B of Biomphalaria glabrata belongs to the C1A family of peptidases
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
-
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
additional information
the enzyme belongs to the group of cysteine proteases
additional information
-
cathepsin B belongs to the class of lysosomal cysteine cathepsins
additional information
cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family
CAS REGISTRY NUMBER
COMMENTARY
9047-22-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
canine hookworm
-
-
Manually annotated by BRENDA team
Schistosoma mansoni-resistant BS-90, or Salvador strain, and Schistosoma mansoni-susceptible M-line strains
UniProt
Manually annotated by BRENDA team
single-chain and double-chain isoform
-
-
Manually annotated by BRENDA team
buffalo
-
-
Manually annotated by BRENDA team
CmCatB1; genes CmCatB1 and CmCatB2 probably resulting from alternate splicing
SwissProt
Manually annotated by BRENDA team
CmCatB2; gene CmCatB2 probably resulting from alternate splicing
SwissProt
Manually annotated by BRENDA team
cowpea bruchid, a grain storage pest
-
-
Manually annotated by BRENDA team
Capra aegagrus hircus
-
-
Manually annotated by BRENDA team
tongue sole
UniProt
Manually annotated by BRENDA team
Dorytheuthis bleekeri
squid
-
-
Manually annotated by BRENDA team
metacercariae are propagated and harvested from the snail species Lymnaea tormentosa
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
gene CATB or CTSB
SwissProt
Manually annotated by BRENDA team
healthy women and patients with pelvic inflammatory disease
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
recombinant proenzyme
-
-
Manually annotated by BRENDA team
recombinant protein
-
-
Manually annotated by BRENDA team
monkey
-
-
Manually annotated by BRENDA team
Monocercomonoides sp.
-
-
-
Manually annotated by BRENDA team
Balb/c mice
-
-
Manually annotated by BRENDA team
C57/Bl mice
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
female BALB/c nude mice
-
-
Manually annotated by BRENDA team
London APP mice and C57BL/6 mice
-
-
Manually annotated by BRENDA team
male BALB/c mice
-
-
Manually annotated by BRENDA team
male Kunming mice
-
-
Manually annotated by BRENDA team
wild-type C57BL/6 mice, and mutant B6 Rag2-/- and SP6 Rag2-/- Tg mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
Balb/c mice
-
-
Manually annotated by BRENDA team
Mus musculus C57/Bl
C57/Bl mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
C57BL/6J mice
-
-
Manually annotated by BRENDA team
cathepsin B-like cysteine protease Na-CP-2; cathepsin B-like cysteine protease Na-CP-3; cathepsin B-like cysteine protease Na-CP-4; cathepsin B-like cysteine protease Na-CP-5
-
-
Manually annotated by BRENDA team
Japanese flounders, gene PoCatB
UniProt
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
with spinal cord injury
SwissProt
Manually annotated by BRENDA team
strain 90-13
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 90-13
strain 90-13
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
cathepsin B overexpression in glioblastoma is correlated with a short survival of the patient
malfunction
-
genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
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
-
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
-
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
-
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
-
cathespin-B is an important proteolytic enzyme involved in the disease course of invasion in many types of cancer. It correlates with the growth and angiogenesis of tumors, but not with the adhesion induced by CD44v6, in the subcutaneous heteroplastic pancreatic carcinoma model, overview
malfunction
-
BmCatB RNAi treatment results in an arrest of the larval-pupal transformation. RNAi-mediated BmCatB knockdown sustains the expression of BmCatD during the larval-pupal transformation. On the other hand, when BmCatD is inhibited via RNAi, the expression of BmCatB is upregulated
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 is involved in several cancers
malfunction
-
extracellular release of the lysosomal proteases, cathepsins, and their inhibitors is associated with the development and progression of several types of cancer
malfunction
-
CtsB inhibition blunts AKT phosphorylation in activated hepatic stellate cells in response to platelet-derived growth factor. CtsB inactivation mitigates CCl4-induced inflammation, hepatic stellate cell activation, and collagen deposition
malfunction
-
cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor, LeTx, into the cytoplasm, requiring lysosomal fusion with LeTx-containing endosomes. Anthrax lethal toxin is a virulence factor secreted by Bacillus anthracis and has direct cytotoxic effects on most cells once released into the cytoplasm. Inhibition of cathepsin B blocks MEK1 cleavage induced by anthrax lethal toxin through delaying LeTx release into the cytoplasm
malfunction
-
the cathepsin family of endosomal proteases is required for proteolytic processing of several viruses during entry into host cells, cathepsins contribute to reovirus tropism, spread, and disease outcome. Mammalian reoviruses utilize cathepsins B, L, and S for disassembly of the virus outer capsid and activation of the membrane penetration machinery. The survival rate of Ctsb-/- mice infected with reovirus is enhanced in comparison to that of wild-type mice, viremia in wild-type and cathepsin-deficient mice following peroral inoculation, overview
malfunction
-
cathepsin B confers protection against cell death in clonogenic assays of CD34+ primary cells from chronic myelogenous leukemia patients
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
-
exposure of GSH-depleted B cells to NO-releasing compounds lowers their capacity to present a reduced and alkylated lysozyme due to inhibition of cathepsin B by NO, overview. Cells with a normal GSH content are protected from this inhibition
malfunction
-
cathepsin B significantly decreases the number of apoptotic nuclei in both the cumulus cell layer of matured oocytes and blastocysts
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
malfunction
Mus musculus BALB/c
-
exposure of GSH-depleted B cells to NO-releasing compounds lowers their capacity to present a reduced and alkylated lysozyme due to inhibition of cathepsin B by NO, overview. Cells with a normal GSH content are protected from this inhibition
-
malfunction
Mus musculus C57BL/6
-
cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor, LeTx, into the cytoplasm, requiring lysosomal fusion with LeTx-containing endosomes. Anthrax lethal toxin is a virulence factor secreted by Bacillus anthracis and has direct cytotoxic effects on most cells once released into the cytoplasm. Inhibition of cathepsin B blocks MEK1 cleavage induced by anthrax lethal toxin through delaying LeTx release into the cytoplasm; CtsB inhibition blunts AKT phosphorylation in activated hepatic stellate cells in response to platelet-derived growth factor. CtsB inactivation mitigates CCl4-induced inflammation, hepatic stellate cell activation, and collagen deposition; genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
-
malfunction
Mus musculus C57BL/6J
-
the cathepsin family of endosomal proteases is required for proteolytic processing of several viruses during entry into host cells, cathepsins contribute to reovirus tropism, spread, and disease outcome. Mammalian reoviruses utilize cathepsins B, L, and S for disassembly of the virus outer capsid and activation of the membrane penetration machinery. The survival rate of Ctsb-/- mice infected with reovirus is enhanced in comparison to that of wild-type mice, viremia in wild-type and cathepsin-deficient mice following peroral inoculation, overview
-
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
-
TiO2-induced interleukin-1beta production depends on active cathepsin B and reactive oxygen species production
physiological function
-
CatB is involved in but is not essential for antigen processing
physiological function
-
apoptotic stimuli, e.g. exposure to etoposide, ultraviolet light, FasL or deprivation of interleukin-3, trigger lysosomal membrane permeability, leading to the release of cathepsins, dependent on Bax/Bak and components of the apoptosome, which activate death signaling pathways in the cytosol, overview. Cathepsin B does not contribute to the commitment step of apoptosis, as Bax and Bak do, but enhances the efficiency of apoptosis through an amplification loop
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
cathepsin B is involved in the regulation of apoptosis during serum-starvation in teleost follicles. Cathepsin B may play a role in the activation of the executioner caspase-3
physiological function
-
BmCatB is involved in the programmed cell death of the fat body during metamorphosis, and CatB and CatD contribute to the metamorphosis
physiological function
-
the cysteine protease CatB facilitates insects coping with dietary protease inhibitor challenge
physiological function
-
the endopeptidase activity of cathepsin B is associated with the degradation of the extracellular matrix proteins, which is a process required for tumour cell invasion and metastasis, the activity can be inhbited by the 2A2 monoclonal antibody
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
-
cathepsin B is required for interleukin-1beta maturation, the maturation of pro-IL-1beta in chromogranin A-stimulated microglia is dependent on the enzymatic activities of both cathepsin B and caspase-1
physiological function
-
cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
physiological function
-
cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential, the enzyme is required for transdifferentiation of the cells into myofibroblasts, overview. CtsB modulates the phosphoinositide 3-kinase/AKT pathway in activated mouse hepatic stellate cells, overview
physiological function
-
the FhcatB1 protease functions largely as a digestive enzyme in the gut of the parasite. It may be likely important to a vital stage of the parasite's life cycle
physiological function
-
CTSB is a lysosomal cysteine protease primarily involved in the degradation or processing of lysosomal proteins
physiological function
-
CmCatB has a unique role in insect adaptation to the effect of dietary scN. Cowpea bruchids dramatically induce CmCatB expression when major digestive proteases are inactivated by dietary scN, which is presumably an adaptive strategy that insects use to minimize effects of nutrient deficiency
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
-
infection with Neisseria gonorrhoeae induces cathepsin B in apical controlling of the downstream activities of NLRP3 including interleukin-1beta production, pyronecrosis, and HMGB1 release. NLRP3 mediates cell death in B-lymphocytes and macrophages, overview
physiological function
-
the TLR9 ligand CpG DNA inhibits the proliferation of pro-B, but not pre-B, cells by inducing caspase-independent cell death through a pathway that requires the expression of cathepsin B, mechanism, overview
physiological function
-
cathepsin B acts as the main executor of caspase dependent or independent cell death in major organs including the liver, kidney, and lungs
physiological function
-
cathepsin B activity is necessary for TAP-HEL, a reduced and alkylated lysozyme, processing, it is essential for generation of the HEL-derived antigenic peptide recognized by B9.1 cells
physiological function
-
cathepsin B plays a role in doxorubicin-induced cell death
physiological function
cathepsin B is involved in host immune response during bacterial infection and vaccination
physiological function
-
cathepsin B proteinase plays roles in the early development of Ancylostoma caninum
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
physiological function
-
the enzyme has stimulatory effects on embryonic development, metamorphosis, and larval growth during larval development
physiological function
cathepsin B is involved in the nutrient digestion of Meretrix meretrix
physiological function
-
cathepsin B is involved in cuticle renewal
physiological function
Mus musculus BALB/c
-
cathepsin B activity is necessary for TAP-HEL, a reduced and alkylated lysozyme, processing, it is essential for generation of the HEL-derived antigenic peptide recognized by B9.1 cells
-
physiological function
Mus musculus C57BL/6
-
cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential, the enzyme is required for transdifferentiation of the cells into myofibroblasts, overview. CtsB modulates the phosphoinositide 3-kinase/AKT pathway in activated mouse hepatic stellate cells, overview; CTSB is a lysosomal cysteine protease primarily involved in the degradation or processing of lysosomal proteins
-
physiological function
Mus musculus C57/Bl
-
cathepsin B is required for interleukin-1beta maturation, the maturation of pro-IL-1beta in chromogranin A-stimulated microglia is dependent on the enzymatic activities of both cathepsin B and caspase-1
-
metabolism
-
cathepsin B is involved in TNF-alpha-induced signal transduction pathways in lung cells
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
-
coordination between transcription factors CmHNF-4 and CmSvp is important in counter-defense gene regulation in insects, overview
additional information
-
increased CatB expression in malignant ovarian tumors might be balanced by a corresponding increase in inhibitor CysC, 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
-
relation between cathepsin B activity and the quality of in vitro matured cumulus-oocyte complexes, IVM COCs, and denuded oocytes, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl-GARFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GDRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GERFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFAFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFDFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFEFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFFFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFGFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFHFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFIFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFKFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFLFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFPFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFQFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRAW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRDW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFREW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRGW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRHW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRIW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRKW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRLW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRPW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRQW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRRW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRSW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRVW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWA-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWF-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWG-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWI-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWL-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWP-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWQ-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWV-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRWY-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFRYW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFSFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFVFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GFYFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GGRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GHRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GIRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GKRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GLRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GPRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GQRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GRRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GSRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GVRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-GYRFW-OH + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
an exoproteolytic substrate
-
?
4-(4-dimethylaminophenylazo)benzoyl-IEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-IEGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
no hydrolysis at pH 6.0
-
?
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-D-Glu + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-L-Glu + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-D-Glu + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-L-Glu + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-LEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-LEGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
no hydrolysis at pH 6.0
-
?
4-(4-dimethylaminophenylazo)benzoyl-LRGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-LRGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RIEGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RIIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RIIEGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
no hydrolysis at pH 6.0
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLEGIE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLVG-beta-(2-naphthyl)alanine-E-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLVG-beta-(2-naphthyl)alanine-E + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLVGFD-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLVGFD + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLVGFE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLVGFE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLVGFL-alpha-aminoadipic acid-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLVGFL-alpha-aminoadipic acid + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-RLVGWE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-RLVGWE + 5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Arg-Phe(NO2)-Leu + H2O
?
show the reaction diagram
pH 6.4, 37C, 2 mM cysteine, 1 mM EDTA
-
-
?
6-maleimidocaproic acid-L-Arg-Arg-Ala-Leu-Ala-Leu-Ala-camptothecin + H2O
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
-
major cleavage products are L-Leu-Ala-Leu-doxorubicin, L-Leu-doxorubicin, and doxorubicin
-
?
Abz-GIVRAK(Dnp)-OH + H2O
?
show the reaction diagram
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
-
-
?
Abz-GXXRZK(Dnp)-OH + H2O
?
show the reaction diagram
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
-
-
?
Abz-GXXZXK(Dnp)-OH + H2O
?
show the reaction diagram
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
-
-
?
Abz-GXZRXK(Dnp)-OH + H2O
?
show the reaction diagram
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
-
-
?
Abz-GZXRXK(Dnp)-OH + H2O
?
show the reaction diagram
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
-
-
?
Ac-Arg-Arg-4-methyl-7-amidocoumarin + H2O
Ac-Arg-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
Ac-His-Pro-Val-Lys-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
Ac-His-Pro-Val-Lys + 7-amino-3-carbamoyl-4-methylcoumarin
show the reaction diagram
-
assay at pH 5.5, 37C
-
?
acetyl-Arg-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
a synthetic substrate of caspase-3 and caspase-7
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
cleavage occurs at pH 4.0, but not at pH 7.5
-
?
acetyl-F-R-4-methylcoumarin-7-amide + H2O
acetyl-F-R + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
show the reaction diagram
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
show the reaction diagram
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
show the reaction diagram
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
show the reaction diagram
-
-
-
?
alpha-N-benzoyl-DL-Arg-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
amino acid-beta-naphthylamides + H2O
amino acid + beta-naphthylamine
show the reaction diagram
-
-
-
?
amyloid beta peptide + H2O
?
show the reaction diagram
-
cathepsin B is involved in degradation of amyloid beta peptides, its inhibition can lead to amyloid beta accumulation, an early trigger of Alzheimer's disease, cystatin C regulates the enzyme negatively, CysC ablation ameliorates amyloid beta-associated neuronal and synaptic deficits in hippocampal circuits, neuroprotective effects of CysC ablation depend on CatB, overview
-
-
?
amyloid beta precursor protein + H2O
?
show the reaction diagram
-
cathepsin B selectively cleaves the wild-type beta-secretase site but not the rare Swedish mutant beta-secretase site
-
-
?
amyloid precursor protein C-terminal fragment + H2O
?
show the reaction diagram
-
cathepsin B degraded C-terminal fragments regardless of phosphorylation
-
-
?
amyloid precursor protein intracellular domain + H2O
?
show the reaction diagram
-
-
-
-
?
antiprotease secretory leucoprotease inhibitor + H2O
cleaved SLP1 protein
show the reaction diagram
-
i.e. SLP1 protein, cleavage between residues Thr67 and Tyr68
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
poor substrate
-
-
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
show the reaction diagram
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
show the reaction diagram
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
show the reaction diagram
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
show the reaction diagram
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
-
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
Dorytheuthis bleekeri
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
show the reaction diagram
Dorytheuthis bleekeri
-
-
-
?
benzoyl-L-3-pyridyl-Ala-l-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-3-pyridyl-Ala-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-4-aminocyclohexy-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
benzoyl-L-4-aminomethyl-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminomethyl-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-4-guanidine-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-guanidine-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-4-piperidinyl-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-piperidinyl-Ala-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-Arg-beta-naphthylamide + H2O
benzoyl-L-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzoyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-L-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-His-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-N-dimethyl-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-N-dimethyl-His-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Arg-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-FR-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-L-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Phe-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Phe-Arg + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-phenylalanyl-arginine-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, activity at pH 5.0 is 80fold greater than with Arg-Arg
-
?
benzyloxycarbonyl-phenylalanyl-arginyl-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
37C, 1 mM DTT, 1 mM EDTA, pH 6.0
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
beta-lipotropin + H2O
hydrolyzed beta-lipotropin
show the reaction diagram
-
-
-
?
Boc-Asp-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Boc-Asp-Pro-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
Boc-Asp-Pro-Arg-4-methylcoumarin 7-amide + H2O
Boc-Asp-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumarin-7-amide + H2O
Boc-L-Leu-L-Lys-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
pH-dependence of reaction
-
?
Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin + H2O
Boc-Val-Leu-Lys + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
Boc-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
BODIPY FL casein + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate of Na-CP-3
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
an endoproteolytic substrate
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin hydrochloride + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin hydrochloride
show the reaction diagram
-
-
-
?
carbobenzoxy-Gly-Gly-Arg-naphthylamide + H2O
? + naphthylamine
show the reaction diagram
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
a fluorogenic substrate
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate of Na-CP-3
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
?
caspase 1 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
Cbz-FR-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
37C, pH 6.0, 200 mM NaCl, 1 mM EDTA, 5 nM DTT
-
?
Cbz-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Cbz-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
chemokine (C-C motif) ligand 20 + H2O
CCL20 1-66 isoform + ?
show the reaction diagram
-
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
?
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
show the reaction diagram
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
-
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
collagen IV of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
quenched fluorescent protein
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
D-Val-Leu-Arg-4-methylcoumarin 7-amide + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
show the reaction diagram
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
show the reaction diagram
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
show the reaction diagram
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
show the reaction diagram
-
-
-
?
DQ-collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
epsilon-aminocaproic acid-L-Leu-Gly-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-Gly + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-Phe-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
epsilon-aminocaproic acid-L-R-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-R + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
filaggrin + H2O
hydrolyzed filaggrin
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
a substrate of Na-CP-3
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
quenched fluorescent protein
-
-
?
gelatin + H2O
hydrolyzed gelatine
show the reaction diagram
-
-
-
?
globin + H2O
partially degraded globin
show the reaction diagram
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
show the reaction diagram
-
-
-
?
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
-
from goat and from buffalo
-
?
herpes simplex virus type 1 origin binding protein + H2O
herpes simplex virus type 1 origin binding protein 1
show the reaction diagram
-
53 kDa protein
50 kDa protein
?
histones + H2O
hydrolyzed histones
show the reaction diagram
-
-
-
?
L-Arg-L-Arg-4-nitroanilide + H2O
L-Arg-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
myelin basic protein + H2O
?
show the reaction diagram
-
-
-
?
myoglobin + H2O
hydrolyzed myoglobin
show the reaction diagram
-
-
-
?
myosin + H2O
hydrolyzed myosin
show the reaction diagram
-
-
-
?
myristoylated alanine-rich C kinase substrate + H2O
p40 + ?
show the reaction diagram
-
i.e. MARCKS
-
?
myristoylated alanine-rich C kinase substrate + H2O
?
show the reaction diagram
-
i.e. MARCKS
-
-
-
N,N-dimethyl hemoglobin + H2O
hydrolyzed N,N-dimethyl hemoglobin
show the reaction diagram
Dorytheuthis bleekeri
-
-
-
?
N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine-4-methyl-7-coumarylamide + H2O
N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine + 4-methyl-7-coumarylamine
show the reaction diagram
-
-
-
?
N-benzoyl-Arg-Arg-4-nitroanilide + H2O
N-benzoyl-Arg-Arg + 4-nitroaniline
show the reaction diagram
-
-
?
N-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzoyl-Val-Asn-Leu-7-amido-4-methylcoumarin + H2O
N-benzoyl-Val-Lys-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
the substrate represents the wild-type beta-secretase site
-
?
N-benzoyl-Val-Lys-Met-7-amido-4-methylcoumarin + H2O
N-benzoyl-Val-Lys-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
the substrate represents the wild-type beta-secretase site
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Mus musculus BALB/c
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-arginyl-L-arginyl-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
show the reaction diagram
-
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-lysine 4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-L-lysine + 4-nitrophenol
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg-beta-naphthylamide + H2O
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg + beta-naphthylamine
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Ile-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Val-Ile-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Ile-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Val-Ile-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-carbobenzoxy-L-lysine 4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-t-butyloxycarbonyl-Gln-p-nitrophenyl ester + H2O
N-t-butyloxycarbonyl-Gln + 4-nitrophenol
show the reaction diagram
-
-
-
-
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-Val-Lys-Lys-Arg-7-amido-4-trifluoromethylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
?
Nalpha-CBZ-Arg-Arg 7-amido-4-methylcoumarin + H2O
Nalpha-CBZ-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
1 mM DTT
-
?
neuropeptides + H2O
hydrolyzed neuropeptides
show the reaction diagram
-
such as Leu-enkephalin, beta-neoendorphin, alpha-neoendorphin, dynorphin(1-13), substance P
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide + H2O
?
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
show the reaction diagram
-
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, 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
-
-
?
phenylacetyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
phenylacetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
pro-rhoptry protein 2 + H2O
rhoptry protein 2 + propeptide
show the reaction diagram
-
-
-
?
Protamine + H2O
Hydrolyzed protamine
show the reaction diagram
-
-
-
?
protein rGSII-D88N + H2O
?
show the reaction diagram
-
-
-
?
protein rGSII-D88N + H2O
?
show the reaction diagram
-
degradation
-
-
?
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
Dorytheuthis bleekeri
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
degradation of tissue proteins within lysosomes
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
muscle proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
plays a role in cancer invasion and metastasis
-
-
-
Proteins + H2O
?
show the reaction diagram
-
enzyme activation and conversion of precursor proteins to their active form
-
-
-
proteoglycans + H2O
hydrolyzed proteoglycans
show the reaction diagram
-
-
-
?
serum albumin + H2O
partially degraded serum albumin
show the reaction diagram
-
-
-
?
sheep immunoglobulin heavy chain + H2O
hydrolyzed sheep immunoglobulin heavy chain
show the reaction diagram
-
-
-
?
sphingosine kinase-1 + H2O
?
show the reaction diagram
-
cleaves at histidine 122 and arginine 199
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
-
-
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides
-
-
?
Tos-Gly-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Tos-Gly-Pro-Arg + 4-methyl-7-aminocoumarin
show the reaction diagram
-
-
-
?
Tos-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
trypsinogen + H2O
trypsin + peptide
show the reaction diagram
-
-
-
?
trypsinogen + H2O
trypsin + ?
show the reaction diagram
-
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
?
trypsinogen activation peptide + H2O
?
show the reaction diagram
-
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
-
?
yolk protein + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
1 mM DTT, 2 mM EDTA, pH 6.8, 37C, 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-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, least preferred substrate
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, negligible hydrolysis
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
20 mM DTT, pH 5.5
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
37C, pH 6.0, 8 mM DTT, 352 mM KH2PO4, 48 mM Na2HPO4, 4 mM disodium EDTA
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
pH 5, 1 mM EDTA, 4 mM DTT
-
?
Z-Arg-Arg-cresyl violet + H2O
Z-Arg-Arg + cresyl violet
show the reaction diagram
-
-
-
?
Z-Arg-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
1 microM, pH 6.0, 10 nanoM cathepsin B
-
-
?
Z-Arg-Leu-7-amido-4-methylcoumarin + H2O
Z-Arg-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature
-
?
Z-Arg-Leu-7-amido-4-methylcoumarin + H2O
Z-Arg-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, less than 25% hydrolysis compared to Z-Arg-Val-7-amido-4-methylcoumarin
-
?
Z-Arg-Phe-7-amido-4-methylcoumarin + H2O
Z-Arg-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature
-
?
Z-Arg-Phe-7-amido-4-methylcoumarin + H2O
Z-Arg-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, less than 25% hydrolysis compared to Z-Arg-Val-7-amido-4-methylcoumarin
-
?
Z-Arg-Val-7-amido-4-methylcoumarin + H2O
Z-Arg-Val + 7-amino-4-methylcoumarin
show the reaction diagram
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, preferred substrate
-
?
Z-arginyl-arginyl-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
37C, pH 5.5, 5 mM DTT
-
?
Z-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
Z-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
laminin of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
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
?
-
-
preference for substrate cleavage through dipeptidyl pathway, influence of substrate P2-P1 residues
-
-
?
additional information
?
-
-
enzyme is involved in myoblast-myoblast fusion
-
-
?
additional information
?
-
-
cathepsin B can partially process the 48000 Da intermediate into 34000 Da mature cathepsin D
-
-
-
additional information
?
-
no degradation of hemoglobin
-
-
-
additional information
?
-
-
no reaction with Abz-GIVRPK(Dnp)-OH
-
-
-
additional information
?
-
-
no reaction with procarboxypeptidase and proelastase
-
-
-
additional information
?
-
this isoform encodes an inactive enzyme
-
-
-
additional information
?
-
-
cathepsin B is able to self-activate
-
-
-
additional information
?
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
-
additional information
?
-
-
absence of Ctsb significantly impairs development of high-grade invasive ductal carcinomas and reduces the metastatic burden in the lungs, and cancer cells lacking Ctsb exhibit significantly higher resistance to apoptosis induction by the lysosomotropic agent Leu-Leu-OMe
-
-
-
additional information
?
-
-
autocatalytic activation of the inactive proenzyme
-
-
-
additional information
?
-
-
cathepsin B belongs to the lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling. Cathepsin B is involved in matrix degradation at podosomes, cysteine protease inhibitors reduce matrix degradation and invasion in vitro
-
-
-
additional information
?
-
cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family with multiple biological functions
-
-
-
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 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 expressed in induced 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 plays a key role in parasite infection, overview
-
-
-
additional information
?
-
-
cathepsin B plays an essential role in the pathogenesis of fulminant hepatic failure, and the cathepsin B inhibitor CA-074me can attenuate apoptosis and liver injury, overview
-
-
-
additional information
?
-
-
cathepsin B secreted by activated microglia is closely associated with the MeHg-induced severe pyknotic changes of the cerebellar granule cells, overview. Cathepsin B is involved in apoptotic processes
-
-
-
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
?
-
differential regulation of snail cathepsin B transcript pre- and postparasite exposure, overview
-
-
-
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
?
-
-
effective inhibition of cathepsin B can decrease the severity of joint inflammation and to reduce the destruction of particular tissues in the rat model of antigen adjuvant-induced arthritis
-
-
-
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
?
-
-
inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, beta-secretase site of the amyloid precursor protein
-
-
-
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 has a principle function in gross protein degradation of internalized proteins within endo-lysosomes, but cathepsins are also involved in the processing of precursor proteins to biologically active peptides in endosomes of entero-endocrine cells. Cathepsin B, released form intestinal mucosa due to mechanical injury, plays an important role in extracellular matrix damage and the onset of postoperative ileus, an inevitable consequence of abdominal surgery, in that it contributes to disintegration of the basement membrane of the gastrointestinal tract in early post-traumatic phases. Cathepsin B is best known for its critical contribution to enhanced tumor cell invasion and metastasis, including colorectal carcinomas, by degradation of extracellular matrix components
-
-
-
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
?
-
-
under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells
-
-
-
additional information
?
-
-
cathepsin B is a lysosomal cysteine protease, a unique cysteine member showing dual roles as both endopeptidase and exopeptidase activities due to the presence of the occluding loop in structure
-
-
-
additional information
?
-
-
no activity with carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin by Na-CP-3, recombinant Na-CP-3 does not digest intact hemoglobin but digests globin fragments generated by prior hydrolysis with aspartic hemoglobinases
-
-
-
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
?
-
-
Boc-Val-Leu-Lys-4-methylcoumarin 7-amide is no substrate of catB1. CatB1 substrate specificity, homology modelling and molecular dynamics simulations of FhcatB1 interaction with peptide substrates, molecular modelling, overview. A P2 Ile residue positions the substrate optimally for interaction with catalytic residues of the enzyme, and the enzyme lacks an occluding loop His residue crucial for exopeptidase activity. The enzyme performs autolytic processing
-
-
-
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
-
-
-
additional information
?
-
-
no activity with benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
-
additional information
?
-
Trypanosoma brucei 90-13
-
cathepsin B plays a key role in parasite infection, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amyloid beta peptide + H2O
?
show the reaction diagram
-
cathepsin B is involved in degradation of amyloid beta peptides, its inhibition can lead to amyloid beta accumulation, an early trigger of Alzheimer's disease, cystatin C regulates the enzyme negatively, CysC ablation ameliorates amyloid beta-associated neuronal and synaptic deficits in hippocampal circuits, neuroprotective effects of CysC ablation depend on CatB, overview
-
-
?
amyloid beta precursor protein + H2O
?
show the reaction diagram
-
cathepsin B selectively cleaves the wild-type beta-secretase site but not the rare Swedish mutant beta-secretase site
-
-
?
caspase 1 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
-
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
collagen IV of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
myristoylated alanine-rich C kinase substrate + H2O
?
show the reaction diagram
-
i.e. MARCKS
-
-
-
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
show the reaction diagram
-
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
-
-
?
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
Dorytheuthis bleekeri
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
-
-
-
-
Proteins + H2O
?
show the reaction diagram
-
degradation of tissue proteins within lysosomes
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
turnover of intracellular proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
muscle proteins
-
-
-
Proteins + H2O
?
show the reaction diagram
-
plays a role in cancer invasion and metastasis
-
-
-
Proteins + H2O
?
show the reaction diagram
-
enzyme activation and conversion of precursor proteins to their active form
-
-
-
TNF-alpha + H2O
?
show the reaction diagram
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha
-
-
?
TNF-alpha + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides
-
-
?
Laminin + H2O
?
show the reaction diagram
-
laminin of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
additional information
?
-
-
enzyme is involved in myoblast-myoblast fusion
-
-
?
additional information
?
-
B2XVS9, Q5VJM8
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
-
additional information
?
-
-
absence of Ctsb significantly impairs development of high-grade invasive ductal carcinomas and reduces the metastatic burden in the lungs, and cancer cells lacking Ctsb exhibit significantly higher resistance to apoptosis induction by the lysosomotropic agent Leu-Leu-OMe
-
-
-
additional information
?
-
-
autocatalytic activation of the inactive proenzyme
-
-
-
additional information
?
-
-
cathepsin B belongs to the lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling. Cathepsin B is involved in matrix degradation at podosomes, cysteine protease inhibitors reduce matrix degradation and invasion in vitro
-
-
-
additional information
?
-
Q68J69
cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family with multiple biological functions
-
-
-
additional information
?
-
P07858
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 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 expressed in induced 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 plays a key role in parasite infection, overview
-
-
-
additional information
?
-
-
cathepsin B plays an essential role in the pathogenesis of fulminant hepatic failure, and the cathepsin B inhibitor CA-074me can attenuate apoptosis and liver injury, overview
-
-
-
additional information
?
-
-
cathepsin B secreted by activated microglia is closely associated with the MeHg-induced severe pyknotic changes of the cerebellar granule cells, overview. Cathepsin B is involved in apoptotic processes
-
-
-
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
?
-
A7LM75
differential regulation of snail cathepsin B transcript pre- and postparasite exposure, overview
-
-
-
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
?
-
-
effective inhibition of cathepsin B can decrease the severity of joint inflammation and to reduce the destruction of particular tissues in the rat model of antigen adjuvant-induced arthritis
-
-
-
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
?
-
-
inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, beta-secretase site of the amyloid precursor protein
-
-
-
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 has a principle function in gross protein degradation of internalized proteins within endo-lysosomes, but cathepsins are also involved in the processing of precursor proteins to biologically active peptides in endosomes of entero-endocrine cells. Cathepsin B, released form intestinal mucosa due to mechanical injury, plays an important role in extracellular matrix damage and the onset of postoperative ileus, an inevitable consequence of abdominal surgery, in that it contributes to disintegration of the basement membrane of the gastrointestinal tract in early post-traumatic phases. Cathepsin B is best known for its critical contribution to enhanced tumor cell invasion and metastasis, including colorectal carcinomas, by degradation of extracellular matrix components
-
-
-
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
?
-
-
under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells
-
-
-
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
?
-
Mus musculus C57BL/6
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
-
additional information
?
-
Trypanosoma brucei 90-13
-
cathepsin B plays a key role in parasite infection, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
a slight increase of activity (4.2%) is induced by 1 mM Ca2+
Mg2+
-
a slight increase of activity (3.3%) is induced by 1 mM Mg2+
monomethylmercuric cation
-
treatment leads to increased cathepsin B mainly in activated microglia which accumulate in the granule cell layer of the cerebellum
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1E,4E)-1-chloro-4-ethenyl-2-(trichloro-lambda4-tellanyl)hepta-1,4,6-trien-3-ol
-
-
(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)
-
-
(2E)-3-chloro-1-phenyl-2-(trichloro-lambda4-tellanyl)prop-2-en-1-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)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
(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
-
-
(2Z)-1,3-bis(4-ethoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
-
(2Z)-1,3-bis(4-methoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
-
(2Z)-1,3-diphenyl-4-(trichloro-llambda4-tellanyl)but-2-en-1-one
-
-
(3E)-2-bromo-3-(bromomethylidene)-2-(4-methoxyphenyl)-1-oxa-2l4-telluraspiro[3.5]nonane
-
-
(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-2l4-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
-
-
(3E)-4-chloro-3-[dichloro(4-methoxyphenyl)-l4-tellanyl]-2-methylbut-3-en-2-ol
-
-
(acetatato-kO)[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](pyridine)palladium(1+)
-
-
(acetatato-kO)[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](triphenylphosphane)palladium(1+)
-
-
(acetato)(isopropylamine)(2-((2dimethylamino)-methyl)phenyl)Pd(II)
-
-
(chloro)(isopropylamine)(2-((2dimethylamino)methyl)phenyl)Pd(II)
-
-
(chloro)(pryidinyl)(2-((2dimethylamino)methyl)phenyl)Pd(II)
-
-
(chloro)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN1] oxorhenium(V)
-
-
(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)
-
-
(triethylphosphine)gold(I) chloride
-
-
1,1,3-trichloro-2,4,5,6-tetrahydro-1H-1-benzotellurophene
-
-
1,10-phenanthroline
66% remaining activity at 1 mM, 68% remaining activity at 2 mM
1,10-phenanthroline
-
77.3% residual activity at 1 mM
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[(1Z,3E,5Z)-2-chloroocta-1,3,5,7-tetraen-1-yl]-lambda4-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-tosylamide-2-phenylethyl chloromethylketone
-
-
1-tosylamide-2-phenylethyl chloromethylketone
-
-
1-tosylamide-2-phenylethyl chloromethylketone
-
-
1-tosylamide-2-phenylethyl chloromethylketone
-
moderate effect
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
-
-
1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]-3-(ethoxycarbonyl)aziridine-2-carboxylic acid
-
-
1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]aziridine-2,3-dicarboxylic acid
-
-
2,12-diethyl-11-methylhexadecyl 2-ethyl-11-methylhexadecyl phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
2,2'-dipyridyl disulfide
-
-
2,2'-dipyridyl disulfide
-
-
2,2'-dipyridyl disulfide
-
-
2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
-
-
2-ethyldecyl 2-ethylundecyl phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
2-pentyl-1,2-thiazol-3(2H)-one
-
-
2-phenylisothiazol-3(2H)-one
-
-
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
-
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-([(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'''-methylamentoflavone
-
IC50: 0.00168 mM
4-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
-
IC50: 0.000005 mM
4-hydroxy-2-nonenal
-
0.015 mM, 76% loss of activity, formation of Michael adducts with C29 of A chain and H150 of B chain
5,5'-dithiobis-2-nitrobenzoic acid
-
-
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
5-amino-1-(phenylsulfonyl)-1H-pyrazol-3-yl thiophene-2-carboxylate
-
-
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl furan-2-carboxylate
-
-
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 furan-2-carboxylate
-
-
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
-
-
5-chloro-2-(2-chloro-4,5-dimethoxyphenethyl)isothiazol-3(2H)-one
-
-
-
5-chloro-2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
-
-
5-chloro-2-pentyl-1,2-thiazol-3(2H)-one
-
-
5-chloro-2-phenylisothiazol-3(2H)-one
-
-
-
7'',4'''-dimethylamentoflavone
-
IC50: 0.00055 mM
7-epiclusianone
-
a prenylated benzophenone isolated from pericarp hexane extract of dried fruits of Rheedia brasiliensis
aceto[2,6-bis[(butylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
-
-
aceto[2,6-bis[(methylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
-
-
aceto[2,6-bis[(phenylthio-kappaS)methyl]phenyl-kappaC]-, (SP-4-3)Pd(II)
-
-
acetyl-Asp-Glu-Val-Asp-CHO
-
complete DEVDase activity inhibition in brain cell supernatant
acetyl-DEVD-CHO
-
-
acetyl-Leu-Ile-arginal
-
IC50: 0.00015 mM
acetyl-Leu-Leu-lysinal
-
IC50: 0.00013 mM
acetyl-Leu-Phe-arginal
-
IC50: 0.0011 mM
acetyl-Leu-Phe-lysinal
-
IC50: 0.0001 mM
acetyl-Leu-Val-lysinal
-
IC50: 0.000004 mM
acetyl-Phe-Val-arginal
-
IC50: 0.000039 mM
acetyl-YVAD-chloromethyl ketone
-
caspase inhibitor, inhibition of enzyme contributes to neuroprotective properties of the inhibitor
AM4299A
-
irreversible inhibition, IC50: 0.000073 mM
AM4299B
-
irreversible inhibition, IC50: 0.000130 mM
amentoflavone
-
IC50: 0.00175 mM
AMF1
-
-
AMF2
-
-
AMF3
-
-
AMF4
-
IC50: 0.00062 mM
AMF5
-
-
ammonium 1-tribromo-1,3,2-dioxatellurolane
-
-
ammonium 1-trichloro-1,3,2-dioxatellurolane
-
-
antipain
-
93% inhibition at 1 microM
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
-
antipain
-
complete inhibition at 1 mM
APC-3316
-
kinetics, pH-dependence of inhibition
APC-5840
-
kinetics, pH-dependence of inhibition
APC-8754
-
kinetics, pH-dependence of inhibition
arsenite
-
i.e. arsenic trioxide, inhibits CatB in glioblastoma cells, 20% inhibition at 0.022 mM, 50% at 0.020 mM
auranofin
-
competitive, reversible inhibitor of cathepsin B
bafilomycin
-
-
-
bafilomycin A1
-
100 nM significantly inhibits activity
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-([(2R,3R)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-prolinate
-
-
benzyl N-([(2S,3S)-3-(ethoxycarbonyl)aziridin-2-yl]carbonyl)-L-leucinate
-
-
benzyl N-([(2S,3S)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-prolinate
-
-
benzyl N-[(3-carboxyaziridin-2-yl)carbonyl]-L-leucyl-L-prolinate
-
-
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
benzylamido-L-trans-epoxysuccinyl-Ile-O-benzyl ester
-
-
benzylamido-L-trans-epoxysuccinyl-Ile-Pro-OH
-
-
benzyloxycarbonyl-Arg-Ser-chloromethylketone
-
-
benzyloxycarbonyl-FA-fmk
-
benzyloxycarbonyl-FGNHO-Bz
-
benzyloxycarbonyl-L-Phe-Ala-fluoromethyl ketone
-
specific inhibitor
benzyloxycarbonyl-L-phenylalanyl-alanine-fluoromethylketone
-
inhibits cathepsin B, treatment stimulates proliferation of type-II pneumocytes and improves degenerative alterations in injured lung occurring with liver injury induced by D-GalN/TNF-alpha, overview
benzyloxycarbonyl-Leu-Leu-Tyr-CHN2
-
-
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Trp-Met-CHN2
-
-
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
bis(2-ethyldodecyl) phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
bis(2-ethylheptyl) phthalate
-
isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
BzlNH-tES-Ile-Pro-OBzl
-
-
BzlNH-tES-Ile-Pro-OH
-
-
CA-074
-
-
CA-074
-
specific inhibitor
CA-074
-
0.0005 mM
CA-074
a cathepsin B-specific inhibitor, inhibition CmCatB1
CA-074
-
0.001 mM
CA-074
-
irreversible cathepsin B inhibitor
CA-074
-
cathepsin B-specific inhibitor
CA-074
-
a selective cell-impermeable cathepsin B inhibitor
CA-074
-
a cathepsin B inhibitor
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
-
-
CA-074 Me
-
99.4% inhibition at 0.010 mM in cell lysates
CA-074 Me
-
a specific cathepsin B inhibitor
Ca-074 methyl ester
-
-
CA-074-Me
-
Cat B-selective inhibitor
CA-074-Me
-
suppresses microglia conditioned culture medium-induced glioma cell death
CA-074-Me
-
strong inhibition
CA-074-Me
-
CA-074Me clearly inhibits cath-B expression in the subcutaneous heteroplastic pancreatic carcinoma model, and demonstrates an anti-neoplastic and anti-angiogenesis effect, overview
CA-074-Me
-
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
-
a specific inhibitor, inhibits pro-interleukin-1beta processing in microglia
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
-
a potent and specific CtsB inhibitor, CtsB inhibition blunts AKT phosphorylation in activated hepatic stellate cells in response to platelet-derived growth factor
CA-074-Me
-
cathepsin B inhibitor IV. Inhibition of cathepsin B blocks MEK1 cleavage induced by anthrax lethal toxin through delaying LeTx release into the cytoplasm. The cathepsin B inhibitor prevents cell death induced by anthrax lethal toxin in RAW 264.7 macrophages
CA-074-Me
-
i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester
CA-074-Me
-
-
CA-074-Me
-
in vivo inhibition
CA-074-Me
-
-
CA-074-OMe
-
blocks cysteine cathepsins in addition to CatB in in primary human antigen-presenting cells
CA-074Me
-
-
CA-074Me
-
a specific inhibitor for cathepsin B
CA-074Me
-
a selective cell-permeable cathepsin B inhibitor
CA-074Me
-
a cathepsin B inhibitor
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
CA-074Me
-
-
CA028
-
irreversible inhibition, IC50: 0.000140 mM
CA030
-
irreversible inhibition, IC50: 0.00000438 mM
CA030
-
-
CA030
-
i.e. ethoxy-L-trans-epoxysuccinyl-Ile-Pro-OH
CA074
-
kinetic analysis
CA074
-
high specificity, 34000fold more effective on enzyme than on cathepsin X
CA074
-
irreversible inhibition, IC50: 0.00000194 mM
CA074
-
an irreversible CB inhibitor
CA074Me
-
inhibition affects myotube size and number, fusion-related creatine phosphokinase activity and myosin heavy chain protein, inhibition occurs at each stage of differentiation
CA074Me
-
-
CA074Me
-
cathepsin B specific inhibitor
Ca2+
-
; 40% inhibition at 2 mM
CAA0445
-
noncovalent-type, specific
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
Cabin-A1
-
i.e. SLHTLF, peptide derived from human serum albumin
Cabin-A2
-
i.e. FQNAL, peptide derived from human serum albumin
canecystatin-1
-
-
-
canecystatin-4
-
-
-
carbobenzoxy-Phe-NH-CH2CN
-
reversible, 50% inhibition at 0.062 mM
cathepsin B inhibitor III
-
i.e. L-trans.epoxysuccinyl(propylamide)-Ile-Pro or 1-[3-methyl-2-[[3-(propylcarbamoyl)oxirane]-2-carbonyl]amino]pentanoylpyrrolidine-2-carboxylic acid
cathepsin B inhibitor IV
-
i.e. CA074me or methyl 1-[3-methyl-2-[[3-(propylcarbamoyl)oxirane]-2-carbonyl]amino]pentanoylpyrrolidine-2-carboxylate, bone marrow-derived macrophages treated with the cathepsin B-specific chemical inhibitor CA074 methyl ester secret significantly less TNF-alpha than wild-type or nontreated macrophages
cathestatin A
-
irreversible inhibition, IC50: 0.000260 mM
cathestatin B
-
irreversible inhibition, IC50: 0.000280 mM
cathestatin C
-
irreversible inhibition, IC50: 0.000114 mM
Cbz-Phe-Ser(OBzl)-CHN2
-
cysteine protease inhibitor 1 (CP-1), effective inhibition at 0.05 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
-
chicken cystatin
-
-
-
chloro(diethylphenylphosphine)gold(I)
-
-
chloro(ethyldiphenylphosphine)gold(I)
-
-
chloro(triphenylphosphine)gold(I)
-
-
chloro(tris(p-fluorophenyl)phosphine)gold(I)
-
-
chloro-[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
-
-
Chloroquine
-
-
Chloroquine
-
-
chloro[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](pyridine)palladium(1+)
-
-
chloro[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](triphenylphosphane)palladium(1+)
-
-
chloro[4-(diphenylphosphino-kappaP)benzenamine]gold(I)
-
-
chloro[4-(diphenylphosphino-kappaP)benzoato]gold(I)
-
-
chloro[diphenyl(phenylmethyl)phosphine]gold(I)
-
-
chloro[diphenyl[4-(2-phenyl-1,3-dioxolan-2-yl)phenyl]phosphine-kappaP]gold(I)
-
-
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzamide]gold(I)
-
-
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzeneacetamide]gold(I)
-
-
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzenepropanamide]gold(I)
-
-
chloro[tris(p-methoxyphenyl)phosphine]gold(I)
-
-
chloro[tris(pentafluorophenyl)phosphine]gold(I)
-
-
chloro[[1,1'-biphenyl]-4-yldiphenylphosphine]gold(I)
-
-
chymostatin
-
85% inhibition at 5 microM
chymostatin
-
-
chymostatin
-
-
chymostatin
-
-
chymostatin
-
80% inhibition at 6 microM
chymostatin
-
-
chymostatin
-
-
chymostatin
-
-
CID 11834381
-
-
CID 11834389
-
-
CID 11834392
-
-
CID 1506381
-
-
CID 2212050
-
-
CID 286532
-
-
CID 2998380
-
-
CID 3236798
-
-
CID 3240114
-
-
CID 3241895
-
-
CID 3243025
-
-
CID 3243128
-
-
CID 3243168
-
-
CID 3250046
-
-
CID 3685806
-
-
CID 5293426
-
-
CID 573353
-
-
CID 646525
-
-
CID 646749
-
-
CID 647501
-
-
CID 647599
-
-
CID 648315
-
-
CID 651936
-
-
CID 653297
-
-
CID 653316
-
-
CID 653862
-
-
CID 654815
-
-
CID 655490
-
-
CID 658111
-
-
CID 658152
-
-
CID 658724
-
-
CID 658964
-
-
CID 660829
-
-
CID 66541
-
-
CID 665480
-
-
CID 714967
-
-
CID 794694
-
-
CID 971438
-
-
CLIK148
-
-
CPI-H
-
peptide inhibitor of 13 kDa from rabbit skeletal muscle, noncompetitive
-
CPI-L
-
peptide inhibitor of 23 kDa from rabbit skeletal muscle, noncompetitive
-
Cu2+
-
-
Cu2+
-
-
Cu2+
-
32% residual activity at 1 mM
Cystatin
-
poor inhibitor, 51% inhibition at 100 nM
-
Cystatin
-
Ki: 29 nM
-
Cystatin
-
-
-
Cystatin
-
-
-
Cystatin
binding sequence is FFEYDGVVSGGPYLGK, by mass spectrometric analysis
-
Cystatin
-
the enzyme retains 10% and 5% of its initial activity, after 30 min of incubation at 37C, in the presence of 75 and 100 nM recombinant cystatin, respectively
-
cystatin C
-
Porphyromonas gingivalis interrupts the interaction of cathepsin B with its inhibitor cystatin
-
cystatin C
-
CysC or CST3, an endogenous inhibitor of cysteine proteases, including cathepsin B
-
cystatin C
-
an endogenous inhibitor of cysteine cathepsins, expression patterns of cathepsin B and cystatin C
-
cystatin C
-
-
-
DCG-04
-
an E-64-type inhibitor, inhibits both mature cathepsin B and its zymogen
di-(2-ethylhexyl)phthalate
-
non-competitive inhibitor
diacetato(2-((2dimethylamino)methyl)phenyl)-Au(III)
-
-
diaceto[2-[(2-pyridinyl-kappaN)methyl]-phenyl-kappaC]Au(III)- (SP-4-3)
-
-
dibutyl phthalate
-
non-competitive inhibitor
dichloro(2-((2dimethylamino)methyl)phenyl)Au(III)
-
-
dichloro[2-[(2-pyridinyl-kappaN)methyl]phenyl-kappaC]Au(III)
-
-
Dimethylsulfoxide
-
-
doxorubicin
-
-
E-64
-
irreversible inhibition, IC50: 0.000055 mM
E-64
-
irreversible inhibitor
E-64
a cysteine protease inhibitor, inhibition of CmCatB1
E-64
-
broad-spectrum cysteine protease inhibitor, complete inhibition
E-64
-
a broad cysteine protease inhibitor
E-64
-
an irreversible cysteine protease inhibitor
E-64
-
inhibition of cathepsin B greatly improves the developmental competence of bovine oocytes and increases the number of high-quality embryos, overview
E-64
-
complete inhibition at 1 mM
E-64
-
i.e. L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane, irreversible inhibitor
E-64c
-
irreversible inhibition, IC50: 0.00000870 mM
E-64d
-
-
E-64d
-
i.e. (L-3-trans-ethoxycarbonyloxirane-2-carbonyl)-L-leucine(3-methylbutyl)amide
E64
-
kinetic analysis
E64
-
kinetics, pH-dependence of inhibition
E64c
-
-
E64c
-
the (2S,3S)-3-(L-[N-(3-methylbutyl)amino]leucyl) side chain binds at the S1 and S3 subsites
EDTA
89% remaining activity at 1 mM, 80% remaining activity at 2 mM
Elastatinal
-
-
Elastatinal
-
-
estatin A
-
irreversible inhibition, IC50: 0.000270 mM
estatin B
-
irreversible inhibition, IC50: 0.000320 mM
ethoxy-L-trans-epoxysuccinyl-Gly-Pro-OH
-
-
ethoxy-L-trans-epoxysuccinyl-Ile-Ala-OH
-
-
ethoxy-L-trans-epoxysuccinyl-Ile-Ile-OH
-
-
ethoxy-L-trans-epoxysuccinyl-Ile-OH
-
-
ethoxy-L-trans-epoxysuccinyl-Thr-Ile-OH
-
-
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 1-[(2R)-2-((1S)-1-(acetyloxy)-2-[((N-[(2,4-difluorophenyl)carbonyl]-L-phenylalanyl)amino)oxy]-2-oxoethyl)pentanoyl]prolinate
-
IC50: 4.4 mM
ethyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
-
-
EtO-tES-Gly-Pro-OH
-
-
EtO-tES-Ile-Ala-OH
-
-
EtO-tES-Ile-Ile-OH
-
-
EtO-tES-Ile-OH
-
-
EtO-tES-Ile-Pro-OH
-
CA-030
Fe2+
-
79.9% residual activity at 1 mM
Fe3+
-
82.3% residual activity at 1 mM
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
Gly-Pro-Phe-Pro-Ile
-
amino acids 203-207 of bovine beta-casein, competitive
H2O2
-
-
heparin
-
inhibition is strongly dependent on pH, no inhibition above pH 7.0
Hg2+
-
-
HIF
-
IC50: 0.00058 mM
HNO
-
from Angeli's salt or induced by LPS and IFN-gamma in RAW macrophages, causes DTT-irreversible inhibition and covalently and permanently inactivation of cathepsin B. Cathepsin B activity is reduced to 53%, 25%, and 57% of maximal activity in nonstimulated, LPS-, and IFN-gamma-treated cells, respectively. Endogenous NO production can provide direct protection for the less reactive protein cysteines by scavenging HNO. Additionally, endogenous cellular production of NO can rescue enzyme function by protective nitrosation of cysteines prior to exposure to HNO
human albutensin A
-
i.e. AFKAWAVAR
human cystatin A
-
-
-
human cystatin B
-
-
-
Human cystatin C
-
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
-
concentrations above10 mM significantly decrease activity
iodoacetic acid
-
-
iodoacetic acid
-
100% inhibition at 0.5 mM
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
complete inhibition at 1 mM
iodoacetic acid
-
complete inhibition at 1 mM
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
-
E-64
L-tosylphenylalanylchloromethane
-
-
L-trans-epoxysuccinyl-3,5-diiodo-L-tyrosylamido(3-methyl)-butane
-
compound 13b
L-trans-epoxysuccinyl-3,5-diiodo-L-tyrosylamido(3-methyl)-butane ethylester
-
compound 13a
L-trans-epoxysuccinyl-Ile-Pro-methyl ester
-
complete inhibition at 0.025 mM
Leupeptin
-
98% inhibition at 1 microM
Leupeptin
-
-
Leupeptin
-
-
Leupeptin
-
-
Leupeptin
-
Ki: 0.15-0.17 nM
Leupeptin
-
-
Leupeptin
-
-
Leupeptin
-
-
Leupeptin
4% remaining activity at 0.010 mM, 1% remaining activity at 0.1 mM
Leupeptin
-
IC50: 0.0000213 mM
Leupeptin
-
-
Leupeptin
-
42.5% residual activity at 0.1 mM
leupeptine
-
-
-
lipopolysaccharides
-
-
-
malonato(2-((2dimethylamino)methyl)phenyl)Au(III)
-
-
MeO-Gly-Gly-Leu-NH-tES-Leu-Pro-OH
-
NS-134
methoxy-Gly-Gly-L-Leu(2S,3S)-trans-epoxysuccinyl-L-Leu-L-Pro-OH
-
selective for cathepsin B over cathepsin L
methyl 3-(4,5-dichloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-4-methyl-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
-
-
methyl 4-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)butanoate
-
-
methyl 6-(3-(propyldisulfanyl)acrylamido)hexanoate
-
-
-
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
-
-
MG-132
-
-
Mg2+
-
-
Mg2+
-
; 50% inhibition at 2 mM
mizaridine
-
IC50: 0.00205 mM
Mn2+
-
-
Mn2+
-
10% inhibition at 8 mM, no inhibition at 2 mM
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-(3-methyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
-
IC50: 0.447 mM
N-(3-phenyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
-
IC50: 0.074 mM
N-(L-3-trans-carboxyoxirane-2-carbonyl)-Ile-Pro
-
CA-030
-
N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucylamino-3-methylbutane
-
E64c
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-Ile-Pro
-
CA-074
-
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-Ile-Pro
-
CA-074
-
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
CA-074
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
CA-074; CA-074; CA-074; CA-074
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
-
i.e. CA074, a cathepsin B-selective inhibitor
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline
-
i.e. CA074
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-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
-
i.e. CA074Me, a cathepsin B-selective inhibitor
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
-
i.e. CA074Me
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-(butoxycarbonyl)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-(ethoxycarbonyl)oxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
-
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-([(2R,3R)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-arginine
-
-
N-([(2R,3R)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
-
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-([(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
-
N-([(2S,3S)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-leucine
-
-
N-([(2S,3S)-3-carboxyoxiran-2-yl]carbonyl)-L-leucyl-L-proline
-
-
N-benzyl-N,N-diethylethanaminium 1-trichloro-4-chloro-2,3-dihydro-2-oxatellurophene
-
-
N-benzyl-N,N-diethylethanaminium 2,2,2,4-tetrachloro-2,5-dihydro-2lambda6-[1,2]-oxatellurolinate complex
-
-
N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
-
N-chloroacetyl-Gly-Leu-OH
-
-
N-chloroacetyl-Leu-Leu-OH
-
-
N-chloroacetyl-Leu-Leu-OMe
-
-
N-chloroacetyl-Lys-Leu-OH
-
-
N-chloroacetyl-Phe-Leu-OH
-
-
N-chloroacetyl-Phe-Met-OH
-
-
N-chloroacetyl-Ser-Leu-OH
-
-
N-ethylmaleimide
-
no inhibition at 1 mM
N-ethylmaleimide
-
no inhibition at 1 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
concentrations above10 mM significantly decrease activity
N-p-tosylphenyl-L-lysine-chloromethane
-
-
N-phenyl-3-(propyldisulfanyl)-3-chloro-acrylamide
-
-
-
N-phenyl-3-(propyldisulfanyl)acrylamide
-
-
-
n-propyl-(2S,3S)-trans-epoxysuccinyl-L-Ile-OH
-
kinetic analysis
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-lysyl chloromethylketone
-
-
N-tosyl-phenylalanine chloromethylketone
-
-
N-tosyl-phenylalanine chloromethylketone
-
-
N-tosyl-phenylalanine chloromethylketone
-
-
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
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-[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
-
-
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
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
Ni2+
-
26.7% residual activity at 1 mM
NS-196
-
0.0005 mM
oryzacystatin-1
-
-
-
oryzacystatin-1 clone A10
-
-
-
Os(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
-
i.e. OSPTAC
-
oxalo-RAPTA
-
ruthenium(II)-arene compound
oxidized glutathione
-
concentrations above10 mM significantly decrease activity
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-Chloromercuriphenyl sulfonic acid
-
-
p-Chloromercuriphenyl sulfonic acid
-
-
p-hydroxymercuribenzoate
-
-
penetratin
-
-
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
Peptidyl chloromethylketones
-
-
peptidyl diazomethyl ketone derivatives
-
-
-
peptidyl diazomethyl ketone derivatives
-
peptidyl diazomethanes
-
phenylmethanesulfonyl fluoride
-
no inhibition at 0.1 mM
phenylmethanesulfonyl fluoride
-
27-33% inhibition at 0.5 mM
phenylmethanesulfonyl fluoride
-
18% inhibition in the presence of 10 microM
phenylmethanesulfonyl fluoride
-
no inhibition at 10 microM
phenylmethanesulfonyl fluoride
-
no inhibition at 0.5 mM
phenylmethylsulfonyl fluoride
-
62.8% residual activity at 1 mM
PMSF
98% remaining activity at 0.5 mM, 93% remaining activity at 1 mM
PrnNH-tES-Ile-Pro-OBzl
-
-
PrnNH-tES-Ile-Pro-OH
-
CA-074
PrnNH-tES-Ile-Pro-OMe
-
-
Pro-Phe-Pr-Gly-Pro-Ile
-
amino acids 61-66 of bovine beta-casein, competitive
propylcarbonyl-L-trans-epoxysuccinyl-Ile-O-benzyl ester
-
-
propylcarbonyl-L-trans-epoxysuccinyl-Ile-Pro-O-methyl ester
-
-
Proteinase inhibitors
-
from potato tuber
-
Proteinase inhibitors
-
from rat, human, tuna fish, toad, chicken
-
Proteinase inhibitors
-
from chickens egg white
-
PRT2005
-
commercial peptidyl ketone inhibitors, Prototek, 50% inhibition at less than 0.001 mM
-
PRT2253
-
commercial peptidyl ketone inhibitors, Prototek, 50% inhibition at less than 0.001 mM
-
RAPTA-BC
-
ruthenium(II)-arene compound
RAPTA-BI
-
ruthenium(II)-arene compound
RAPTA-C
-
i.e. carbo-RAPTA, ruthenium(II)-arene compound
RAPTA-H
-
ruthenium(II)-arene compound
-
RAPTA-Me+C
-
ruthenium(II)-arene compound
RAPTA-NH3
-
ruthenium(II)-arene compound
RAPTA-OH
-
ruthenium(II)-arene compound
RAPTA-pentaOH
-
binding structure from cyrstal structure of the inhibitor bound to cathepsin B, overview
RAPTA-T
-
ruthenium(II)-arene compound
RAPTA-TBMe
-
ruthenium(II)-arene compound
RAPTA-TBOH
-
ruthenium(II)-arene compound
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
-
sheep cystatin B
-
-
-
sodium chloro[[4,4',4''-(phosphinidyne-kappaP)tris[benzenesulfonato]]aurate]
-
-
Soybean trypsin inhibitor
-
51.2% residual activity at 0.1 g/l
-
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
-
-
TMC-52A
-
irreversible inhibition, IC50: 0.000320 mM
TMC-52B
-
irreversible inhibition, IC50: 0.000200 mM
TMC-52C
-
irreversible inhibition, IC50: 0.000460 mM
TMC-52D
-
irreversible inhibition, IC50: 0.000280 mM
tokarimide A
-
IC50: 0.0000624 mM
-
trans-cis-cis-[RuCl2(DMSO)2(2-amino-5-methyl-thiazole)2]
-
i.e. (PMRu52), a ruthenium(II) compound acting as a strong inhibitor of cathepsin B, crystal structure and binding structure analysis, overview
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
E-64, 43% remaining activity at 0.005 mM, 32% remaining activity at 0.020 mM, 2% remaining activity at 0.030 mM
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
-
E-64
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
E-64; E-64; E-64
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
-
E-64, 63.2% inhibition at 0.010 mM in cell lysates
trans-epoxysuccinyl-L-leucyl-smido(4-guanidino)butane
E-64
trans-epoxysuccinyl-leucylamido(4-guanidino)butane
-
-
trichloro(dioxoethylene-O,O')tellurate
-
-
triethylphosphine(2,3,4,6-tetra-O-acetyl-beta-1-D-thiopyranosato-S)gold(I)
-
auranofin
Urea
-
inactivated at 3 M
WF14861
-
irreversible inhibition, IC50: 0.000016 mM
-
WF14865A
-
irreversible inhibition, IC50: 0.0000084 mM
WF14865B
-
irreversible inhibition, IC50: 0.000013 mM
-
wortmannilactone E
-
i.e. (19S)-(4S,7R)-7-[(1E,3E,5E,7E)-8-[(2S,5S,6S)-5,6-dihydro-5-hydroxy-3,5,6-trimethyl-2H-pyran-2-yl]nona-1,3,5,7-tetraen-1-yl]-4,6,7-trimethyl-2-oxabicyclo[2.2.1]heptane-3,5-dione, isolated from the culture medium of the soil filamentous fungus Talaromyces wortmannii, Chuxiong, Yunnan Province, China. Determination of structure and relative configuration by 1D- and 2D-NMR techniques, overview
wortmannilactone F
-
i.e. (19R)-(4S,7R)-7-[(1E,3E,5E,7E)-8-[(2S,5R,6S)-5,6-dihydro-5-hydroxy-3,5,6-trimethyl-2H-pyran-2-yl]nona-1,3,5,7-tetraen-1-yl]-4,6,7-trimethyl-2-oxabicyclo[2.2.1]heptane-3,5-dione, isolated from the culture medium of the soil filamentous fungus Talaromyces wortmannii, Chuxiong, Yunnan Province, China. Determination of structure and relative configuration by 1D- and 2D-NMR techniques, overview
wortmannilactone G
-
i.e. methyl (2R)-2-[(3R,4R)-3-[(1E,3E,5E,7E)-8-[(2S,3R,6S)-3,6-dihydro-3-hydroxy-3,5,6-trimethyl-2H-pyran-2-yl]nona-1,3,5,7-tetraen-1-yl]-3,4-dimethyl-5-oxotetrahydrofuran-2-yl]propanoate, isolated from the culture medium of the soil filamentous fungus Talaromyces wortmannii, Chuxiong, Yunnan Province, China. Determination of structure and relative configuration by 1D- and 2D-NMR techniques, overview
wortmannilactone H
-
i.e. (4S,7R)-7-[(1E,3E,5E,7E)-8-[(2S,3R,6S)-3,6-dihydro-3-hydroxy-3,6-dimethyl-2H-pyran-2-yl]nona-1,3,5,7-tetraen-1-yl]-4,6,7-trimethyl-2-oxabicyclo[2.2.1]heptane-3,5-dione, isolated from the culture medium of the soil filamentous fungus Talaromyces wortmannii, Chuxiong, in Chinas Yunnan Province. Determination of structure and relative configuration by 1D- and 2D-NMR techniques, overview
YM 51084
-
IC50: 0.000012 mM
-
Z-Arg-Gly-Pro-Agly-Gly-Glu-OMe
-
-
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-Arg-Leu-His-Agly-Ile-Val-OMe
-
-
Z-Arg-Leu-Phe-Agly-Val-Ala-OMe
-
-
Z-Arg-Leu-Val-Agly-Gly-Asp-OMe
-
-
Z-Arg-Leu-Val-Agly-Gly-Glu-OMe
-
-
Z-Arg-Leu-Val-Agly-Ser-Ala-OMe
-
-
Z-Arg-Nle-Pro-Agly-Gly-Glu-OMe
-
-
Z-Arg-Nle-Val-Agly-Gly-Glu-OMe
-
-
Z-Phe-Ala-CH2-O-CO-(2,4,6-trimethyl)-Ph
-
-
Z-Phe-Ala-CH2-O-CO-(2,5-(CF3)2)-Ph
-
-
Z-Phe-Ala-CH2-O-CO-(2,6-(CF3)2)-Ph
-
-
Z-Phe-Cys(SBzl)-CH2-O-CO-(2,6-(CF3)2)-Phe
-
-
Z-Phe-Gly-NHO-Bz
-
an inhibitor of both cathepsins B and L, causes death of many cell types
Z-Phe-Lys-CH2-O-CO-(2,4,6-trimethyl)-Ph
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
Zn2+
-
; 80% inhibition at 2 mM
Zn2+
-
14.7% residual activity at 1 mM
[(1-methyl-5-phenyl-1H-1,4-benzodiazepin-2(3H)-one)PdCl]2
-
-
[(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
-
-
[(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)Pd(1,3,5-triaza-7-phosphoadamantane)Cl]
-
-
[(benzyl(methyl)sulfane)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
-
-
[(N,N-dimethyl-1-phenylmethanamine)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
-
-
[(N,N-dimethyl-1-phenylmethanamine)Pd(1,3,5-triaza-7-phosphoadamantane)Cl]
-
-
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
-
-
[2-(1-benzyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](chloro)(pyridine)palladium(1+)
-
-
[2-(1-benzyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](chloro)(triphenylphosphane)palladium(1+)
-
-
[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
[imidazoleH][trans-Ru(imidazole)2Cl4]
-
i.e. KP1019
-
[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
-
-
[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
[N-benzyl-N,N-diethylethanaminium]2 hexachloro-lambda6-tellane
-
-
[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-1,4-benzodiazepin-2(3H)-one)2(m-1,2-ethanebis(diphenylphosphine))Cl2]
-
structure analysis by NMR spectroscopy and in the solid state by X-ray crystallography; structure analysis by NMR spectroscopy and in the solid state by X-ray crystallography. It inhibits cathepsin B, and also K562 leukemia cells with an IC50 value of 0.0043 mM after 1 h exposure
-
[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]
-
-
-
Mn2+
-
85.4% residual activity at 1 mM
additional information
-
not inhibitory: Z-FY(tert-butyl)-CHN(2)
-
additional information
-
analysis of further dipeptidyl nitriles as selective inhibitors
-
additional information
-
no inhibition with N-chloroacetyl-Gly-Gly-OH
-
additional information
no inhibition with pepstatin A at 0.005 and 0.1 mM
-
additional information
no inhibition of CmCatB1 by PMSF, leupeptin, pepstatin A, ethanol and DMSO
-
additional information
-
ruthenium(II)-arene compounds behave as powerful inhibitors
-
additional information
-
inhibitory activities of N-cyano-tetrahydro-pyridazine derivatives, docking studies, overview
-
additional information
-
inhibitor screening and docking studies to cathepsin B, overview. Predicted bioactivities of inhibitor candidates and molecular mechanics
-
additional information
-
the inhibition of cathepsin B causes accumulation of 26-kDa pro-TNF-containing vesicles
-
additional information
-
inhibition of cathepsin B by antitumor ruthenium(II)-arene compounds, mechanisms of binding/inhibition, overview
-
additional information
-
isolation and identification of a protein inhibitor of cathepsin B from Pseudomonas sp. strain PB01, phylogenetic distribution in Pseudomonas species, overview
-
additional information
-
inhibitor screening, overview
-
additional information
-
alpha-1-antitrypsin aerosolised augmentation abrogates neutrophil elastase-induced expression of cathepsin B in vivo and in vitro
-
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
-
no inhibition of cathepsin B by SDF-1 in vivo
-
additional information
-
95-100% enzyme inhibition is required to cause neuroblastoma cell death
-
additional information
No effects on cathepsin B activity by human chorionic gonadotropin and 17beta-estradiol
-
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 assement of inhbitor binding at the SN-site of cathepsin B, overview
-
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
-
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
-
growth inhbition of B-16 cells by the palladacycle compounds, overview
-
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
-
cathepsin B inhibitory activity of tetraene lactones from the fungus Talaromyces wortmannii, overview
-
additional information
-
no inhibition by human cystatin B
-
additional information
-
no inhibition of CatB by soybean cysteine protease inhibitor
-
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
-
inhibition of cathepsin B increases cell viability in the presence of imatinib
-
additional information
-
not inhibited by oryzacystatin-1 N-terminal deletion, reverse mutant 1 (T30I), reverse mutant 2 (Q97L), and reverse mutant 3 (T30I, Q97L)
-
additional information
-
not inhibited by dithiothreitol, L-cysteine, EDTA, and EGTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Dimercaptopropanol
-
-
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
activates
2-mercaptoethylamine
-
-
asparaginyl endopeptidase from Schistosoma mansoni
-
-
cysteamine
-
activates
cysteamine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
cysteine
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
the presence of dithiothreitol at concentrations of more than 10 mM significantly increases activity at pH 4.0
dithiothreitol
-
required to reduce the enzyme to its catalytically active form
EDTA
-
activates
EDTA
-
activates
EDTA
-
activates
EDTA
-
no effect at 0.5 mM
EDTA
-
activates in presence of thiol compound
EDTA
-
activates
emodin
-
i.e. 1,3,8-trihydroxy-6-methylanthraquinone, emodin at apoptosis-inducing concentrations causes expression and activation of cathepsin B protein
glutathione
-
activates
glutathione
-
activates
glutathione
-
activates
glutathione
-
activates
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
interferon-gamma
-
-
-
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
Kainic acid
-
1.25-5 nM
L-cysteine
-
cathepsin B is activated at 22C for 5 min in 100 mM sodium acetate, 1 mM DTT, 2 mM EDTA, 4 mM cysteine, pH 5.5
pepsin A
-
-
-
reduced glutathione
-
the presence of reduced glutathione at concentrations of more than 10 mM significantly increases activity at pH 4.0
thioglycerol
-
activates
thioglycerol
-
activates
thiol compounds
-
-
thiol compounds
-
required for full activity
thiol compounds
-
required for full activity
thiol compounds
-
required for full activity
thiol compounds
-
required for full activity
thiol compounds
-
absolute requirement
thiol compounds
-
required for full activity
thiol compounds
-
absolute requirement
thiol compounds
-
required for full activity
thiol compounds
-
required for full activity
thiol compounds
-
required for full activity
thiol compounds
-
-
thiol compounds
-
required for full activity
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)
-
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
additional information
soyacystatin N induces expression of CmCatB1, but not of CmCatB2; soyacystatin N induces expression of CmCatB1, but not of CmCatB2
-
additional information
-
cell treatment with attenuated bacillus Calmette-Guerin increases enzyme expression and activity
-
additional information
-
Schistosome asparaginyl endopeptidase, i.e. legumain, is not essential for cathepsin B1 activation in vivo
-
additional information
-
bafilomycin A1 induces lysosome-associated podosome-like structures and promotes degradation of extracellular gelatin
-
additional information
-
activator buffer contains 5 mM EDTA, 10 mM DTT, pH 5.2
-
additional information
the enzyme expression is induced by virus, e.g. Scophthalmus maximus rhabdovirus, SMRV, or UV-inactivated grass carp hemorrhage virus, GCHV, by poly I:C, and lipopolysaccharide, overview. SMRV upregulation takes place predominantly in spleen, head kidney, posterior kidney, intestine, gill, and muscle
-
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
3.5fold higher up-regulation of cathepsin B transcript in resistant than in the susceptible snail after Schistosoma mansoni parasite exposure
-
additional information
-
neutrophil elastase induces expression of cathepsin B in vivo and in vitro
-
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
-
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
serum-starvation increases cathepsin B-like activation in zebrafish follicles, not due to an increase in gene expression. No effects on cathepsin B activity by human chorionic gonadotropin and 17beta-estradiol
-
additional information
-
deglycosylation enhances CmCatB activity, but compromises CmCatB stability
-
additional information
-
the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview
-
additional information
-
during in vivo liver fibrogenesis, caused by CCl4 administration, CtsB expression increases in hepatic stellate cells but not in hepatocytes
-
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0161
2,4-dinitrophenyl-GARFW-OH
-
pH 6.0, 37C
0.0096
2,4-dinitrophenyl-GDRFW-OH
-
pH 6.0, 37C
0.012
2,4-dinitrophenyl-GERFW-OH
-
pH 6.0, 37C
0.0016
2,4-dinitrophenyl-GFAFW-OH
-
pH 6.0, 37C
0.0034
2,4-dinitrophenyl-GFDFW-OH
-
pH 6.0, 37C
0.0008
2,4-dinitrophenyl-GFEFW-OH
-
pH 6.0, 37C
0.0005
2,4-dinitrophenyl-GFFFW-OH
-
pH 6.0, 37C
0.0014
2,4-dinitrophenyl-GFGFW-OH
-
pH 6.0, 37C
0.0007
2,4-dinitrophenyl-GFHFW-OH
-
pH 6.0, 37C
0.0021
2,4-dinitrophenyl-GFKFW-OH
-
pH 6.0, 37C
0.0005
2,4-dinitrophenyl-GFLFW-OH
-
pH 6.0, 37C
0.0017
2,4-dinitrophenyl-GFLFW-OH
-
pH 6.0, 37C
0.0006
2,4-dinitrophenyl-GFQFW-OH
-
pH 6.0, 37C
0.0052
2,4-dinitrophenyl-GFRAW-OH
-
pH 6.0, 37C
0.0053
2,4-dinitrophenyl-GFRDW-OH
-
pH 6.0, 37C
0.0096
2,4-dinitrophenyl-GFREW-OH
-
pH 6.0, 37C
0.0012
2,4-dinitrophenyl-GFRFW-OH
-
pH 6.0, 37C
0.0077
2,4-dinitrophenyl-GFRGW-OH
-
pH 6.0, 37C
0.0045
2,4-dinitrophenyl-GFRHW-OH
-
pH 6.0, 37C
0.0033
2,4-dinitrophenyl-GFRIW-OH
-
pH 6.0, 37C
0.0008
2,4-dinitrophenyl-GFRKW-OH
-
pH 6.0, 37C
0.0021
2,4-dinitrophenyl-GFRLW-OH
-
pH 6.0, 37C
0.0045
2,4-dinitrophenyl-GFRQW-OH
-
pH 6.0, 37C
0.005
2,4-dinitrophenyl-GFRRW-OH
-
pH 6.0, 37C
0.0095
2,4-dinitrophenyl-GFRSW-OH
-
pH 6.0, 37C
0.0018
2,4-dinitrophenyl-GFRVW-OH
-
pH 6.0, 37C
0.009
2,4-dinitrophenyl-GFRWA-OH
-
pH 6.0, 37C
0.0055
2,4-dinitrophenyl-GFRWD-OH
-
pH 6.0, 37C
0.0106
2,4-dinitrophenyl-GFRWE-OH
-
pH 6.0, 37C
0.0022
2,4-dinitrophenyl-GFRWF-OH
-
pH 6.0, 37C
0.0162
2,4-dinitrophenyl-GFRWG-OH
-
pH 6.0, 37C
0.012
2,4-dinitrophenyl-GFRWI-OH
-
pH 6.0, 37C
0.0126
2,4-dinitrophenyl-GFRWK-OH
-
pH 6.0, 37C
0.0042
2,4-dinitrophenyl-GFRWL-OH
-
pH 6.0, 37C
0.0124
2,4-dinitrophenyl-GFRWP-OH
-
pH 6.0, 37C
0.0115
2,4-dinitrophenyl-GFRWR-OH
-
pH 6.0, 37C
0.0128
2,4-dinitrophenyl-GFRWS-OH
-
pH 6.0, 37C
0.0223
2,4-dinitrophenyl-GFRWV-OH
-
pH 6.0, 37C
0.0066
2,4-dinitrophenyl-GFRWY-OH
-
pH 6.0, 37C
0.0036
2,4-dinitrophenyl-GFRYW-OH
-
pH 6.0, 37C
0.0012
2,4-dinitrophenyl-GFSFW-OH
-
pH 6.0, 37C
0.0004
2,4-dinitrophenyl-GFVFW-OH
-
pH 6.0, 37C
0.0011
2,4-dinitrophenyl-GFYFW-OH
-
pH 6.0, 37C
0.0086
2,4-dinitrophenyl-GHRFW-OH
-
pH 6.0, 37C
0.0019
2,4-dinitrophenyl-GIRFW-OH
-
pH 6.0, 37C
0.0041
2,4-dinitrophenyl-GKRFW-OH
-
pH 6.0, 37C
0.0106
2,4-dinitrophenyl-GLRFW-OH
-
pH 6.0, 37C
0.0022
2,4-dinitrophenyl-GPRFW-OH
-
pH 6.0, 37C
0.0066
2,4-dinitrophenyl-GRRFW-OH
-
pH 6.0, 37C
0.0038
2,4-dinitrophenyl-GSRFW-OH
-
pH 6.0, 37C
0.0023
2,4-dinitrophenyl-GVRFW-OH
-
pH 6.0, 37C
0.0011
2,4-dinitrophenyl-GYRFW-OH
-
pH 6.0, 37C
0.004
4-(4-dimethylaminophenylazo)benzoyl-IEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0028
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0036
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0035
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0053
4-(4-dimethylaminophenylazo)benzoyl-L-Arg-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0046
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0078
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0037
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0082
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0056
4-(4-dimethylaminophenylazo)benzoyl-LEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.006
4-(4-dimethylaminophenylazo)benzoyl-LRGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0066
4-(4-dimethylaminophenylazo)benzoyl-LRGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0035
4-(4-dimethylaminophenylazo)benzoyl-R-LVGFE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0037
4-(4-dimethylaminophenylazo)benzoyl-RIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0046
4-(4-dimethylaminophenylazo)benzoyl-RIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0055
4-(4-dimethylaminophenylazo)benzoyl-RIIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0034
4-(4-dimethylaminophenylazo)benzoyl-RLEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0049
4-(4-dimethylaminophenylazo)benzoyl-RLEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.001
4-(4-dimethylaminophenylazo)benzoyl-RLVG-beta-(2-naphthyl)alanine-E-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0038
4-(4-dimethylaminophenylazo)benzoyl-RLVG-beta-(2-naphthyl)alanine-E-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0029
4-(4-dimethylaminophenylazo)benzoyl-RLVGF-L-alpha-aminoadipic acid-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0059
4-(4-dimethylaminophenylazo)benzoyl-RLVGF-L-alpha-aminoadipic acid-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.003
4-(4-dimethylaminophenylazo)benzoyl-RLVGFD-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0145
4-(4-dimethylaminophenylazo)benzoyl-RLVGFD-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0022
4-(4-dimethylaminophenylazo)benzoyl-RLVGFE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0047
4-(4-dimethylaminophenylazo)benzoyl-RLVGWE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0078
4-(4-dimethylaminophenylazo)benzoyl-RLVGWE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0021
Abz-FF-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37C
0.003
Abz-FR-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37C
0.0177
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-P-OH
-
pH 6.0, 37C
0.0038
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37C
0.0179
Abz-FRA-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37C
0.0328
Abz-FRF-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37C
0.0059
Abz-GIVRAK(Dnp)-OH
-
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37C
0.247
acetyl-F-R-4-methylcoumarin-7-amide
-
pH 6.0
0.4
acetyl-L-Arg-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.056
acetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
1.02
alpha-N-benzoyl-DL-Arg-beta-naphthylamide
-
free enzyme
1.5 - 2
alpha-N-benzoyl-DL-Arg-beta-naphthylamide
-
encapsulated enzyme
0.05
Arg-4-methylcoumaryl-7-amide
-
-
0.51 - 2.36
benzoyl-DL-Arg-beta-naphthylamide
-
depending on concentration of dimethylsulfoxide, 1-2.5%
0.53
benzoyl-DL-Arg-beta-naphthylamide
-
-
0.8
benzoyl-DL-Arg-beta-naphthylamide
-
isoenzyme II
0.93
benzoyl-DL-Arg-beta-naphthylamide
-
-
1.2
benzoyl-DL-Arg-beta-naphthylamide
-
-
1.25
benzoyl-DL-Arg-beta-naphthylamide
Dorytheuthis bleekeri
-
-
1.82
benzoyl-DL-Arg-beta-naphthylamide
-
-
2
benzoyl-DL-Arg-beta-naphthylamide
-
-
2.5
benzoyl-DL-Arg-beta-naphthylamide
-
-
2.9
benzoyl-DL-Arg-beta-naphthylamide
-
isoenzyme I
3.3
benzoyl-DL-Arg-beta-naphthylamide
-
-
6.7
benzoyl-DL-Arg-beta-naphthylamide
-
tumor enzyme
24
benzoyl-DL-Arg-beta-naphthylamide
-
liver enzyme
0.685
benzoyl-DL-Arg-p-nitroanilide
-
-
1
benzoyl-DL-Arg-p-nitroanilide
-
-
1.6
benzoyl-DL-Arg-p-nitroanilide
-
-
2.08
benzoyl-DL-Arg-p-nitroanilide
-
-
20
benzoyl-DL-Arg-p-nitroanilide
-
-
0.039
benzoyl-L-3-pyridyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.015
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.032
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.019
benzoyl-L-4-aminomethyl-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.023
benzoyl-L-4-guanidine-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.052
benzoyl-L-4-piperidinyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.032
benzoyl-L-Arg-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.034
benzoyl-L-His-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.03
benzoyl-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37C
0.0232
benzoyl-Phe-Val-Arg-p-nitroanilide
-
liver enzyme
0.07
benzoyl-Phe-Val-Arg-p-nitroanilide
-
isoenzyme I
0.13
benzoyl-Phe-Val-Arg-p-nitroanilide
-
isoenzyme II
0.18
benzoyl-Phe-Val-Arg-p-nitroanilide
-
tumor enzyme
0.2
benzoyl-Pro-Phe-Arg-p-nitroanilide
-
liver enzyme
0.43
benzoyl-Pro-Phe-Arg-p-nitroanilide
-
isoenzyme I
0.59
benzoyl-Pro-Phe-Arg-p-nitroanilide
-
tumor enzyme
1
benzoyl-Pro-Phe-Arg-p-nitroanilide
-
isoenzyme II
0.022
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
-
-
0.066
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
-
isoenzyme II
0.07
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
-
liver enzyme and tumor enzyme
0.13
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
-
isoenzyme I
1.25
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
-
-
0.02
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide
-
-
0.055
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide
-
-
0.09 - 0.29
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide
-
depending on concentration of dimethylsulfoxide, 1-2.5%
0.006
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.032
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.038
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.041
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.046
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.093
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.114 - 0.125
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.17
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.184
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.262
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.34
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.467
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.131
benzyloxycarbonyl-F-R-4-methylcoumarin-7-amide
-
pH 6.0
0.021
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.038
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.058
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.071
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.09
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.129
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.2
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.204 - 0.225
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.252
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
-
0.012
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
-
-
0.0561
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
tumor enzyme
-
0.091
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
liver enzyme
-
0.14
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
-
-
0.2
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
isoenzyme I
-
0.91
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
-
isoenzyme II
-
1.16
Boc-Asp-Pro-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22C
0.35
Boc-Asp-Pro-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
0.3
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumaryl-7-amide
-
22C, value is quite stable in the range of pH 4.0 to pH 7.8
1.67
Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin
-
pH 6.0, 22C
0.53
Boc-Val-Pro-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
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 25C
-
0.13
D-Pro-Phe-Arg-p-nitroanilide
-
-
4.53
D-Val-Leu-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
0.089
epsilon-aminocaproic acid-L-Leu-Gly-4-methylcoumarin-7-amide
-
pH 6.0
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
0.034
epsilon-aminocaproic acid-L-Leu-L-Phe-4-methylcoumarin-7-amide
-
pH 6.0
0.055
epsilon-aminocaproic acid-L-R-4-methylcoumarin-7-amide
-
pH 6.0
0.00143 - 0.00217
hemoglobin
-
-
-
0.00145
hemoglobin
-
-
-
0.1
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22C
1.22
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
0.047
N-benzyloxycarbonyl-Phe-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22C
0.19
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
0.007
N-benzyloxycarbonyl-Val-Ile-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22C
0.072
N-t-butyloxycarbonyl-Gln-p-nitrophenyl ester
-
isoenzyme I and isoenzyme II
0.212
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
-
pH 6.0, 37C, recombinant enzyme
0.226
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
-
pH 6.0, 37C, recombinant enzyme
0.043
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
-
pH 6.0, 37C, recombinant enzyme
0.075
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
-
pH 6.0, 37C, recombinant enzyme
0.00611
Nalpha-carbobenzoxy-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin
recombinant enzyme, at pH 7.3 and 37C
-
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