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2,4-dinitrophenyl-GARFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GDRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GERFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFAFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFDFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFEFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFFFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFGFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFHFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFIFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFKFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFLFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFPFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFQFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRAW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRDW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFREW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRGW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRHW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRIW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRKW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRLW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRPW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRQW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRRW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRSW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRVW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRW R-OH + H2O
?
-
-
-
-
?
2,4-dinitrophenyl-GFRWA-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWD-OH + H2O
?
-
-
-
-
?
2,4-dinitrophenyl-GFRWE-OH + H2O
?
-
-
-
-
?
2,4-dinitrophenyl-GFRWF-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWG-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWI-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWK-OH + H2O
?
-
-
-
-
?
2,4-dinitrophenyl-GFRWL-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWP-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWQ-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWS-OH + H2O
?
-
-
-
-
?
2,4-dinitrophenyl-GFRWV-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRWY-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFRYW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFSFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFVFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GFYFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GGRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GHRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GIRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GKRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GLRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GPRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GQRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GRRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GSRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GVRFW-OH + H2O
?
-
-
-
?
2,4-dinitrophenyl-GYRFW-OH + H2O
?
-
-
-
?
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-(Nepsilon-2,4-dinitrophenyl)Lys + H2O
2-aminobenzoyl-Gly-Ile-Val-Arg + Ala-(Nepsilon-2,4-dinitrophenyl)Lys
-
an exoproteolytic substrate
-
-
?
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH + H2O
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
5-amino-1-(phenylsulfonyl)-1H-pyrazol-3-yl thiophene-2-carboxylate + H2O
5-amino-1-(phenylsulfonyl)-1,2-dihydro-3H-pyrazol-3-one + thiophene-2-carbaldehyde
-
-
-
-
?
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl pyridine-4-carboxylate + H2O
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1,2-dihydro-3H-pyrazol-3-one + pyridine-4-carbaldehyde
-
-
-
-
?
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Arg-Phe(NO2)-Leu + H2O
?
pH 6.4, 37°C, 2 mM cysteine, 1 mM EDTA
-
-
?
6-maleimidocaproic acid-L-Arg-Arg-Ala-Leu-Ala-Leu-Ala-camptothecin + H2O
?
-
-
major cleavage products are L-Leu-Ala-Leu-Ala-camptothecin, L-Ala-Leu-Ala-camptothecin, L-Leu-Ala-camptothecin, and camptothecin
-
?
6-maleimidocaproic acid-L-Arg-Arg-Ala-Leu-Ala-Leu-doxorubicin + H2O
?
-
-
major cleavage products are L-Leu-Ala-Leu-doxorubicin, L-Leu-doxorubicin, and doxorubicin
-
?
Abeta peptide + H2O
?
the enzyme cleaves the Abeta peptide from the carboxylic end of Glu11
-
-
?
Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp + H2O
Abz-Ala-Phe-Arg + Ser-Ala-X-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-Ala-X-Gln-EDDnp, with X is Asn > Tyr, His, Leu, Trp > Ser, Phe, Pro Lys > Asp, Ala
-
-
?
Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-Ala-Phe-Arg + Ser-X-Arg-Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-Phe-Arg-Ser-X-Arg-Ser-Ala-Gln-EDDnp, with X is Asn > Trp, Tyr, Ala > Ser, Phe > His, Lys > Asp, Leu, Pro
-
-
?
Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-Ala-X-Ala-Phe-Arg + Ser-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp, with X is Leu, Tyr > Phe, Ala, Ser, Pro > His, Lys > Asn, Asp
-
-
?
Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp + H2O
Abz-Ala-X-Arg + Ser-Ala-Ala-Gln-EDDnp
kcat/Km for Abz-Ala-X-Arg-Ser-Ala-Ala-Gln-EDDnp, with X is Phe, Leu > Arg > Ala > Pro
-
-
?
Abz-FF-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH + H2O
?
-
-
-
-
?
Abz-FR-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH + H2O
?
-
-
-
-
?
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-P-OH + H2O
?
-
-
-
-
?
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-W-OH + H2O
?
-
-
-
-
?
Abz-FRA-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH + H2O
?
-
-
-
-
?
Abz-FRF(NO2)A + H2O
?
-
-
-
?
Abz-FRF-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH + H2O
?
-
-
-
-
?
Abz-GIVRAK(Dnp)-OH + H2O
?
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
-
-
?
Abz-GIVRAK-Dnp + H2O
?
-
-
-
?
Abz-GXXRZK(Dnp)-OH + H2O
?
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
-
-
?
Abz-GXXZXK(Dnp)-OH + H2O
?
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
-
-
?
Abz-GXZRXK(Dnp)-OH + H2O
?
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
-
-
?
Abz-GZXRXK(Dnp)-OH + H2O
?
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
-
-
?
Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp + H2O
Abz-X-Ala-Phe-Arg + Ser-Ala-Gln-EDDnp
kcat/Km for Abz-X-Ala-Phe-Arg-Ser-Ala-Gln-EDDnp, with X is Leu, Phe, Trp > Ser, Asn, Asp, Ala > Tyr, His, Lys
-
-
?
Ac-Arg-Arg-4-methyl-7-amidocoumarin + H2O
Ac-Arg-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Ac-Arg-Arg-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
?
Ac-Arg-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Arg-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Ac-His-Pro-Val-Lys-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
Ac-His-Pro-Val-Lys + 7-amino-3-carbamoyl-4-methylcoumarin
-
assay at pH 5.5, 37°C
-
-
?
acetyl-Arg-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
?
-
a synthetic substrate of caspase-3 and caspase-7
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
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
-
-
-
?
acetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
acetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
alpha-N-benzoyl-DL-Arg-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-Arg + beta-naphthylamine
-
-
-
-
?
amino acid-beta-naphthylamides + H2O
amino acid + beta-naphthylamine
-
-
-
?
amyloid beta peptide + H2O
?
amyloid beta precursor protein + H2O
?
-
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
?
-
cathepsin B degraded C-terminal fragments regardless of phosphorylation
-
-
?
amyloid precursor protein intracellular domain + H2O
?
-
-
-
-
?
amyloid-beta + H2O
?
-
-
-
-
?
antiprotease secretory leucoprotease inhibitor + H2O
cleaved SLP1 protein
-
i.e. SLP1 protein, cleavage between residues Thr67 and Tyr68
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
azocasein + H2O
fragments of azocasein
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
benzoyl-L-3-pyridyl-Ala-l-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-3-pyridyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminocyclohexy-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-aminomethyl-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-aminomethyl-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-guanidine-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-guanidine-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-4-piperidinyl-Ala-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-4-piperidinyl-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Arg-beta-naphthylamide + H2O
benzoyl-L-Arg + beta-naphthylamine
-
-
-
?
benzoyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
benzoyl-L-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-His-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-N-dimethyl-His-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-N-dimethyl-His-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
benzyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
benzyloxycarbonyl-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
benzyloxycarbonyl-Arg-Arg-4-methyl-7-coumarylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
benzyloxycarbonyl-Arg-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-FR-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
benzyloxycarbonyl-L-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-phenylalaninyl-L-arginine 4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
benzyloxycarbonyl-Phe-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Phe-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-AMC + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-phenylalanyl-arginine-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
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
37°C, 1 mM DTT, 1 mM EDTA, pH 6.0
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
beta-lipotropin + H2O
hydrolyzed beta-lipotropin
-
-
-
?
Boc-Asp-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Boc-Asp-Pro-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Boc-Asp-Pro-Arg-4-methylcoumarin 7-amide + H2O
Boc-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumarin-7-amide + H2O
Boc-L-Leu-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
pH-dependence of reaction
-
?
Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Boc-Phe-Ser-Arg + 7-amino-4-methylcoumarin
29% of the activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin + H2O
Boc-Val-Leu-Lys + 4-methyl-7-aminocoumarin
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
Boc-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Val-Pro-Arg + 7-amino-4-methylcoumarin
8% of the activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
BODIPY FL casein + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin hydrochloride + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin hydrochloride
-
-
-
-
?
carbobenzoxy-Gly-Gly-Arg-naphthylamide + H2O
? + naphthylamine
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
casein + H2O
hydrolyzed casein
caspase 1 precursor + H2O
?
-
-
-
-
?
CBZ-Arg-Arg-4-nitroanilide + H2O
CBZ-Arg-Arg + 4-nitroaniline
-
-
-
?
CBZ-Arg-Arg-7-amido-4-methylcoumarin + H2O
CBZ-Arg-Arg + 7-amino-4-methylcoumarin
-
endopeptidase activity
-
-
?
Cbz-FR-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
37°C, pH 6.0, 200 mM NaCl, 1 mM EDTA, 5 nM DTT
-
-
?
CBZ-L-Arg-L-Arg-4-nitroanilide + H2O
L-Arg-L-Arg + 4-nitroaniline
-
-
-
?
Cbz-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Cbz-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CBZ-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
chemokine (C-C motif) ligand 20 + H2O
CCL20 1-66 isoform + ?
-
CCL20 is also known as liver- and activation-regulated chemokine (LARC), MIP-3alpha, or exodus-1
cathepsin B specifically cleaves off four C-terminally located amino acids and generates a CCL20 1-66 isoform with full functional activity
-
?
Collagen + H2O
Hydrolyzed collagen
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
-
-
-
?
D-Val-Leu-Arg-4-methylcoumarin 7-amide + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
Dnp-Gly-Phe-Arg-Trp-X-OH + H2O
Dnp-Gly-Phe + Arg-Trp-X-OH
kcat/Km for Dnp-Gly-Phe-Arg-Trp-X-OH, with X is Phe > Tyr, Ile > Leu > Cval > Arg > Lys, Pro > Gln, Ser > Asp, Glu, Ala
-
-
?
Dnp-Gly-Phe-Arg-X-Trp-OH + H2O
Dnp-Gly-Phe + Arg-X-Trp-OH
kcat/Km for Dnp-Gly-Phe-Arg-X-Trp-OH, with X is Phe > Ser > Leu > Ala > Ile > Tyr, Val > Gln > Lys > Gly > His, Asp > Arg > Glu
-
-
?
Dnp-Gly-Phe-X-Phe-Trp-OH + H2O
Dnp-Gly-Phe-X + Phe-Trp-OH
kcat/Km for Dnp-Gly-Phe-X-Phe-Trp-OH, with X is Arg > Lys > Phe > Leu > Val > His, Gln > Ser > Gly Ala > Glu > Tyr > Ile, Asp
-
-
?
Dnp-Gly-X-Arg-Phe-Trp-OH + H2O
Dnp-Gly-X-Arg + Phe-Trp-OH
kcat/Km for Dnp-Gly-X-Arg-Phe-Trp-OH, with X is Phe > Tyr > Lys > Val > Ala > Ile > Ser, Pro > His > Leu > Arg > Asp, Glu
-
-
?
DQ-collagen IV + H2O
?
-
-
-
-
?
epithelial sodium channel alpha subunit + H2O
?
-
in vitro cleavage studies show that the full-length ENaC alpha subunit fusion protein is cleaved by active cathepsin B but not the full-length beta or gamma subunit fusion proteins
-
-
?
epsilon-aminocaproic acid-L-Leu-Gly-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-Gly + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)serine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)serine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)threonine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-benzyl)threonine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(O-methyl)-tyrosine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(O-methyl)-tyrosine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-(S-benzyl)cysteine-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-(S-benzyl)cysteine + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-Leu-L-Phe-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-Leu-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
epsilon-aminocaproic acid-L-R-4-methylcoumarin-7-amide + H2O
epsilon-aminocaproic acid-L-R + 7-amino-4-methylcoumarin
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
filaggrin + H2O
hydrolyzed filaggrin
-
-
-
?
gelatin + H2O
hydrolyzed gelatine
-
-
-
?
globin + H2O
partially degraded globin
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
-
-
?
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
from goat and from buffalo
-
?
herpes simplex virus type 1 origin binding protein + H2O
herpes simplex virus type 1 origin binding protein 1
53 kDa protein
50 kDa protein
-
?
histones + H2O
hydrolyzed histones
-
-
-
?
human anti-HIV-1 antibody + H2O
?
NbCathB is far more efficient than aleurain-like protease in processing the human anti-HIV-1 antibody 2F5 into fragments
-
-
?
human fibronectin + H2O
?
-
-
-
?
human hemoglobin + H2O
?
-
-
-
?
human IgG + H2O
?
-
-
-
?
human serum albumin + H2O
?
-
-
-
?
L-Arg-L-Arg-4-nitroanilide + H2O
L-Arg-L-Arg + 4-nitroaniline
-
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
mouse T7 trypsinogen mutant D22A/K24G + H2O
?
engineering of a mouse T7 trypsinogen mutant (D22A,K24G), which is robustly activated by cathepsin B but cannot undergo autoactivation
-
-
?
myelin basic protein + H2O
?
-
-
-
?
myoglobin + H2O
hydrolyzed myoglobin
-
-
-
?
myosin + H2O
hydrolyzed myosin
-
-
-
?
myristoylated alanine-rich C kinase substrate + H2O
?
-
i.e. MARCKS
-
-
?
myristoylated alanine-rich C kinase substrate + H2O
p40 + ?
-
i.e. MARCKS
-
?
N,N'-diBoc-dityrosine-Gly-(isoniazid)2 + H2O
?
-
-
-
?
N,N'-diBoc-dityrosine-Lys-(isoniazid)2 + H2O
?
-
-
-
?
N,N-dimethyl hemoglobin + H2O
hydrolyzed N,N-dimethyl hemoglobin
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
-
-
-
-
?
N-benzoyl-Arg-Arg-4-nitroanilide + H2O
N-benzoyl-Arg-Arg + 4-nitroaniline
-
-
-
?
N-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-L-Arg-2-naphthylamide + H2O
N-benzoyl-L-Arg + 2-naphthylamine
-
-
-
?
N-benzoyl-Val-Asn-Leu-7-amido-4-methylcoumarin + H2O
N-benzoyl-Val-Lys-Met + 7-amino-4-methylcoumarin
-
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
-
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
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-arginyl-L-arginyl-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
substrate of mature cathepsin B, also procathepsin B is catalytically active on the synthetic substrate but to a lower extent. The unfolded proenzymeis inactive
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg 7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
?
N-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-L-lysine + 4-nitrophenol
-
-
-
-
?
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg-beta-naphthylamide + H2O
N-benzyloxycarbonyl-L-Val-Lys-Lys-Arg + beta-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Val-Ile-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Val-Ile-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Val-Ile-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Val-Ile-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzoxy-L-lysine 4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
-
-
-
-
?
N-carbobenzoxy-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-CBZ-L-Arg-L-Arg-7-amido- 4-methylcoumarin + H2O
N-CBZ-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-t-butyloxycarbonyl-Gln-p-nitrophenyl ester + H2O
N-t-butyloxycarbonyl-Gln + 4-nitrophenol
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
Nalpha-benzoyl-Val-Lys-Lys-Arg-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
Nalpha-CBZ-Arg-Arg 7-amido-4-methylcoumarin + H2O
Nalpha-CBZ-Arg-Arg + 7-amino-4-methylcoumarin
1 mM DTT
-
-
?
neuropeptides + H2O
hydrolyzed neuropeptides
-
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
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine + H2O
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln + 2,4-dinitrophenyl-ethylenediamine
-
-
-
?
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide + H2O
?
-
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
phenylacetyl-L-Arg-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
phenylacetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
phenylacetyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pro-rhoptry protein 2 + H2O
rhoptry protein 2 + propeptide
-
-
-
?
Protamine + H2O
Hydrolyzed protamine
-
-
-
?
protein rGSII-D88N + H2O
?
proteoglycans + H2O
hydrolyzed proteoglycans
-
-
-
?
serum albumin + H2O
partially degraded serum albumin
-
-
-
?
sheep immunoglobulin heavy chain + H2O
hydrolyzed sheep immunoglobulin heavy chain
-
-
-
?
sphingosine kinase-1 + H2O
?
-
cleaves at histidine 122 and arginine 199
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Suc-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
6% of the activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
Tos-Gly-Pro-Arg-4-methyl-7-amidocoumarin + H2O
Tos-Gly-Pro-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
Tos-Gly-Pro-Arg-4-methylcoumarin 7-amide + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
-
?
trypsinogen + H2O
trypsin + peptide
-
-
-
-
?
trypsinogen activation peptide + H2O
?
1 mM DTT, 1 mM EDTA, pH 4.1, room temperature
-
-
?
Type I collagen + H2O
?
-
-
-
?
yolk protein + H2O
?
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
Z-Arg-Arg-cresyl violet + H2O
Z-Arg-Arg + cresyl violet
-
-
-
?
Z-Arg-Arg-p-nitroanilide + H2O
?
-
1 microM, pH 6.0, 10 nanoM cathepsin B
-
-
?
Z-Arg-Leu-7-amido-4-methylcoumarin + H2O
Z-Arg-Leu + 7-amino-4-methylcoumarin
Z-Arg-Phe-7-amido-4-methylcoumarin + H2O
Z-Arg-Phe + 7-amino-4-methylcoumarin
Z-Arg-Val-7-amido-4-methylcoumarin + H2O
Z-Arg-Val + 7-amino-4-methylcoumarin
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
37°C, 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
-
-
-
?
Z-L-Phe-L-Arg 7-amido-4-methylcoumarin + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
Z-L-Phe-L-Arg-4-methylcoumarin-7-amide + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
additional information
?
-
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH + H2O
?
-
exopeptidase activity
-
-
?
2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH + H2O
?
exopeptidase activity
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
-
-
-
?
Aldolase + H2O
Hydrolyzed aldolase
-
-
-
?
amyloid beta peptide + H2O
?
-
-
-
-
?
amyloid beta peptide + H2O
?
-
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
-
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
-
-
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
-
-
-
?
azocasein + H2O
fragments of azocasein
-
poor substrate
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
-
-
-
?
benzoyl-arginine ethyl ester + H2O
benzoyl-arginine + ethanol
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
Dorytheuthis bleekeri
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-beta-naphthylamide + H2O
benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-Arg-p-nitroanilide + H2O
benzoyl-DL-Arg + p-nitroaniline
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
Dorytheuthis bleekeri
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
-
-
-
?
benzoyl-DL-argininamide + H2O
benzoyl-DL-arginine + NH3
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
-
-
-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
-
-
-
?
benzoyl-Phe-Val-Arg-p-nitroanilide + H2O
benzoyl-Phe-Val-Arg + p-nitroaniline
-
-
-
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
-
-
-
?
benzoyl-Pro-Phe-Arg-p-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + 4-methoxy-beta-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
endopeptidase activity
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
17% of the activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-Arg-beta-naphthylamide + H2O
benzyloxycarbonyl-Arg-Arg + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Lys-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
low activity with cathepsin B3 and B2, higher activity with cathepsin B1 and B4
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide + H2O
? + 4-methoxy-beta-naphthylamine
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate of Na-CP-3
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
an endoproteolytic substrate
-
-
?
carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Phe-Ala-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Ala-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
a fluorogenic substrate
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate of Na-CP-3
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
?
Collagen + H2O
Hydrolyzed collagen
-
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
quenched fluorescent protein
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
collagen IV of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
-
-
-
?
denatured hemoglobin + H2O
hydrolyzed denatured hemoglobin
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
quenched fluorescent protein
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
a substrate of Na-CP-3
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
?
IgG + H2O
?
-
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
laminin of the basement membrane damaged by cathepsin B, that is released after mechanical injury, during initial post-traumatic stages, overview
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 4-methyl-7-aminocoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
-
albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B and in tumor homogenates of MDA-MB 435 tumor cells from in vitro culture transplanted subcutaneously into the left flank region of mice, overview
-
-
?
Phe-Lys-4-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin + H2O
?
-
albumin-binding prodrug of doxorubicin, which incorporates a maleimide moiety and a 4-aminobenzyloxycarbonyl spacer coupled to the dipeptide Phe-Lys, is cleaved by cathepsin B
-
-
?
protein rGSII-D88N + H2O
?
-
-
-
?
protein rGSII-D88N + H2O
?
-
degradation
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
enzyme activation and conversion of precursor proteins to their active form
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
Dorytheuthis bleekeri
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
34990, 34991, 36622, 36626, 36632, 36634, 36641, 36647, 36650, 36662, 36665 -
-
?
Proteins + H2O
?
-
plays a role in cancer invasion and metastasis
-
-
?
Proteins + H2O
?
-
muscle proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
-
-
-
?
Proteins + H2O
?
-
degradation of tissue proteins within lysosomes
-
-
?
Proteins + H2O
?
-
turnover of intracellular proteins
-
-
?
Proteins + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha
-
-
?
TNF-alpha + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides
-
-
?
TNF-alpha + H2O
?
-
-
-
-
?
TNF-alpha + H2O
?
-
cathepsin B is required for optimal posttranslational processing of TNF-alpha in response to the bacterial cell wall component lipopolysacchrides
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
1 mM DTT, 2 mM EDTA, pH 6.8, 37°C, activity varied from 0.013 to 3.4 U/mg protein in normal tissue and from 0.007 to 20.0 U/mg protein in cancer tissue
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
pH 5, 1 mM EDTA, 4 mM DTT
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
20 mM DTT, pH 5.5
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
37°C, 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
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
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
2 mM DTT, pH 3.0-8.0, 0.3 M NaCl, room temperature, negligible hydrolysis
-
-
?
Z-Arg-Leu-7-amido-4-methylcoumarin + H2O
Z-Arg-Leu + 7-amino-4-methylcoumarin
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
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
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
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-L-Phe-L-Arg 7-amido-4-methylcoumarin + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-L-Phe-L-Arg 7-amido-4-methylcoumarin + H2O
Z-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
differential regulation of snail cathepsin B transcript pre- and postparasite exposure, overview
-
-
?
additional information
?
-
-
differential regulation of snail cathepsin B transcript pre- and postparasite exposure, overview
-
-
?
additional information
?
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
?
additional information
?
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
?
additional information
?
-
-
CmCatB2 may be an inactive protease isoform resulting from splicing errors
-
-
?
additional information
?
-
the enzyme shows substantial exopeptidase activity at a relative rate of 34.26% compared to human cathepsin B
-
-
?
additional information
?
-
-
the enzyme shows substantial exopeptidase activity at a relative rate of 34.26% compared to human cathepsin B
-
-
?
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
?
-
enzyme prefers dipeptidyl pathway over monopeptidyl carboxypeptidase pathway
-
?
additional information
?
-
enzyme prefers large aromatic residues at S2' subsite and the exopeptidase activity prefers aromatic side chains in P2' position
-
?
additional information
?
-
-
enzyme prefers large aromatic residues at S2' subsite and the exopeptidase activity prefers aromatic side chains in P2' position
-
?
additional information
?
-
-
preference for substrate cleavage through dipeptidyl pathway, influence of substrate P2-P1 residues
-
?
additional information
?
-
cathepsin B can partially process the 48000 Da intermediate into 34000 Da mature cathepsin D
-
-
?
additional information
?
-
-
cathepsin B can partially process the 48000 Da intermediate into 34000 Da mature cathepsin D
-
-
?
additional information
?
-
no reaction with Abz-GIVRPK(Dnp)-OH
-
-
?
additional information
?
-
-
no reaction with Abz-GIVRPK(Dnp)-OH
-
-
?
additional information
?
-
no reaction with procarboxypeptidase and proelastase
-
-
?
additional information
?
-
-
no reaction with procarboxypeptidase and proelastase
-
-
?
additional information
?
-
-
cathepsin B is able to self-activate
-
-
?
additional information
?
-
-
autocatalytic activation of the inactive proenzyme
-
-
?
additional information
?
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
-
cathepsin B is a target of Hedgehog signaling in pancreatic cancer, downregulation of CATB by Hedgehog, cyclopamine reduces CATB protein and mRNA levels. CATB might influence pancreatic cancer cell invasiveness
-
-
?
additional information
?
-
-
cathepsin B is an intracellular lysosomal cysteine proteinase that can degrade extracellular components including collagen and protein turnover in the lysosomal system. Cathepsin B plays an important role in the resolution of organic matrix, a final step in bone resorption. It is also known to play an important role in the initiation and perpetuation of inflammatory processes
-
-
?
additional information
?
-
-
cathepsin B is expressed in cerebral aneurysms and promotes the progression of cerebral aneurysms, which include degradation of extracellular matrix in arterial walls in strong subarachnoid hemorrhage, overview
-
-
?
additional information
?
-
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
?
additional information
?
-
-
cathepsin B, together with cathepsin L, urokinase-type plasminogen activator and its inhibitor PAI-1, plays an important role in colorectal cancer invasion. Correlation analysis of proteolytic enzymes in colorectal cancer, overview
-
-
?
additional information
?
-
-
cathepsin-B is a lysosomal cysteine proteasewith broad substrate specificity, which belongs to a family of 11 cysteine proteases. The enzyme is involved in tumor progression, e.g. of endometrial carcinomas
-
-
?
additional information
?
-
-
cysteine cathepsins play a critical role in the biologic activity of tumor-shed vesicles at acidic pH, but not at physiological pH, endothelial cell invasiveness is increased by tumor-shed vesicles exposed to acidic pH, overview
-
-
?
additional information
?
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
-
disturbances in the regulation of the intracellular activities and uncontrolled release of cathepsins from lysosomes have been implicated in many disease states, such as osteoporosis, inflammatory diseases, and tumor progression
-
-
?
additional information
?
-
-
increased cathepsin B levels in acute and chronic lung diseases resulting from high levels of extracellular neutrophil elastase, expression of the protease can be inhibited by alpha1-antitrypsin augmentation therapy
-
-
?
additional information
?
-
-
NF-kappaB induced up-regulation of cathepsin B expression contributes to the invasive property of the 143B cells lacking mtDNA, overview. Extracellularly released cathepsin B can act alone or in concert with some matrix metalloproteinases
-
-
?
additional information
?
-
-
participation of cathepsin B in emodin-induced apoptosis in HK-2 cells, enzyme inhibition by Ca-074 causes significant attenuation the ratio of hypodiploid and apoptotic cells, partially blockage of caspase 3 activation and inhibition of reduction of cell viability induced by emodin, overview
-
-
?
additional information
?
-
-
Porphyromonas gingivalis strain 381 or its lipopolysaccharides increases the expression of cathepsin B in oral epithelial cells
-
-
?
additional information
?
-
-
regulation of cathepsin B in gingival fibroblasts involves interleukin-6 and its receptor along with the Cav-1-JNK-AP-1 pathway, overview
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of extracellular matrix and of basement membrane components leading to tumor invasion in the intestine. Expression of matrix metalloproteinase-9 and cathepsin B is correlated with lymph node metastasis in advanced gastric carcinoma, but not with patients' postoperative survival, overview. Correlation between the synthesis of cysteine and serine proteases and the potential tumor invasion
-
-
?
additional information
?
-
-
the enzyme is involved in extracellular matrix degradation in caveolae of endothelial cells during tube formation, overview. Cathepsin B regulates both pro- and anti-angiogenic factors and may be a contributor to the angiogenic switch of endothelial cells
-
-
?
additional information
?
-
-
the enzyme is involved in inflammatory processes
-
-
?
additional information
?
-
-
the enzyme plays an important role in cancer invasion and metastasis, the enzyme content is positively correlated with tumors in different tissue types
-
-
?
additional information
?
-
-
autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins
-
-
?
additional information
?
-
-
cathepsin B is a cysteine protease with both endopeptidase and exopeptidase activity
-
-
?
additional information
?
-
-
No activity with Boc-Val-Pro-Arg-4-methyl-7-amidocoumarin, Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin, and D-Val-Leu-Arg-4-methyl-7-amidocoumarin. Wild-type cathepsin B exhibits exopeptidase activity
-
-
?
additional information
?
-
-
procathepsin B shows autocatalytic processing triggered by proenzyme activity, identification of cleavage sites and initiation mechanism, overview. A multi-step process, starting with a unimolecular conformational change of the zymogen, which unmasks the active site and, in the presence of negatively charged molecules and/or surfaces, also converts the zymogen into a better substrate, followed by the bimolecular proteolytic removal of the propeptide
-
-
?
additional information
?
-
-
the assay uses a modified aminomethylcoumarin dipeptide substrate, which generates a fluorescent signal upon cleavage by cathepsin B
-
-
?
additional information
?
-
active site mapping with peptidic substrates and inhibitors
-
-
?
additional information
?
-
-
active site mapping with peptidic substrates and inhibitors
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
co-incubation of recombinant LycCatB with recombinant Lyc-TR-Ii (invariant chain) leads to an efficient cleavage of recombinant Lyc-TR-Ii
-
-
?
additional information
?
-
-
co-incubation of recombinant LycCatB with recombinant Lyc-TR-Ii (invariant chain) leads to an efficient cleavage of recombinant Lyc-TR-Ii
-
-
?
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
?
-
-
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 involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
cathepsin B is involved in the trafficking of TNF-alpha-containing vesicles to the plasma membrane in macrophages
-
-
?
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
?
-
cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family with multiple biological functions
-
-
?
additional information
?
-
-
cathepsin B is a lysosomal cysteine protease of the papain-like enzyme family with multiple biological functions
-
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enzyme is involved in myoblast-myoblast fusion
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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
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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
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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
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under certain conditions, e.g. in hypoxia, cathepsin B participates in cleavage of caspase-3 substrates in brain cells
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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
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no activity with Arg-7-amido-4-methylcoumarin
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no activity with Arg-7-amido-4-methylcoumarin
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no degradation of hemoglobin
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no degradation of hemoglobin
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no degradation of hemoglobin
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no degradation of hemoglobin
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no degradation of hemoglobin
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no degradation of hemoglobin
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no degradation of hemoglobin
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this isoform encodes an inactive enzyme
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this isoform encodes an inactive enzyme
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additional information
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this isoform encodes an inactive enzyme
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additional information
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this isoform encodes an inactive enzyme
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additional information
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this isoform encodes an inactive enzyme
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additional information
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this isoform encodes an inactive enzyme
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additional information
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this isoform encodes an inactive enzyme
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cathepsin B plays a key role in parasite infection, overview
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cathepsin B plays a key role in parasite infection, overview
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(1E,4E)-1-chloro-4-ethenyl-2-(trichloro-lambda4-tellanyl)hepta-1,4,6-trien-3-ol
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(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
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-
(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
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a Phe-Lys-para-aminobenzyloxycarbonyl-doxorubicin prodrug-albumin
(2(1H)-pyridinethionato-kappaS2)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
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(2E)-3-chloro-1-phenyl-2-(trichloro-lambda4-tellanyl)prop-2-en-1-ol
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-
(2R,3R)-3-(((1S)-1-[(4-carbamimidamidobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylic acid
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(2R,3R)-3-(((1S)-3-methyl-1-[(3-methylbutoxy)carbonyl]butyl)carbamoyl)aziridine-2-carboxylic acid
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(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
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(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
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(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
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(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
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-
(2Z)-1,3-bis(4-methoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
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(2Z)-1,3-diphenyl-4-(trichloro-llambda4-tellanyl)but-2-en-1-one
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(3E)-2-bromo-3-(bromomethylidene)-2-(4-methoxyphenyl)-1-oxa-2l4-telluraspiro[3.5]nonane
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-
(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
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-
(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
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(3E)-4-chloro-3-[dichloro(4-methoxyphenyl)-l4-tellanyl]-2-methylbut-3-en-2-ol
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(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-7-[(2,6-dimethylbenzoyl)oxy]-6-oxoheptan-1-aminium trifluoroacetate
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(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalany]amino)-6-oxo-7-[(2,4,6-trimethylbenzoyl)oxy]heptan-1-aminium trifluoroacetate
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(acetatato-kO)[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](pyridine)palladium(1+)
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(acetatato-kO)[2-(1-methyl-2-oxo-2,3-dihydro-1H-1,4-benzodiazepin-5-yl-kN4)phenyl-kC1](triphenylphosphane)palladium(1+)
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(acetato)(isopropylamine)(2-((2dimethylamino)-methyl)phenyl)Pd(II)
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(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
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(chloro)(isopropylamine)(2-((2dimethylamino)methyl)phenyl)Pd(II)
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(chloro)(pryidinyl)(2-((2dimethylamino)methyl)phenyl)Pd(II)
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(chloro)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN1] oxorhenium(V)
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(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
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(p-methoxyphenylthiolato-S)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
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(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
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(S)-18-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodo-1H-1,2,3-triazol-1-yl)-12,19-dioxo-3,6,9-trioxa-13-azaicosan-20-yl 2,4,6-trimethylbenzoate
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(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(3-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
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(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
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(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 630
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[3-(3-iodophenyl)ureido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 0.013
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[3-(4-iodophenyl)ureido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 0.0035
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(3-iodobenzamido)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 280
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodo-1H-1,2,3-triazol-1-yl)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
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(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodobenzamido)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C, ki/Ki (sec-1M-1): 310
(S)-3-[(S)-2-[(benzyloxycarbonyl)amino]-3-phenylpropanamido]-7-(6-[3-(3-iodophenyl)ureido]hexanamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
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(S)-3-[(S)-2-[(benzyloxycarbonyl)amino]-3-phenylpropanamido]-7-(6-[3-(4-iodophenyl)ureido]hexanamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
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(triethylphosphine)gold(I) chloride
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([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
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([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
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best performing inhibitor is effective in cell-based in vitro models of tumor invasion, where it significantly abrogates invasion of MCF-10A neoT cells
1,1'-[[3-(5-nitroquinolin-8-yl)furan-2,5-diyl]dibenzene-4,1-diyl]diethanone
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1,1,3-trichloro-2,4,5,6-tetrahydro-1H-1-benzotellurophene
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1,3,5-triphenyl pyrazole
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1,3,5-triphenyl-2-pyrazoline
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1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
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1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
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1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
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1-(4-nitronaphthalen-1-yl)pyrrolidine
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1-(dichloro[(1E)-1-chloro-3-methoxyprop-1-en-2-yl]-l4-tellanyl)-4-methoxybenzene
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1-(dichloro[(1Z,3E,5Z)-2-chloroocta-1,3,5,7-tetraen-1-yl]-lambda4-tellanyl)-4-methoxybenzene
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1-(dichloro[(Z)-2-chloro-2-phenylethenyl]-l4-tellanyl)-4-methoxybenzene
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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-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
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1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
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1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
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1-[4-[3-(5-nitroquinolin-8-yl)furan-2-yl]phenyl]ethan-1-one
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1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]-3-(ethoxycarbonyl)aziridine-2-carboxylic acid
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1-[N-(tert-butoxycarbonyl)-L-phenylalanyl]aziridine-2,3-dicarboxylic acid
-
2,12-diethyl-11-methylhexadecyl 2-ethyl-11-methylhexadecyl phthalate
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isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
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-
2-bromo-4-nitronaphthalen-1-amine
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-
2-chlorobenzohydrazide
competitive inhibition
2-ethyldecyl 2-ethylundecyl phthalate
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isolated from seahorse, Hippocampus Kuda Bleeker, NMR structure determination and analysis, overview
2-methoxybenzohydrazide
competitive inhibition
2-methyl-5-nitroquinolin-8-ol
-
2-pentyl-1,2-thiazol-3(2H)-one
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2-phenylisothiazol-3(2H)-one
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2-[(6-([3'-(aminomethyl)biphenyl-3-yl]oxy)-3,5-difluoropyridin-2-yl)oxy]benzoic acid
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2A2 monoclonal antibody
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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
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3,5-diphenyl-2-pyrazoline
-
3,5-diphenyl-4-amino-1,2,4-triazole
non-competitive inhibition
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-(2-hydroxy-3-methylphenyl)-5-(2-hydroxy-3-methylphenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(2-methylphenyl)-5-(2-methylphenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(3-aminophenyl)-5-(3-aminophenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(3-methylphenyl)-5-(3-methylphenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(4-chlorophenyl)-5-(4-chlorophenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(4-methylphenyl)-5-(4-methylphenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-(N-benzyloxycarbonylphenylalanylamido)-DL-1-fluoro-2-butanone
irreversible covalent inhibitor
3-([(2R)-2-cyano-2-([3-methyl-N-(2-methyl-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000049 mM
3-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-2,3-dihydro-1H-inden-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000053 mM
3-([(2R)-2-cyano-2-([N-(1,1-dimethyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-3-methyl-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
IC50: 0.0000053 mM
3-methylbutyl N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-prolinate
IC50: 0.367 mM
3-phenyl-5-(3-nitrophenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
3-phenyl-5-(4-nitrophenyl)-4-amino-1,2,4-triazole
non-competitive inhibition
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-(4-nitronaphthalen-1-yl)morpholine
-
-
4-bromochalcone phenyl hydrazone
-
4-chlorochalcone phenyl hydrazone
-
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
4-hydroxybenzohydrazide
competitive inhibition
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
-
4-methoxybenzohydrazide
competitive inhibition
4-methoxychalcone phenyl hydrazone
-
4-methylchalcone phenyl hydrazone
-
4-nitro-L-phenylalanine
inactivation rate is 3.0 mM/min
4-nitrochalcone phenyl hydrazone
-
4-nitronaphthalen-1-amine
-
-
4-nitronaphthalen-1-ol
-
-
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
5,7-dinitroquinolin-8-ol
-
-
5-(((2R)-2-cyano-2-[(3-methyl-N-phenyl-L-phenylalanyl)amino]ethoxy)methyl)-2-fluorobenzoic acid
IC50: 0.0000122 mM
5-(4-bromophenyl)-1,3-diphenyl pyrazole
-
5-(4-bromophenyl)-1,3-diphenyl-2-pyrazoline
-
5-(4-bromophenyl)-3-phenyl-2-pyrazoline
-
5-(4-chlorophenyl)-1,3-diphenyl pyrazole
-
5-(4-chlorophenyl)-1,3-diphenyl-2-pyrazoline
-
5-(4-chlorophenyl)-3-phenyl-2-pyrazoline
-
5-(4-methoxyphenyl)-1,3-diphenyl pyrazole
-
5-(4-methoxyphenyl)-1,3-diphenyl-2-pyrazoline
-
5-(4-methoxyphenyl)-3-phenyl-2-pyrazoline
-
5-(4-methylphenyl)-1,3-diphenyl pyrazole
-
5-(4-methylphenyl)-1,3-diphenyl-2-pyrazoline
-
5-(4-methylphenyl)-3-phenyl-2-pyrazoline
-
5-(4-nitrophenyl)-1,3-diphenyl pyrazole
-
5-(4-nitrophenyl)-1,3-diphenyl-2-pyrazoline
-
5-(4-nitrophenyl)-3-phenyl-2-pyrazoline
-
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
-
-
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
-
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
-
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
-
-
7'',4'''-dimethylamentoflavone
IC50: 0.00055 mM
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
-
-
7-epiclusianone
-
a prenylated benzophenone isolated from pericarp hexane extract of dried fruits of Rheedia brasiliensis
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
-
-
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
-
-
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
-
-
8-(morpholin-4-yl)-5-nitroquinoline
-
-
8-hydroxy-5-nitroquinoline-2-carbonitrile
-
8-hydroxy-5-nitroquinoline-7-carboxylic acid
-
-
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-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
AEBSF
0.2 mM, partial inhibition; 0.2 mM, partial inhibition; 0.2 mM, partial inhibition; 0.2 mM, partial inhibition
AM4299A
irreversible inhibition, IC50: 0.000073 mM
AM4299B
irreversible inhibition, IC50: 0.000130 mM
amentoflavone
IC50: 0.00175 mM
ammonium 1-tribromo-1,3,2-dioxatellurolane
-
-
ammonium 1-trichloro-1,3,2-dioxatellurolane
-
-
ankyrin repeat protein
i.e. DARPin 8h6
-
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
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-L-phenylalanyl-L-phenylalanyl diazomethyl ketone
irreversible covalent inhibitor
benzyloxycarbonyl-Leu-Leu-Tyr-CHN2
-
-
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-phenylalanyl diazomethyl ketone
irreversible covalent inhibitor
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
Bz-Phe-Arg-CH2F
irreversible covalent inhibitor
BzlNH-tES-Ile-Pro-OBzl
-
-
CA-074-OMe
-
blocks cysteine cathepsins in addition to CatB in in primary human antigen-presenting cells
CA028
irreversible inhibition, IC50: 0.000140 mM
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
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
-
chalcone phenyl hydrazone
-
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)
-
-
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)
-
-
CPI-H
-
peptide inhibitor of 13 kDa from rabbit skeletal muscle, noncompetitive
-
CPI-L
-
peptide inhibitor of 23 kDa from rabbit skeletal muscle, noncompetitive
-
CysC
-
natural inhibitor of CatB. CysC deletion in knockout mice leads to an enhanced CatB activity
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)
-
-
EDTA
89% remaining activity at 1 mM, 80% remaining activity at 2 mM
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 (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
-
ethyl (2R,3R)-3-(((1S)-1-[(4-carbamimidamidobutyl)carbamoyl]-3-methylbutyl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((1S)-3-methyl-1-[(3-methylbutyl)carbamoyl]butyl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-1-((3-fluorophenethyl)amino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-1-(hexylamino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((3-phenylpropyl)amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((4-phenylbutyl)-amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-(pentan-3-ylamino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
-
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-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
-
-
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
-
-
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
heparin
-
inhibition is strongly dependent on pH, no inhibition above pH 7.0
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
L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane
L-3-trans-(propylcarbamoyl)-oxirane-2-carbonyl-L-isoleucyl-L-proline
-
inhibition of cathepsin B decreases the number of active alpha ENaCs in 2F3 cells
L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl-L-isoleucyl-L-proline
treatment with a cathepsin B inhibitor, leads to transient reduction of local induration, expression of inflammatory cytokines, and subsequent attenuation of the systemic adaptive immune response
L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl-L-isoleucyl-L-proline methyl ester
activity of caspase 3 is significantly reduced in Dengue virus-infected HepG2 cells treated with cathepsin B or S inhibitor. Treatment with cathepsin B inhibitor also reduces the activity of caspase 9
L-3-trans-propylcarbamoyloxirane-2-carbonyl-L-isoleucyl-proline
-
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
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
-
Miraziridine A
irreversible covalent inhibitor
mizaridine
IC50: 0.00205 mM
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
-
-
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-(1-cyanocyclopropyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
-
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-(cyanomethyl)-5-nitroquinoline-8-carboxamide
-
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
-
N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
-
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
N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
N-(trans-epoxysuccinyl)-L-leucine 4-guanidinobutylamide
addition of E-64 significantly decreases the activities of cathepsin B and caspase 3, and TUNEL-positive cells in heat-shocked in vitro maturated (IVM) bovine cumulus-oocyte complexes. Addition of inhibitor during in vitro maturation under heat shock conditions significantly improves both developmental competence and quality of the produced embryos
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-acetyl-3,5-diphenyl pyrazolines
-
N-acetyl-5-(4-bromophenyl)-3-phenyl-2-pyrazoline
-
N-acetyl-5-(4-chlorophenyl)-3-phenyl-2-pyrazoline
-
N-acetyl-5-(4-methoxyphenyl)-3-phenyl-2-pyrazoline
-
N-acetyl-5-(4-methylphenyl)-3-phenyl-2-pyrazoline
-
N-acetyl-5-(4-nitrophenyl)-3-phenyl-2-pyrazoline
-
N-Acetyl-Leu-Leu-methional
reversible inhibitor
N-alpha-[(benzyloxy)carbonyl]-N-[(3S)-1-[(2,6-dimethylbenzoyl)oxy]-7-[(6-[(2Z)-2-[(2E,4E)-5-(1-ethyl-3,3-dimethyl-5-sulfo-3H-indolium-2-yl)penta-2,4-dien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
N-benzoyl-3,5-diphenylpyrazoline
-
N-benzoyl-5-(2-chloro phenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(3-chloro phenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(3-methoxy phenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(4-chloro phenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(4-methoxy phenyl)-3-phenylpyrazoline
-
N-benzoyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
N-benzyl-5-nitroquinolin-8-amine
-
-
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-benzyl-N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
-
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-2-carboxamide
-
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
-
N-benzyl-N-methyl-5-nitroquinolin-8-amine
-
-
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-formyl-3,5-diphenylpyrazoline
-
N-formyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
N-formyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
N-formyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
N-formyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
N-formyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
N-formyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
N-formyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
N-formyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
N-formyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
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-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
N-[[1-(1,3-benzothiazol-2-yl)piperidin-3-yl]methyl]-8-hydroxy-5-nitroquinoline-7-carboxamide
-
N-[[1-(1,3-benzoxazol-2-yl)piperidin-3-yl]methyl]-8-hydroxy-5-nitroquinoline-7-carboxamide
-
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
-
Ni2+
-
26.7% residual activity at 1 mM
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-chloromercuriphenyl sulfonic acid
p-hydroxymercuribenzoate
-
-
Pefabloc SC
1.0 mM, 11% loss of activity
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 cyclopropenone
reversible inhibitor
-
peptidyl diazomethyl ketone derivatives
-
phenylacetyl hydrazine
competitive inhibition
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
-
62.8% residual 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
-
-
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
RNA interference oligonucleotide shRNA-CTSB2
most efficient inhibition of cathepsin B at both mRNA and protein levels and results in suppressing endometrial cancer growth and development in vivo
-
Ru(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
-
i.e. RAPTA-C
-
sodium chloro[[4,4',4''-(phosphinidyne-kappaP)tris[benzenesulfonato]]aurate]
-
-
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
tokaramide A
IC50: 0.0000624 mM
TPCK
0.2 mM, partial inhibition; 0.2 mM, partial inhibition; 0.2 mM, partial inhibition; 0.2 mM, partial inhibition
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
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
Trp
inactivation rate is 12 mM/min
Tyr-(O-methyl)
inactivation rate is 1.548 mM/min
Tyr-(O-tert-butyl)
inactivation rate is 0.618 mM/min
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
-
[(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]
-
-
-
(2Z)-1,3-bis(2-methoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
(2Z)-1,3-bis(2-methoxyphenyl)-4-(trichloro-lambda4-tellanyl)but-2-en-1-one
-
-
1,10-phenanthroline
-
77.3% residual activity at 1 mM
1,10-phenanthroline
66% remaining activity at 1 mM, 68% remaining activity at 2 mM
1-tosylamide-2-phenylethyl chloromethylketone
-
moderate effect
1-tosylamide-2-phenylethyl chloromethylketone
-
-
1-tosylamide-2-phenylethyl chloromethylketone
-
-
1-tosylamide-2-phenylethyl chloromethylketone
-
-
2,2'-dipyridyl disulfide
-
-
2,2'-dipyridyl disulfide
-
-
2,2'-dipyridyl disulfide
-
-
acetyl-YVAD-chloromethyl ketone
-
caspase inhibitor, inhibition of enzyme contributes to neuroprotective properties of the inhibitor
acetyl-YVAD-chloromethyl ketone
-
caspase inhibitor, inhibition of enzyme contributes to neuroprotective properties of the inhibitor
antipain
-
complete inhibition at 1 mM
antipain
-
93% inhibition at 1 microM
bafilomycin A1
-
bafilomycin A1
-
100 nM significantly inhibits activity
CA-074
-
-
CA-074
a cathepsin B-specific inhibitor, inhibition CmCatB1
CA-074
irreversible cathepsin B 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
i.-e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline and its derivates, irreversible covalent inhibitor
CA-074
-
specific inhibitor
CA-074
irreversible cathepsin B inhibitor
CA-074
-
cathepsin B-specific inhibitor
CA-074
0.01 mM, 97% loss of activity
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
0.001 mM, complete inhibition; 0.001 mM, complete inhibition; 0.001 mM, complete inhibition; 0.001 mM, complete inhibition
CA-074-Me
-
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
-
i.e. propylcarbonyl-L-trans-epoxysuccinyl-Ile-Pro-OH, enzyme binding structure at the active site cleft, modelling, overview
CA-074-Me
-
cathepsin B inhibition decreases hepatic stellate cell proliferation and the expression of phenotypic markers of hepatic stellate cell activation, and it down-regulate alpha-smooth musle actin mRNA and protein levels in LX2 cells, overview. Reduction of CtsB and/or CtsD levels by siRNA decreases cell proliferation, compared to control siRNA-transfected LX2 cells
CA-074-Me
-
i.e. [L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline methyl ester
CA-074-Me
-
in vivo 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
-
a specific inhibitor, inhibits pro-interleukin-1beta processing in microglia
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
-
suppresses microglia conditioned culture medium-induced glioma cell death
CA-074Me
-
-
CA-074Me
-
a specific inhibitor for cathepsin B
CA-074Me
-
a selective cell-permeable 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
-
a cathepsin B inhibitor
CA030
irreversible inhibition, IC50: 0.00000438 mM
CA030
-
i.e. ethoxy-L-trans-epoxysuccinyl-Ile-Pro-OH
CA074
-
-
CA074
-
high specificity, 34000fold more effective on enzyme than on cathepsin X
CA074
irreversible inhibition, IC50: 0.00000194 mM
CA074
treatment of colorectal cancer cells cells with the cathepsin B inhibitor Ca074 leads to invasiveness of human CRC cells
CA074
-
an irreversible CB inhibitor
CA074Me
-
-
CA074Me
-
cathepsin B specific 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
chicken cystatin
-
-
Chloroquine
-
-
chymostatin
-
80% inhibition at 6 microM
chymostatin
-
85% inhibition at 5 microM
chymostatin
0.1 mM, 96% loss of activity
Cu2+
-
32% residual activity at 1 mM
cystatin
-
the enzyme retains 10% and 5% of its initial activity, after 30 min of incubation at 37°C, in the presence of 75 and 100 nM recombinant cystatin, respectively
-
cystatin
binding sequence is FFEYDGVVSGGPYLGK, by mass spectrometric analysis
-
cystatin
-
poor inhibitor, 51% inhibition at 100 nM
-
cystatin C
-
-
cystatin C
-
Porphyromonas gingivalis interrupts the interaction of cathepsin B with its inhibitor cystatin
-
cystatin C
-
an endogenous inhibitor of cysteine cathepsins, expression patterns of cathepsin B and cystatin C
-
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
-
DCG-04
-
an E-64-type inhibitor, inhibits both mature cathepsin B and its zymogen
E-64
-
complete inhibition at 1 mM
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
a cysteine protease inhibitor, inhibition of CmCatB1
E-64
0.02 mM, complete inhibition; 0.02 mM, complete inhibition; 0.02 mM, complete inhibition; 0.02 mM, complete inhibition
E-64
-
an irreversible cysteine protease inhibitor
E-64
irreversible inhibition, IC50: 0.000055 mM
E-64
-
irreversible inhibitor
E-64
-
broad-spectrum cysteine protease inhibitor, complete inhibition
E-64
-
an irreversible cysteine protease inhibitor
E-64
irreversible covalent inhibitor
E-64
-
i.e. L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane, irreversible inhibitor
E-64
-
a broad cysteine protease inhibitor
E-64
0.01 mM, 99% loss of activity
E-64c
irreversible inhibition, IC50: 0.00000870 mM
E-64c
inhibition of Cathepsin B alone not only reduces hyperthermic injury-induced apoptosis significantly but enhances the beneficial effects of preinduction of HSP-70 in reducing hyperthermic injury-induced apoptosis in H9C2 cells significantly
E-64d
-
E-64d
-
i.e. (L-3-trans-ethoxycarbonyloxirane-2-carbonyl)-L-leucine(3-methylbutyl)amide
E64
-
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
E64d
substituting ethyl(methyl) sulfane for 2-methylbutane (R2) of E64d improves the inhibitory activity and selectivity for cathepsin B inhibition
E64d
i.e. loxistatin, irreversible covalent inhibitor
Elastatinal
-
-
Hg2+
-
-
human cystatin A
-
-
-
Human cystatin C
-
-
-
iodoacetamide
-
-
iodoacetamide
-
concentrations above10 mM significantly decrease activity
iodoacetic acid
-
complete inhibition at 1 mM
iodoacetic acid
0.01 mM, partial inhibition; 0.01 mM, partial inhibition; 0.01 mM, partial inhibition; 0.01 mM, partial inhibition
iodoacetic acid
-
100% inhibition at 0.5 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
leupeptin
-
42.5% residual activity at 0.1 mM
leupeptin
-
98% inhibition at 1 microM
leupeptin
IC50: 0.0000213 mM
leupeptin
leupeptin lacks selectivity since it inhibits both serine and cysteine proteases
leupeptin
-
Ki: 0.15-0.17 nM
leupeptin
4% remaining activity at 0.010 mM, 1% remaining activity at 0.1 mM
Mg2+
-
-
Mg2+
-
50% inhibition at 2 mM
Mn2+
-
85.4% residual activity at 1 mM
Mn2+
-
10% inhibition at 8 mM, no inhibition at 2 mM
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, 40.4% inhibition at 0.010 mM in cell lysates
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-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-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
-
N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
-
N-ethylmaleimide
-
no inhibition at 1 mM
N-ethylmaleimide
-
no inhibition at 1 mM
N-ethylmaleimide
-
concentrations above10 mM significantly decrease activity
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
-
-
NC-2300
-
i.e. monosodium (2S,3S)-3-[[(1S)-1-isobutoxymethyl-3-methylbutyl]carbamoyl]oxirane-2-carboxylate, a cysteine cathepsin inhibitor
NC-2300
-
i.e. monosodium (2S,3S)-3-[[(1S)-1-isobutoxymethyl-3-methylbutyl]carbamoyl]oxirane-2-carboxylate, a cysteine cathepsin inhibitor
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuriphenyl sulfonic acid
-
-
p-chloromercuriphenyl sulfonic acid
-
-
peptidyl diazomethyl ketone derivatives
-
-
-
peptidyl diazomethyl ketone derivatives
-
peptidyl diazomethanes
-
phenylmethanesulfonyl fluoride
-
no inhibition at 10 microM
phenylmethanesulfonyl fluoride
-
no inhibition at 0.1 mM
phenylmethanesulfonyl fluoride
-
27-33% inhibition at 0.5 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 0.5 mM
PMSF
2 mM, partial inhibition; 2 mM, partial inhibition; 2 mM, partial inhibition; 2 mM, partial inhibition
PMSF
98% remaining activity at 0.5 mM, 93% remaining activity at 1 mM
Proteinase inhibitors
-
from chicken´s egg white
-
Proteinase inhibitors
-
from potato tuber
-
Proteinase inhibitors
-
from rat, human, tuna fish, toad, chicken
-
sheep cystatin B
-
-
-
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
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-amido(4-guanidino)butane
E-64; E-64; E-64
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-leucylamido(4-guanidino)butane
-
-
trans-epoxysuccinyl-leucylamido(4-guanidino)butane
-
-
Zn2+
-
14.7% residual activity at 1 mM
Zn2+
-
80% inhibition at 2 mM
[(benzyl(methyl)sulfane)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
-
-
[(benzyl(methyl)sulfane)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
-
-
[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-1,1'-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((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((S)-3-isopropyl-1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
-
-
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,1'-bis(diphenylphosphino)ferrocene)Cl2]
-
-
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,1'-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]
-
-
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
-
-
additional information
-
not inhibited by dithiothreitol, L-cysteine, EDTA, and EGTA
-
additional information
no inhibition with N-chloroacetyl-Gly-Gly-OH
-
additional information
-
no inhibition with N-chloroacetyl-Gly-Gly-OH
-
additional information
-
inhibitor screening and docking studies to cathepsin B, overview. Predicted bioactivities of inhibitor candidates and molecular mechanics
-
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
-
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
no inhibition of CmCatB1 by PMSF, leupeptin, pepstatin A, ethanol and DMSO
-
additional information
no inhibition of CmCatB1 by PMSF, leupeptin, pepstatin A, ethanol and DMSO
-
additional information
-
no inhibition of CmCatB1 by PMSF, leupeptin, pepstatin A, ethanol and DMSO
-
additional information
-
no inhibition of CatB by soybean cysteine protease inhibitor
-
additional information
No effects on cathepsin B activity by human chorionic gonadotropin and 17beta-estradiol
-
additional information
-
No effects on cathepsin B activity by human chorionic gonadotropin and 17beta-estradiol
-
additional information
-
analysis of further dipeptidyl nitriles as selective inhibitors
-
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, 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
-
development of cathepsin inhibitors and structure-based design of cathepsin B-specific inhibitor, binding mode at the active site and structure-activity relationship, overview. Quantitative assesment of inhibitor binding at the SN-site of cathepsin B, overview
-
additional information
-
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
-
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
-
no inhibition by human cystatin B
-
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
concanamycin A is an indirect inhibitor by specific inhibiton of VATPase
-
additional information
-
the inhibition of cathepsin B causes accumulation of 26-kDa pro-TNF-containing vesicles
-
additional information
-
growth inhibition of B-16 cells by the palladacycle compounds, overview
-
additional information
-
cathepsin B inhibitory activity of tetraene lactones from the fungus Talaromyces wortmannii, overview
-
additional information
-
not inhibitory: Z-FY(tert-butyl)-CHN(2)
-
additional information
inhibitory potency of a series benzyloxycarbonyl-Phe-X-diazomethylketone, in which Phe promotes binding at S2 while the amino acid X probes S1. The S1 region of cathepsin L also has the ability to accommodate large hydrophobic side chains. In this respect cathepsin L differs from cathepsin B. Thus benzyloxycarbonyl-Phe-Tyr(O-l-butyl)-diazomethylketone, inactivates cathepsin L with higher efficiency compared to cathepsin B
-
additional information
no inhibition with pepstatin A at 0.005 and 0.1 mM
-
additional information
-
no inhibition with pepstatin A at 0.005 and 0.1 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0161
2,4-dinitrophenyl-GARFW-OH
-
pH 6.0, 37°C
0.0096
2,4-dinitrophenyl-GDRFW-OH
-
pH 6.0, 37°C
0.012
2,4-dinitrophenyl-GERFW-OH
-
pH 6.0, 37°C
0.0016
2,4-dinitrophenyl-GFAFW-OH
-
pH 6.0, 37°C
0.0034
2,4-dinitrophenyl-GFDFW-OH
-
pH 6.0, 37°C
0.0008
2,4-dinitrophenyl-GFEFW-OH
-
pH 6.0, 37°C
0.0005
2,4-dinitrophenyl-GFFFW-OH
-
pH 6.0, 37°C
0.0014
2,4-dinitrophenyl-GFGFW-OH
-
pH 6.0, 37°C
0.0007
2,4-dinitrophenyl-GFHFW-OH
-
pH 6.0, 37°C
0.0021
2,4-dinitrophenyl-GFKFW-OH
-
pH 6.0, 37°C
0.0005 - 0.0017
2,4-dinitrophenyl-GFLFW-OH
0.0006
2,4-dinitrophenyl-GFQFW-OH
-
pH 6.0, 37°C
0.0052
2,4-dinitrophenyl-GFRAW-OH
-
pH 6.0, 37°C
0.0053
2,4-dinitrophenyl-GFRDW-OH
-
pH 6.0, 37°C
0.0096
2,4-dinitrophenyl-GFREW-OH
-
pH 6.0, 37°C
0.0012
2,4-dinitrophenyl-GFRFW-OH
-
pH 6.0, 37°C
0.0077
2,4-dinitrophenyl-GFRGW-OH
-
pH 6.0, 37°C
0.0045
2,4-dinitrophenyl-GFRHW-OH
-
pH 6.0, 37°C
0.0033
2,4-dinitrophenyl-GFRIW-OH
-
pH 6.0, 37°C
0.0008
2,4-dinitrophenyl-GFRKW-OH
-
pH 6.0, 37°C
0.0021
2,4-dinitrophenyl-GFRLW-OH
-
pH 6.0, 37°C
0.0045
2,4-dinitrophenyl-GFRQW-OH
-
pH 6.0, 37°C
0.005
2,4-dinitrophenyl-GFRRW-OH
-
pH 6.0, 37°C
0.0095
2,4-dinitrophenyl-GFRSW-OH
-
pH 6.0, 37°C
0.0018
2,4-dinitrophenyl-GFRVW-OH
-
pH 6.0, 37°C
0.009
2,4-dinitrophenyl-GFRWA-OH
-
pH 6.0, 37°C
0.0055
2,4-dinitrophenyl-GFRWD-OH
-
pH 6.0, 37°C
0.0106
2,4-dinitrophenyl-GFRWE-OH
-
pH 6.0, 37°C
0.0022
2,4-dinitrophenyl-GFRWF-OH
-
pH 6.0, 37°C
0.0162
2,4-dinitrophenyl-GFRWG-OH
-
pH 6.0, 37°C
0.012
2,4-dinitrophenyl-GFRWI-OH
-
pH 6.0, 37°C
0.0126
2,4-dinitrophenyl-GFRWK-OH
-
pH 6.0, 37°C
0.0042
2,4-dinitrophenyl-GFRWL-OH
-
pH 6.0, 37°C
0.0124
2,4-dinitrophenyl-GFRWP-OH
-
pH 6.0, 37°C
0.0115
2,4-dinitrophenyl-GFRWR-OH
-
pH 6.0, 37°C
0.0128
2,4-dinitrophenyl-GFRWS-OH
-
pH 6.0, 37°C
0.0223
2,4-dinitrophenyl-GFRWV-OH
-
pH 6.0, 37°C
0.0066
2,4-dinitrophenyl-GFRWY-OH
-
pH 6.0, 37°C
0.0036
2,4-dinitrophenyl-GFRYW-OH
-
pH 6.0, 37°C
0.0012
2,4-dinitrophenyl-GFSFW-OH
-
pH 6.0, 37°C
0.0004
2,4-dinitrophenyl-GFVFW-OH
-
pH 6.0, 37°C
0.0011
2,4-dinitrophenyl-GFYFW-OH
-
pH 6.0, 37°C
0.0086
2,4-dinitrophenyl-GHRFW-OH
-
pH 6.0, 37°C
0.0019
2,4-dinitrophenyl-GIRFW-OH
-
pH 6.0, 37°C
0.0041
2,4-dinitrophenyl-GKRFW-OH
-
pH 6.0, 37°C
0.0106
2,4-dinitrophenyl-GLRFW-OH
-
pH 6.0, 37°C
0.0022
2,4-dinitrophenyl-GPRFW-OH
-
pH 6.0, 37°C
0.0066
2,4-dinitrophenyl-GRRFW-OH
-
pH 6.0, 37°C
0.0038
2,4-dinitrophenyl-GSRFW-OH
-
pH 6.0, 37°C
0.0023
2,4-dinitrophenyl-GVRFW-OH
-
pH 6.0, 37°C
0.0011
2,4-dinitrophenyl-GYRFW-OH
-
pH 6.0, 37°C
0.004
4-(4-dimethylaminophenylazo)benzoyl-IEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0028 - 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
0.0035 - 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
0.0046 - 0.0078
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-D-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0037 - 0.0082
4-(4-dimethylaminophenylazo)benzoyl-L-Leu-L-Arg-Gly-L-Phe-L-Glu-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0056
4-(4-dimethylaminophenylazo)benzoyl-LEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.006 - 0.0066
4-(4-dimethylaminophenylazo)benzoyl-LRGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0035
4-(4-dimethylaminophenylazo)benzoyl-R-LVGFE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 5.0
0.0037 - 0.0046
4-(4-dimethylaminophenylazo)benzoyl-RIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0055
4-(4-dimethylaminophenylazo)benzoyl-RIIEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 4.5
0.0034 - 0.0049
4-(4-dimethylaminophenylazo)benzoyl-RLEGIE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.001 - 0.0038
4-(4-dimethylaminophenylazo)benzoyl-RLVG-beta-(2-naphthyl)alanine-E-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0029 - 0.0059
4-(4-dimethylaminophenylazo)benzoyl-RLVGF-L-alpha-aminoadipic acid-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.003 - 0.0145
4-(4-dimethylaminophenylazo)benzoyl-RLVGFD-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0022
4-(4-dimethylaminophenylazo)benzoyl-RLVGFE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
-
pH 6.0
0.0047 - 0.0078
4-(4-dimethylaminophenylazo)benzoyl-RLVGWE-5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid
0.0021
Abz-FF-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37°C
0.003
Abz-FR-3-dinitrophenyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37°C
0.0177
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-P-OH
-
pH 6.0, 37°C
0.0038
Abz-FR-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-W-OH
-
pH 6.0, 37°C
0.0179
Abz-FRA-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37°C
0.0014
Abz-FRF(NO2)A
37°C, pH 4.5
0.0328
Abz-FRF-epsilon-dinitrophenyl-L-lysyl-2,3-diaminopropionic acid-OH
-
pH 6.0, 37°C
0.0059
Abz-GIVRAK(Dnp)-OH
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C
0.0008
Abz-GIVRAK-Dnp
37°C, pH 4.5
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, 37°C
0.056
acetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
1.02 - 2
alpha-N-benzoyl-DL-Arg-beta-naphthylamide
0.05
Arg-4-methylcoumaryl-7-amide
-
-
0.51 - 24
benzoyl-DL-Arg-beta-naphthylamide
0.685 - 20
benzoyl-DL-Arg-p-nitroanilide
0.039
benzoyl-L-3-pyridyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.015
benzoyl-L-4-aminocyclohexyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.032
benzoyl-L-4-aminomethyl-N-isopropyl-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.019
benzoyl-L-4-aminomethyl-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.023
benzoyl-L-4-guanidine-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.052
benzoyl-L-4-piperidinyl-Ala-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.032
benzoyl-L-Arg-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.034
benzoyl-L-His-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.03
benzoyl-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.0232 - 0.18
benzoyl-Phe-Val-Arg-p-nitroanilide
0.2 - 1
benzoyl-Pro-Phe-Arg-p-nitroanilide
0.022 - 1.25
benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy-beta-naphthylamide
0.02 - 0.29
benzyloxycarbonyl-Arg-Arg-4-methoxy-beta-naphthylamide
0.006 - 0.467
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
0.099 - 0.2622
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
0.131
benzyloxycarbonyl-F-R-4-methylcoumarin-7-amide
-
pH 6.0
0.0287 - 0.0608
benzyloxycarbonyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide
0.0358 - 0.0656
benzyloxycarbonyl-L-phenylalaninyl-L-arginine 4-methylcoumaryl-7-amide
0.021 - 0.252
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
0.048
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 4.5
0.012 - 0.91
benzyloxycarbonyl-Val-Lys-Lys-Arg-4-methoxy-beta-naphthylamide
1.16
Boc-Asp-Pro-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22°C
0.35
Boc-Asp-Pro-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.3
Boc-L-Leu-L-Lys-L-Arg-4-methylcoumaryl-7-amide
-
22°C, value is quite stable in the range of pH 4.0 to pH 7.8
1.67
Boc-Val-Leu-Lys-4-methyl-7-amidocoumarin
-
pH 6.0, 22°C
0.53
Boc-Val-Pro-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.055
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin
-
pH 6.5, recombinant enzyme
1.2
Cbz-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.13
D-Pro-Phe-Arg-p-nitroanilide
-
-
4.53
D-Val-Leu-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
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
-
0.00288
N,N'-diBoc-dityrosine-Gly-(isoniazid)2
pH 6.2, 25°C
0.00201
N,N'-diBoc-dityrosine-Lys-(isoniazid)2
pH 6.2, 25°C
0.1
N-benzyloxycarbonyl-Arg-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22°C
1.22
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.047
N-benzyloxycarbonyl-Phe-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22°C
0.19
N-benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.007
N-benzyloxycarbonyl-Val-Ile-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.072
N-t-butyloxycarbonyl-Gln-p-nitrophenyl ester
-
isoenzyme I and isoenzyme II
0.212 - 0.226
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
0.043 - 0.075
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
0.00611
Nalpha-carbobenzoxy-L-Arg-L-Arg-7-amido-4-trifluoromethylcoumarin
recombinant enzyme, at pH 7.3 and 37°C
0.008
o-aminobenzoic acid-L-Lys-L-Leu-Gly-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.017
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)serine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.015
o-aminobenzoic acid-L-Lys-L-Leu-L-(O-benzyl)threonine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.019
o-aminobenzoic acid-L-Lys-L-Leu-L-(S-benzyl)cysteine-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.024
o-aminobenzoic acid-L-Lys-L-Leu-L-Arg-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.033
o-aminobenzoic acid-L-Lys-L-Leu-L-Phe-L-Phe-L-Ser-L-Lys-L-Gln-2,4-dinitrophenyl-ethylenediamine
-
pH 6.0
0.0125 - 0.047
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
0.081
phenylacetyl-L-Arg-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.027
phenylacetyl-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.88
Tos-Gly-Pro-Arg-4-methyl-7-amidocoumarin
-
pH 6.0, 22°C
0.06
Tos-Gly-Pro-Arg-4-methylcoumarin 7-amide
-
pH 6.0, 22°C
0.082
Z-L-Arg-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.04068
Z-L-Phe-L-Arg 7-amido-4-methylcoumarin
pH and temperature not specified in the publication
0.023
Z-L-Phe-L-Arg-4-methylcoumarin-7-amide
-
pH 6.0, 37°C
0.0005
2,4-dinitrophenyl-GFLFW-OH
-
pH 6.0, 37°C
0.0017
2,4-dinitrophenyl-GFLFW-OH
-
pH 6.0, 37°C
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
0.006
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
0.0037
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
0.0034
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
0.0047
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
1.02
alpha-N-benzoyl-DL-Arg-beta-naphthylamide
-
free enzyme
1.5 - 2
alpha-N-benzoyl-DL-Arg-beta-naphthylamide
-
encapsulated enzyme
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
-
-
0.0232
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
-
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
0.34
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.467
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.099
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
37°C, pH 4.5
0.2622
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
37°C, pH 4.5
0.0287
benzyloxycarbonyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide
pH 4.5,37°C
0.0608
benzyloxycarbonyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide
pH 4.5,37°C
0.0358
benzyloxycarbonyl-L-phenylalaninyl-L-arginine 4-methylcoumaryl-7-amide
pH 4.5,37°C
0.0656
benzyloxycarbonyl-L-phenylalaninyl-L-arginine 4-methylcoumaryl-7-amide
pH 4.5,37°C
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
-
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
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
0.00143 - 0.00217
hemoglobin
-
-
-
0.212
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.226
Nalpha-benzoyl-Arg-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.043
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.075
Nalpha-benzoyl-Phe-Arg-7-amido-4-methylcoumarin
pH 6.0, 37°C, recombinant enzyme
0.0125
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, wild-type enzyme
0.013
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H110A
0.014
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H111A in presence of heparin
0.016
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H111A
0.043
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, wild-type enzyme in presence of heparin
0.047
o-aminobenzoyl-L-Phe-L-Arg-L-Lys-epsilon-N-2,4-dinitrophenylamide
-
pH 6.0, 25°C, mutant H110A in presence of heparin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.181 - 0.25
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
0.000052
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-7-[(2,6-dimethylbenzoyl)oxy]-6-oxoheptan-1-aminium trifluoroacetate
pH 6, 37°C
0.00008
(5S)-5-([N-[(benzyloxy)carbonyl]-L-phenylalany]amino)-6-oxo-7-[(2,4,6-trimethylbenzoyl)oxy]heptan-1-aminium trifluoroacetate
pH 6, 37°C
0.019 - 0.079
(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
0.00035
(S)-18-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodo-1H-1,2,3-triazol-1-yl)-12,19-dioxo-3,6,9-trioxa-13-azaicosan-20-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.00037
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(3-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.000181
(S)-20-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-1-(4-iodophenyl)-1,14,21-trioxo-5,8,11-trioxa-2,15-diazadocosan-22-yl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.002
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-(3-iodobenzamido)-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.001
(S)-3-[(S)-2-([(benzyloxy)carbonyl]amino)-3-phenylpropanamido]-7-[6-(4-iodo-1H-1,2,3-triazol-1-yl)hexanamido]-2-oxoheptyl 2,4,6-trimethylbenzoate
pH 6, 37°C
0.126 - 0.172
([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
0.005 - 0.426
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
0.08
1,3,5-triphenyl pyrazole
pH 6, 37°C
0.0909
1,3,5-triphenyl-2-pyrazoline
pH 6, 37°C
0.034 - 0.17
1-(4-nitronaphthalen-1-yl)pyrrolidine
0.032 - 0.212
2-bromo-4-nitronaphthalen-1-amine
0.00136
2-chlorobenzohydrazide
pH 5, 37°C
0.0127
2-methoxybenzohydrazide
pH 5, 37°C
0.181 - 0.469
2-methyl-5-nitroquinolin-8-ol
0.04
3,5-diphenyl-2-pyrazoline
pH 6, 37°C
0.1205
3,5-diphenyl-4-amino-1,2,4-triazole
pH 5, 37°C
0.0032
3-(2-hydroxy-3-methylphenyl)-5-(2-hydroxy-3-methylphenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.0149
3-(2-methylphenyl)-5-(2-methylphenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.00095
3-(3-aminophenyl)-5-(3-aminophenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.0385
3-(3-methylphenyl)-5-(3-methylphenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.0024
3-(4-chlorophenyl)-5-(4-chlorophenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.008
3-(4-methylphenyl)-5-(4-methylphenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.00143
3-phenyl-5-(3-nitrophenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.0048
3-phenyl-5-(4-nitrophenyl)-4-amino-1,2,4-triazole
pH 5, 37°C
0.085 - 0.289
4-(4-nitronaphthalen-1-yl)morpholine
0.003883
4-bromochalcone phenyl hydrazone
pH 6, 37°C
0.00328
4-chlorochalcone phenyl hydrazone
pH 6, 37°C
0.0019
4-hydroxybenzohydrazide
pH 5, 37°C
0.118 - 0.323
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
0.00064
4-methoxybenzohydrazide
pH 5, 37°C
0.00288
4-methoxychalcone phenyl hydrazone
pH 6, 37°C
0.00315
4-methylchalcone phenyl hydrazone
pH 6, 37°C
0.000042
4-nitrochalcone phenyl hydrazone
pH 6, 37°C
0.147 - 0.217
4-nitronaphthalen-1-amine
0.373
4-nitronaphthalen-1-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.072 - 0.146
5,7-dinitroquinolin-8-ol
0.0526
5-(4-bromophenyl)-1,3-diphenyl pyrazole
pH 6, 37°C
0.000053
5-(4-bromophenyl)-1,3-diphenyl-2-pyrazoline
pH 6, 37°C
0.01481
5-(4-bromophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.0178
5-(4-chlorophenyl)-1,3-diphenyl pyrazole
pH 6, 37°C
0.01
5-(4-chlorophenyl)-1,3-diphenyl-2-pyrazoline
pH 6, 37°C
0.038
5-(4-chlorophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.0047
5-(4-methoxyphenyl)-1,3-diphenyl pyrazole
pH 6, 37°C
0.001311
5-(4-methoxyphenyl)-1,3-diphenyl-2-pyrazoline
pH 6, 37°C
0.07407
5-(4-methoxyphenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.007243
5-(4-methylphenyl)-1,3-diphenyl pyrazole
pH 6, 37°C
0.001365
5-(4-methylphenyl)-1,3-diphenyl-2-pyrazoline
pH 6, 37°C
0.1143
5-(4-methylphenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.001311
5-(4-nitrophenyl)-1,3-diphenyl pyrazole
pH 6, 37°C
0.01274
5-(4-nitrophenyl)-1,3-diphenyl-2-pyrazoline
pH 6, 37°C
0.000131
5-(4-nitrophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.311 - 0.364
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
0.143 - 0.162
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
0.047 - 0.107
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
0.203 - 0.243
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
0.154 - 0.198
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
0.117 - 0.136
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
0.024 - 0.207
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
0.155 - 0.18
8-(morpholin-4-yl)-5-nitroquinoline
0.142 - 0.214
8-hydroxy-5-nitroquinoline-2-carbonitrile
0.117 - 0.221
8-hydroxy-5-nitroquinoline-7-carboxylic acid
0.0302
ammonium 1-tribromo-1,3,2-dioxatellurolane
-
pH 6.5, 25°C
0.0127
ammonium 1-trichloro-1,3,2-dioxatellurolane
-
pH 6.5, 25°C
0.0024
Cabin-A1
-
pH 5.5, 37°C
0.29
Cabin-A2
-
pH 5.5, 37°C
0.0000876
canecystatin-1
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.00000058
canecystatin-4
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.01274
chalcone phenyl hydrazone
pH 6, 37°C
0.0000003 - 0.00000125
chicken cystatin
-
0.000072
CPI-H
-
pH 6.2, 30°C
-
0.00011
CPI-L
-
pH 6.2, 30°C
-
0.42
di-(2-ethylhexyl)phthalate
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.64
dibutyl phthalate
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.13 - 0.132
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
0.038 - 0.162
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-carboxylate
0.129 - 0.156
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
3.3
Gly-Pro-Phe-Pro-Ile
-
30°C
0.0038
human albutensin
-
pH 5.5, 37°C
0.000225
human cystatin A
-
pH 6.0, 22°C
-
0.0022
human cystatin B
-
pH 6.0, 22°C
-
0.000093
Human cystatin C
-
pH 6.0, 22°C
-
0.000015 - 0.000017
leupeptin
-
-
0.105 - 0.155
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
0.185
N-(1-cyanocyclopropyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.19 - 0.24
N-(cyanomethyl)-5-nitroquinoline-8-carboxamide
0.16 - 0.201
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
0.128
N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.01767
N-acetyl-3,5-diphenyl pyrazolines
pH 6, 37°C
0.06711
N-acetyl-5-(4-bromophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.1087
N-acetyl-5-(4-chlorophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.149
N-acetyl-5-(4-methoxyphenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
1.25
N-acetyl-5-(4-methylphenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.01141
N-acetyl-5-(4-nitrophenyl)-3-phenyl-2-pyrazoline
pH 6, 37°C
0.00012
N-alpha-[(benzyloxy)carbonyl]-N-[(3S)-1-[(2,6-dimethylbenzoyl)oxy]-7-[(6-[(2Z)-2-[(2E,4E)-5-(1-ethyl-3,3-dimethyl-5-sulfo-3H-indolium-2-yl)penta-2,4-dien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxoheptan-3-yl]-L-phenylalaninamide
pH 6, 37°C
0.00115
N-benzoyl-3,5-diphenylpyrazoline
pH 6, 37°C
0.000775
N-benzoyl-5-(2-chloro phenyl)-3-phenylpyrazoline
pH 6, 37°C
0.004901
N-benzoyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
pH 6, 37°C
0.000572
N-benzoyl-5-(2-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.000677
N-benzoyl-5-(3-chloro phenyl)-3-phenylpyrazoline
pH 6, 37°C
0.001594
N-benzoyl-5-(3-methoxy phenyl)-3-phenylpyrazoline
pH 6, 37°C
0.000195
N-benzoyl-5-(3-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.000925
N-benzoyl-5-(4-chloro phenyl)-3-phenylpyrazoline
pH 6, 37°C
0.001277
N-benzoyl-5-(4-methoxy phenyl)-3-phenylpyrazoline
pH 6, 37°C
0.000287
N-benzoyl-5-(4-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.349 - 0.364
N-benzyl-5-nitroquinolin-8-amine
0.035
N-benzyl-N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.156
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.182 - 0.185
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
0.196 - 0.242
N-benzyl-N-methyl-5-nitroquinolin-8-amine
0.0000227
N-formyl-3,5-diphenylpyrazoline
pH 6, 37°C
0.000018
N-formyl-5-(2-chlorophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000668
N-formyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000141
N-formyl-5-(2-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000146
N-formyl-5-(3-chlorophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000455
N-formyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000011
N-formyl-5-(3-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000211
N-formyl-5-(4-chlorophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000448
N-formyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0000113
N-formyl-5-(4-nitrophenyl)-3-phenylpyrazoline
pH 6, 37°C
0.0011
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.000064
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.0000785
oryzacystatin-1
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.0000112
oryzacystatin-1 clone A10
-
in 100 mM sodium acetate pH 5.5, 2.5 mM dithiothreitol, at 37°C
-
0.00087
phenylacetyl hydrazine
pH 5, 37°C
2.31
Pro-Phe-Pr-Gly-Pro-Ile
-
30°C
0.000215
sheep cystatin B
-
pH 6.0, 22°C
-
0.00000083
Z-Arg-Gly-Pro-Agly-Gly-Glu-OMe
-
0.0000000011
Z-Arg-Leu-His-Agly-Ile-Val-OMe
-
0.0000000086
Z-Arg-Leu-Phe-Agly-Val-Ala-OMe
-
0.0000075
Z-Arg-Leu-Val-Agly-Gly-Asp-OMe
-
0.000007
Z-Arg-Leu-Val-Agly-Gly-Glu-OMe
-
0.000000052
Z-Arg-Nle-Val-Agly-Gly-Glu-OMe
-
0.0048 - 0.0113
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
0.1675
[N-benzyl-N,N-diethylethanaminium]2 hexachloro-lambda6-tellane
-
pH 6.5, 25°C
additional information
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
0.181
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.25
(1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylic acid
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.019
(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.079
(benzyl[(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.126
([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.172
([(8-hydroxy-5-nitroquinolin-7-yl)methyl](methyl)amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.005
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.426
([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)acetonitrile
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.034
1-(4-nitronaphthalen-1-yl)pyrrolidine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.17
1-(4-nitronaphthalen-1-yl)pyrrolidine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.032
2-bromo-4-nitronaphthalen-1-amine
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.212
2-bromo-4-nitronaphthalen-1-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.181
2-methyl-5-nitroquinolin-8-ol
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.469
2-methyl-5-nitroquinolin-8-ol
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.085
4-(4-nitronaphthalen-1-yl)morpholine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.289
4-(4-nitronaphthalen-1-yl)morpholine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.118
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.323
4-methoxy-3-(3-methoxypropoxy)-1-(5-nitroquinolin-8-yl)pyridin-1-ium
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.147
4-nitronaphthalen-1-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.217
4-nitronaphthalen-1-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.072
5,7-dinitroquinolin-8-ol
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.146
5,7-dinitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.311
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.364
5-nitro-7-((4-[(pyridin-3-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.143
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.162
5-nitro-7-((4-[(pyridin-4-yl)methyl]piperazin-1-yl)methyl)quinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.047
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.107
5-nitro-N-[(pyridin-2-yl)methyl]quinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.203
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.243
7-([(2R)-2-methylpiperidin-1-yl]methyl)-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.154
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.198
7-[(benzylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.117
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.136
7-[(ethylamino)methyl]-5-nitroquinolin-8-ol
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.024
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.207
8-(4-methylpiperidin-1-yl)-5-nitroquinoline
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.155
8-(morpholin-4-yl)-5-nitroquinoline
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.18
8-(morpholin-4-yl)-5-nitroquinoline
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.142
8-hydroxy-5-nitroquinoline-2-carbonitrile
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.214
8-hydroxy-5-nitroquinoline-2-carbonitrile
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.117
8-hydroxy-5-nitroquinoline-7-carboxylic acid
-
Ki-value (dissociation of the enzyme-substrate-inhibitor-complex), substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.221
8-hydroxy-5-nitroquinoline-7-carboxylic acid
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.0000003
chicken cystatin
-
-
0.00000125
chicken cystatin
-
-
0.13
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.132
ethyl (1R,2S)-2-([(8-hydroxy-5-nitroquinolin-7-yl)methyl]amino)cyclohexane-1-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.038
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.162
ethyl 1-(5-nitroquinolin-8-yl)piperidine-4-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.129
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.156
ethyl 4-[(8-hydroxy-5-nitroquinolin-7-yl)methyl]piperazine-1-carboxylate
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.105
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.155
N,N-dimethyl-1-(5-nitroquinolin-8-yl)piperidine-3-carboxamide
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.19
N-(cyanomethyl)-5-nitroquinoline-8-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.24
N-(cyanomethyl)-5-nitroquinoline-8-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.16
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.201
N-(cyanomethyl)-8-hydroxy-5,7-dinitroquinoline-2-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.349
N-benzyl-5-nitroquinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.364
N-benzyl-5-nitroquinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.182
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: benzyloxycarbonyl-Arg-Arg-AMC, endopeptidase activity, pH and temperature not specified in the publication
0.185
N-benzyl-N-(cyanomethyl)-8-hydroxy-5-nitroquinoline-7-carboxamide
substrate: 2-aminobenzoy-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH, exopeptidase activity, pH and temperature not specified in the publication
0.196
N-benzyl-N-methyl-5-nitroquinolin-8-amine
-
substrate: 2-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys(Dnp)-OH (exopeptidase inhibition), pH 6, 37°C
0.242
N-benzyl-N-methyl-5-nitroquinolin-8-amine
-
substrate: CBZ-Arg-Arg-4-methyl-7-coumarylamide (endopeptidase inhibition), pH 5, 37°C
0.0048
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 4.5, 25°C, competitive versus carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin
0.0067
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 4.5, 25°C, competitive versus ortho-aminobenzoyl-Gly-Ile-Val-Arg-Ala-Lys-Nepsilon-2,4-dinitrophenyl-OH
0.0113
[2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
pH 6.0, 25°C, competitive versus carbobenzoxy-Arg-Arg-7-amido-4-methylcoumarin
additional information
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
value above 0.01
additional information
additional information
-
kinetic mechanism of inhibition by [2-[2-(2,4-dioxo-1,3-thiazolidin-3-yl)ethylamino]-2-oxoethyl] 2-(furan-2-carbonylamino) acetate
-
additional information
additional information
-
rates of association of cysteine protease inhibitors with catB1, overview
-
additional information
additional information
-
second-order inactivation rate constants for cathepsin B, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00012
(2(1H)-pyridinethionato-kappaS2)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
Homo sapiens
-
-
0.005
(acetato)(isopropylamine)(2-((2dimethylamino)-methyl)phenyl)Pd(II)
Homo sapiens
-
-
0.00171
(chloro)(isopropylamine)(2-((2dimethylamino)methyl)phenyl)Pd(II)
Homo sapiens
-
-
0.00152
(chloro)(pryidinyl)(2-((2dimethylamino)methyl)phenyl)Pd(II)
Homo sapiens
-
-
0.0009
(chloro)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN1] oxorhenium(V)
Homo sapiens
-
-
0.00126
(methanethiolato)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.0886
(p-methoxyphenylthiolato-S)[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.00651
(p-methoxyphenylthiolato-S)[2,6-bis[(mercapto-kappaS)methyl]pyridine-kappaN] oxorhenium(V)
Homo sapiens
-
-
0.25
(triethylphosphine)gold(I) chloride
Homo sapiens
-
-
0.000032
1-(3-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.00011
1-(4-chlorophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.00004
1-(4-cyanophenyl)-3-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.000032
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-(3-methylphenyl)urea
Homo sapiens
-
pH 5.5, 30°C
0.000053
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-phenylurea
Homo sapiens
-
pH 5.5, 30°C
0.000023
1-[1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]-3-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
-
pH 5.5, 30°C
0.13
2,12-diethyl-11-methylhexadecyl 2-ethyl-11-methylhexadecyl phthalate
Rattus norvegicus
-
-
0.1
2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
Homo sapiens
-
IC50 above 0.1 mM, in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.21
2-ethyldecyl 2-ethylundecyl phthalate
Rattus norvegicus
-
-
0.013
2-pentyl-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.1
2-phenylisothiazol-3(2H)-one
Homo sapiens
-
IC50 above 0.1 mM, in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
702 - 761
2A2 monoclonal antibody
-
0.000002
3-(([(3S)-3-((N-[(4-chloro-2-fluorophenyl)carbonyl]-3-methyl-L-phenylalanyl)amino)-3-cyanopropyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.000002 mM
0.0000094
3-(([(3S)-3-cyano-3-([3-methyl-N-(phenylcarbonyl)-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.0000094 mM
0.0000018
3-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.0000018 mM
0.0000049
3-([(2R)-2-cyano-2-([3-methyl-N-(2-methyl-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000049 mM
0.0000053
3-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-2,3-dihydro-1H-inden-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000053 mM
0.0000053
3-([(2R)-2-cyano-2-([N-(1,1-dimethyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)-3-methyl-L-phenylalanyl]amino)ethoxy]methyl)benzoic acid
Homo sapiens
IC50: 0.0000053 mM
0.367
3-methylbutyl N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-prolinate
Homo sapiens
IC50: 0.367 mM
0.000018
3-[(5S)-5-cyano-5-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)pentyl]benzoic acid
Homo sapiens
IC50: 0.000018 mM
0.00168
4'''-methylamentoflavone
Homo sapiens
IC50: 0.00168 mM
0.000005
4-(([(3S)-3-cyano-3-([N-(diphenylacetyl)-3-methyl-L-phenylalanyl]amino)propyl]oxy)methyl)benzoic acid
Homo sapiens
IC50: 0.000005 mM
0.00175
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-hydroxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00175 mM
0.00168
5,7-dihydroxy-2-(4-hydroxy-3-[7-hydroxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00168 mM
0.00055
5,7-dihydroxy-2-(4-hydroxy-3-[7-methoxy-2-(4-methoxyphenyl)-4-oxo-4H-chromen-8-yl]phenyl)-4H-chromen-4-one
Homo sapiens
IC50: 0.00055 mM
0.0000122
5-(((2R)-2-cyano-2-[(3-methyl-N-phenyl-L-phenylalanyl)amino]ethoxy)methyl)-2-fluorobenzoic acid
Homo sapiens
IC50: 0.0000122 mM
0.0000041
5-([(2R)-2-cyano-2-([3-methyl-N-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalanyl]amino)ethoxy]methyl)-2-fluorobenzoic acid
Homo sapiens
IC50: 0.0000041 mM
0.00025
5-amino-1-(phenylsulfonyl)-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.00126
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl furan-2-carboxylate
Homo sapiens
-
-
0.00044
5-amino-1-[(4-fluorophenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.00069
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.00175
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl furan-2-carboxylate
Homo sapiens
-
-
0.00199
5-amino-1-[(4-methylphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-2-carboxylate
Homo sapiens
-
-
0.0041
5-chloro-2-(2-chloro-4,5-dimethoxyphenethyl)isothiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.042
5-chloro-2-(3-chloro-4-fluorophenyl)-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0073
5-chloro-2-pentyl-1,2-thiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.013
5-chloro-2-phenylisothiazol-3(2H)-one
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.00055
7'',4'''-dimethylamentoflavone
Homo sapiens
IC50: 0.00055 mM
0.0004
aceto[2,6-bis[(butylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
Homo sapiens
-
-
0.01346
aceto[2,6-bis[(methylthio-kappaS)methyl]phenyl-kappaC]-,(SP-4-3)Pd(II)
Homo sapiens
-
-
0.00274
aceto[2,6-bis[(phenylthio-kappaS)methyl]phenyl-kappaC]-, (SP-4-3)Pd(II)
Homo sapiens
-
-
0.00015
acetyl-Leu-Ile-arginal
Homo sapiens
IC50: 0.00015 mM
0.00013
acetyl-Leu-Leu-lysinal
Homo sapiens
IC50: 0.00013 mM
0.0011
acetyl-Leu-Phe-arginal
Homo sapiens
IC50: 0.0011 mM
0.0001
acetyl-Leu-Phe-lysinal
Homo sapiens
IC50: 0.0001 mM
0.000004
acetyl-Leu-Val-lysinal
Homo sapiens
IC50: 0.000004 mM
0.000039
acetyl-Phe-Val-arginal
Homo sapiens
IC50: 0.000039 mM
0.000073
AM4299A
Homo sapiens
irreversible inhibition, IC50: 0.000073 mM
0.00013
AM4299B
Homo sapiens
irreversible inhibition, IC50: 0.000130 mM
0.00175
amentoflavone
Homo sapiens
IC50: 0.00175 mM
0.00062
AMF4
Homo sapiens
IC50: 0.00062 mM
0.037
benzyl N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-alanyl-L-phenylalaninate
Homo sapiens
IC50: 0.037 mM
0.000044
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.000044 mM
0.029
benzyl [(1R)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-4-methylpentyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.0290 mM
0.1
benzyl [(1R)-1-([1-benzyl-2-hydroxy-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: more than 0.1 mM
0.0229
benzyl [(1R)-1-([2-hydroxy-1-methyl-2-(3-oxo-2-phenylcycloprop-1-en-1-yl)ethyl]carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.0229 mM
0.00945
benzyl [(1R)-2-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)amino)-1-methyl-2-oxoethyl]carbamate
Homo sapiens
IC50: 0.00945 mM
0.00071
benzyl [(1S)-1-((1-[hydroxy(3-oxo-2-phenylcycloprop-1-en-1-yl)methyl]-2-methylpropyl)carbamoyl)-2-methylpropyl]carbamate
Homo sapiens
IC50: 0.00071 mM
0.046
benzylamido-L-trans-epoxysuccinyl-Ile-O-benzyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000029
benzylamido-L-trans-epoxysuccinyl-Ile-Pro-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.18
bis(2-ethyldodecyl) phthalate
Rattus norvegicus
-
-
0.29
bis(2-ethylheptyl) phthalate
Rattus norvegicus
-
-
0.046
BzlNH-tES-Ile-Pro-OBzl
Bos taurus
-
-
0.000029
BzlNH-tES-Ile-Pro-OH
Bos taurus
-
-
0.00000228
CA-030
Homo sapiens
pH and temperature not specified in the publication
0.00000224 - 0.00000661
CA-074
0.000038
CA-074-Me
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
CA028
Homo sapiens
irreversible inhibition, IC50: 0.000140 mM
0.00000438 - 0.00012
CA030
0.00000194
CA074
Homo sapiens
irreversible inhibition, IC50: 0.00000194 mM
0.00026
cathestatin A
Homo sapiens
irreversible inhibition, IC50: 0.000260 mM
0.00028
cathestatin B
Homo sapiens
irreversible inhibition, IC50: 0.000280 mM
0.000114
cathestatin C
Homo sapiens
irreversible inhibition, IC50: 0.000114 mM
0.1
chloro(diethylphenylphosphine)gold(I)
Homo sapiens
-
-
0.018
chloro(ethyldiphenylphosphine)gold(I)
Homo sapiens
-
-
0.000334
chloro(triphenylphosphine)gold(I)
Homo sapiens
-
-
0.000765
chloro(tris(p-fluorophenyl)phosphine)gold(I)
Homo sapiens
-
-
0.0000088
chloro-[2,2'-(thio-kappaS)bis[ethanethiolato-kappaS]] oxorhenium(V)
Homo sapiens
-
-
0.204
chloro[4-(diphenylphosphino-kappaP)benzenamine]gold(I)
Homo sapiens
-
-
0.0097
chloro[4-(diphenylphosphino-kappaP)benzoato]gold(I)
Homo sapiens
-
-
0.064
chloro[diphenyl(phenylmethyl)phosphine]gold(I)
Homo sapiens
-
-
0.23
chloro[diphenyl[4-(2-phenyl-1,3-dioxolan-2-yl)phenyl]phosphine-kappaP]gold(I)
Homo sapiens
-
-
0.18
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzamide]gold(I)
Homo sapiens
-
-
0.28
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzeneacetamide]gold(I)
Homo sapiens
-
-
0.35
chloro[N-[2-(diphenylphosphino-kappaP)ethyl]benzenepropanamide]gold(I)
Homo sapiens
-
-
0.078
chloro[tris(p-methoxyphenyl)phosphine]gold(I)
Homo sapiens
-
-
0.0097
chloro[tris(pentafluorophenyl)phosphine]gold(I)
Homo sapiens
-
-
0.000289
chloro[[1,1'-biphenyl]-4-yldiphenylphosphine]gold(I)
Homo sapiens
-
-
0.0028
CID 11834381
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0331
CID 11834389
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0032
CID 11834392
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.046
CID 1506381
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0071
CID 2212050
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0115
CID 286532
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0094
CID 2998380
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
CID 3236798
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0007
CID 3240114
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00044
CID 3241895
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00085
CID 3243025
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00026
CID 3243128
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0086
CID 3243168
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0184
CID 3250046
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0223
CID 3685806
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00225
CID 5293426
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0339
CID 573353
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
CID 646525
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0123
CID 646749
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000071
CID 647501
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
CID 647599
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0064
CID 648315
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00175
CID 651936
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000072
CID 653297
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.045
CID 653316
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00092
CID 653862
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
CID 654815
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0096
CID 655490
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0067
CID 658111
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0197
CID 658152
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0089
CID 658724
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.04
CID 658964
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0385
CID 660829
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000046
CID 66541
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
CID 665480
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0142
CID 714967
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0042
CID 794694
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0372
CID 971438
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.06
cystatin
Angiostrongylus cantonensis
-
at pH 5.0 and 37°C
-
0.000486
cystatin C
Fasciola gigantica
37°C, pH 4.5
-
0.14 - 0.38
di-(2-ethylhexyl)phthalate
0.0006
diacetato(2-((2dimethylamino)methyl)phenyl)-Au(III)
Homo sapiens
-
-
0.00129
diaceto[2-[(2-pyridinyl-kappaN)methyl]-phenyl-kappaC]Au(III)- (SP-4-3)
Homo sapiens
-
-
0.23 - 0.42
dibutyl phthalate
0.00136
dichloro(2-((2dimethylamino)methyl)phenyl)Au(III)
Homo sapiens
-
-
0.00085
dichloro[2-[(2-pyridinyl-kappaN)methyl]phenyl-kappaC]Au(III)
Homo sapiens
-
-
0.000055
E-64
Homo sapiens
irreversible inhibition, IC50: 0.000055 mM
0.0000087
E-64c
Homo sapiens
irreversible inhibition, IC50: 0.00000870 mM
0.0000003
E64c
Mus musculus
-
-
0.00001203
E64d
Homo sapiens
37°C, pH not specified in the publication
0.00027
estatin A
Homo sapiens
irreversible inhibition, IC50: 0.000270 mM
0.00032
estatin B
Homo sapiens
irreversible inhibition, IC50: 0.000320 mM
0.0153
ethoxy-L-trans-epoxysuccinyl-Gly-Pro-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000023
ethoxy-L-trans-epoxysuccinyl-Ile-Ala-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
ethoxy-L-trans-epoxysuccinyl-Ile-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.024
ethoxy-L-trans-epoxysuccinyl-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00041
ethoxy-L-trans-epoxysuccinyl-Thr-Ile-OH
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00002409
ethyl (2S,3S)-3-(((S)-1-((3-fluorophenethyl)amino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00000427
ethyl (2S,3S)-3-(((S)-1-(hexylamino)-4-(methylthio)-1-oxobutan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00000716
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((3-phenylpropyl)amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00002368
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-((4-phenylbutyl)-amino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
0.00007427
ethyl (2S,3S)-3-(((S)-4-(methylthio)-1-oxo-1-(pentan-3-ylamino)butan-2-yl)carbamoyl)oxirane-2-carboxylate
Homo sapiens
37°C, pH not specified in the publication
4.4
ethyl 1-[(2R)-2-((1S)-1-(acetyloxy)-2-[((N-[(2,4-difluorophenyl)carbonyl]-L-phenylalanyl)amino)oxy]-2-oxoethyl)pentanoyl]prolinate
Homo sapiens
IC50: 4.4 mM
0.014
ethyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.0153
EtO-tES-Gly-Pro-OH
Bos taurus
-
-
0.000023
EtO-tES-Ile-Ala-OH
Bos taurus
-
-
0.000024
EtO-tES-Ile-Ile-OH
Bos taurus
-
-
0.024
EtO-tES-Ile-OH
Bos taurus
-
-
0.00012
EtO-tES-Ile-Pro-OH
Bos taurus
-
-
0.00058
HIF
Homo sapiens
IC50: 0.00058 mM
0.00037
human cystatin A
Homo sapiens
-
pH 6.0, 22°C
-
0.0000006
Human cystatin C
Homo sapiens
-
pH 6.0, 22°C
-
0.0000213 - 0.075
leupeptin
0.00061
malonato(2-((2dimethylamino)methyl)phenyl)Au(III)
Homo sapiens
-
-
0.0085
methyl 3-(4,5-dichloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.012
methyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.011
methyl 3-(5-chloro-4-methyl-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.011
methyl 4-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)butanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.024
methyl 6-(3-(propyldisulfanyl)acrylamido)hexanoate
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.00205
mizaridine
Homo sapiens
IC50: 0.00205 mM
0.0049
myricetin
Homo sapiens
pH and temperature not specified in the publication
0.3
N-(3-carboxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.300 mM
0.0026
N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.0026 mM
0.447
N-(3-methyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.447 mM
0.074
N-(3-phenyl-1,2,4-thiadiazolidin-5-yl)-L-leucyl-L-proline
Homo sapiens
IC50: 0.074 mM
0.00004
N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucylamino-3-methylbutane
Bos taurus
-
-
0.000002
N-(L-3-trans-propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline
Mus musculus
-
-
0.000046
N-phenyl-3-(propyldisulfanyl)-3-chloro-acrylamide
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.012
N-phenyl-3-(propyldisulfanyl)acrylamide
Homo sapiens
-
in 100 mM Na2HPO4, 1.25 mM EDTA., pH 6.8, at 25°C
0.000005
N-[(1R)-1-cyano-2-([3-(2H-tetrazol-2-yl)benzyl]oxy)ethyl]-3-methyl-Na-(3-oxo-1,3-dihydro-2-benzofuran-5-yl)-L-phenylalaninamide
Homo sapiens
IC50: 0.000005 mM
0.0000102
N-[(1S)-3-(benzyloxy)-1-cyanopropyl]-Nalpha-(diphenylacetyl)-3-methyl-L-phenylalaninamide
Homo sapiens
IC50: 0.0000102 mM
0.39
N-[(3-methoxy-1,2,4-thiadiazolidin-5-yl)carbamoyl]-L-leucyl-L-proline
Homo sapiens
IC50: 0.390 mM
0.021
Na-[(benzyloxy)carbonyl]-N-(3-methoxy-1,2,4-thiadiazolidin-5-yl)-L-phenylalaninamide
Homo sapiens
IC50: 0.021 mM
0.00047
Nalpha-[(benzyloxy)carbonyl]-N-[(2R,3S)-2-(carboxyoxy)-4-oxoazetidin-3-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00047 mM
0.00043
Nalpha-[(benzyloxy)carbonyl]-N-[(3S,4R)-2-oxo-4-phenoxyazetidin-3-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00043 mM
0.00035
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-4,4-dioxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00035 mM
0.0005
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6R)-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: more than 0.00050 mM
0.00176
Nalpha-[(benzyloxy)carbonyl]-N-[(5R,6S)-7-oxo-4-oxa-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.00176 mM
0.0164
Nalpha-[(benzyloxy)carbonyl]-N-[(6R)-4-oxido-7-oxo-4-thia-1-azabicyclo[3.2.0]hept-6-yl]-L-phenylalaninamide
Homo sapiens
IC50: 0.0164 mM
0.2
oxalo-RAPTA
Bos taurus
-
above, pH 6.0, 30°C
0.0091
PrnNH-tES-Ile-Pro-OBzl
Bos taurus
-
-
0.000038
PrnNH-tES-Ile-Pro-OH
Bos taurus
-
-
0.068
PrnNH-tES-Ile-Pro-OMe
Bos taurus
-
-
0.0091
propylcarbonyl-L-trans-epoxysuccinyl-Ile-O-benzyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.068
propylcarbonyl-L-trans-epoxysuccinyl-Ile-Pro-O-methyl ester
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0082
quercetin
Homo sapiens
pH and temperature not specified in the publication
0.005
RAPTA-BC
Bos taurus
-
pH 6.0, 30°C
0.1
RAPTA-BI
Bos taurus
-
above, pH 6.0, 30°C
0.0025
RAPTA-C
Bos taurus
-
pH 6.0, 30°C
0.2
RAPTA-H
Bos taurus
-
above, pH 6.0, 30°C
-
0.0065
RAPTA-Me+C
Bos taurus
-
pH 6.0, 30°C
0.003
RAPTA-NH3
Bos taurus
-
pH 6.0, 30°C
0.0016
RAPTA-OH
Bos taurus
-
pH 6.0, 30°C
0.007
RAPTA-pentaOH
Bos taurus
-
pH 6.0, 30°C
0.0015
RAPTA-T
Bos taurus
-
pH 6.0, 30°C
0.082
RAPTA-TBMe
Bos taurus
-
pH 6.0, 30°C
0.0245
RAPTA-TBOH
Bos taurus
-
pH 6.0, 30°C
0.353
Ru(II)-pentamethylcyclopentadienyl 1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane N-acetyl-L-cysteine-N'-methylamide
Homo sapiens
-
pH 6.0, 30°C
-
0.00041
sheep cystatin B
Homo sapiens
-
pH 6.0, 22°C
-
0.075
sodium chloro[[4,4',4''-(phosphinidyne-kappaP)tris[benzenesulfonato]]aurate]
Homo sapiens
-
-
0.00068
stefin-1
Fasciola gigantica
37°C, pH 4.5
-
0.00013
stefin-2
Fasciola gigantica
37°C, pH 4.5
-
0.000038
tert-butyl ([1-[(2-cyanotetrahydropyridazin-1(2H)-yl)carbonyl]-2-methylpropyl]carbamoyl)carbamate
Homo sapiens
-
pH 5.5, 30°C
0.00032
TMC-52A
Homo sapiens
irreversible inhibition, IC50: 0.000320 mM
0.0002
TMC-52B
Homo sapiens
irreversible inhibition, IC50: 0.000200 mM
0.00046
TMC-52C
Homo sapiens
irreversible inhibition, IC50: 0.000460 mM
0.00028
TMC-52D
Homo sapiens
irreversible inhibition, IC50: 0.000280 mM
0.0000624
tokaramide A
Homo sapiens
IC50: 0.0000624 mM
0.0055
trans-cis-cis-[RuCl2(DMSO)2(2-amino-5-methyl-thiazole)2]
Bos taurus
-
pH 6.0, 30°C
0.000016
WF14861
Homo sapiens
irreversible inhibition, IC50: 0.000016 mM
0.0000084
WF14865A
Homo sapiens
irreversible inhibition, IC50: 0.0000084 mM
0.000013
WF14865B
Homo sapiens
irreversible inhibition, IC50: 0.000013 mM
0.0043
wortmannilactone E
Mus musculus
-
pH 5.5, 22°C
0.0065
wortmannilactone F
Mus musculus
-
pH 5.5, 22°C
0.013
wortmannilactone G
Mus musculus
-
pH 5.5, 22°C
0.006
wortmannilactone H
Mus musculus
-
pH 5.5, 22°C
0.000012
YM 51084
Homo sapiens
IC50: 0.000012 mM
0.0002
[(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
Bos taurus
-
pH 6.0, 30°C
0.00015
[(benzyl(methyl)sulfane)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
Bos taurus
-
pH 6.0, 30°C
0.00007
[(N,N-dimethyl-1-phenylmethanamine)Pd(1,3,5-triaza-7-phosphaadamantane)Cl]
Bos taurus
-
pH 6.0, 30°C
0.000011
[1-(2-cyano-tetrahydro-pyridazine-1-carbonyl)-2-methyl-propyl]-carbamic acid benzyl ester
Homo sapiens
-
pH 5.5, 30°C
0.00018
[2-(mercapto-kappaS)benzoato(2-)-kappaO][2-[(2-pyridinyl-kappaN)methyl]phenyl-kappaC]Au(III)
Homo sapiens
-
-
0.5
[Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phospatatricyclo[3.3.1.1]decane)Cl2], [Ir(III)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)2Cl]PF6
Homo sapiens
-
above, pH 6.0, 30°C
-
0.349
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl2]OTf
Homo sapiens
-
pH 6.0, 30°C
-
0.5
[Ir(III)-pentamethylcyclopentadienyl-methyl(1,3,5-triaza-7-phosphatricyclo-[3.3.1.1]decane)Cl](OTf)PF6
Homo sapiens
-
above, pH 6.0, 30°C
-
0.000038
[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]
Bos taurus
-
pH 6.0, 30°C
0.0000095
[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]
Bos taurus
-
pH 6.0, 30°C
0.000012
[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]
Bos taurus
-
pH 6.0, 30°C
0.003
[Pd2(1-methyl-5-phenyl-1H-1,4-benzodiazepin-2(3H)-one)2(m-1,2-ethanebis(diphenylphosphine))Cl2]
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00003
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,1'-bis(diphenylphosphino)ferrocene)Cl2]
Bos taurus
-
pH 6.0, 30°C
0.000023
[Pd2(1-methyl-5-phenyl-1H-benzo[e][1,4]diazepin-2(3H)-one)2(m-1,2-bis(diphenylphosphino)ethane)Cl2]
Bos taurus
-
pH 6.0, 30°C
0.4
[Ru(II)-pentamethylcyclopentadienyl-(1,3,5-triaza-7-phosphatatricyclo[3.3.1.1]decane)Cl2]
Homo sapiens
-
above, pH 6.0, 30°C
-
additional information
additional information
-
702
2A2 monoclonal antibody
Homo sapiens
-
pH 6.0, 37°C, versus substrate DQ-collagen IV
-
761
2A2 monoclonal antibody
Homo sapiens
-
pH 6.0, 37°C, versus substrate BODIPY FL casein
-
0.00000224
CA-074
Homo sapiens
pH and temperature not specified in the publication
0.00000661
CA-074
Homo sapiens
37°C, pH not specified in the publication
0.00000438
CA030
Homo sapiens
irreversible inhibition, IC50: 0.00000438 mM
0.00012
CA030
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.14
di-(2-ethylhexyl)phthalate
Homo sapiens
-
recombinant enzyme, in Hank's balanced salt solution containing 2 mM L-cysteine, pH 7.0, at 37°C
0.38
di-(2-ethylhexyl)phthalate
Homo sapiens
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.23
dibutyl phthalate
Homo sapiens
-
recombinant enzyme, in Hank's balanced salt solution containing 2 mM L-cysteine, pH 7.0, at 37°C
0.42
dibutyl phthalate
Homo sapiens
-
wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C
0.0000213
leupeptin
Homo sapiens
IC50: 0.0000213 mM
0.075
leupeptin
Mus musculus
-
pH 5.5, 22°C
additional information
additional information
Homo sapiens
-
IC50 values for cell proliferation of prenylated benzophenones from Rheedia brasiliensis, overview
-
additional information
additional information
Mus musculus
-
IC50 values for growth inhibition of K-562 cells by palladacycles, overview
-
additional information
additional information
Homo sapiens
-
IC50 values of palladacycles in cytotoxicity assay, overview
-
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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
-
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 confers protection against cell death in clonogenic assays of CD34+ primary cells from chronic myelogenous leukemia patients
malfunction
-
cathepsin B is a major lysosomal protease, its overactivation is involved in muscular dystrophy, bone resorption, pulmonary emphysem, and tumor metastasis
malfunction
-
cathepsin B is involved in several cancers
malfunction
-
cathepsin B is involved in several cancers
malfunction
-
cathepsin B overexpression in glioblastoma is correlated with a short survival of the patient
malfunction
-
cathepsin B significantly decreases the number of apoptotic nuclei in both the cumulus cell layer of matured oocytes and blastocysts
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
-
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
-
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
-
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
-
extracellular release of the lysosomal proteases, cathepsins, and their inhibitors is associated with the development and progression of several types of cancer
malfunction
-
genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
malfunction
-
glioblastoma and endothelial cells cross-talk, mediated by SDF-1, enhances tumour invasion and endothelial proliferation by increasing expression of cathepsins B, S, and MMP-9. Enhanced invasiveness correlates with increased expression of MMP-9 in both U87 and HMEC-1 cells, increased expression of cysteine cathepsins B and S and down-regulation of endogenous cell adhesion molecule NCAM in U-87 cells. U-87 tumour cells significantly enhance the proliferation of co-cultured endothelial cells by a mechanism involving cathepsin B, but not cathepsin S, overview. Regulation of invasion of U-87 cells involves cathepsin B, overview
malfunction
-
inhibition of cathepsin B impairs lysosomal proteolysis. FYAD, an irreversible inhibitor of cathepsin B, induces apoptosis of neuroblastoma cells but not of other tumor cells. Inhibition of cathepsin D does not rescue cells from FYAD-induced death
malfunction
-
lysosomal destabilization contributes for cell death through controlled release of lysosomal enzymes, the prominent among them being cathepsin B. p53-dependent lysosomal destabilization and cathepsin B activation contribute for increased sensitivity of p21-deficient cells to embelin with enhanced caspase 9 and caspase 3 activation, overview
malfunction
-
Microglia induce apoptosis of glioma cells via the release of NO and cathepsin B protease. Cathepsin B causes a decrease in cell survival. Cathepsin B plays a critical role in cytotoxicity in the central nervous system
malfunction
-
Microglia induce apoptosis of glioma cells via the release of NO and cathepsin B protease. Cathepsin B causes a decrease in cell survival. Cathepsin B plays a critical role in cytotoxicity in the central nervous system
malfunction
-
specific blocking cathepsin B expression suppresses apoptosis but does not affect autophagy, which suggests that cathepsin B is a molecular link between autophagy and apoptosis. Cathepsin B inhibition decreases the SPARC-induced release of cytochrome c
malfunction
-
the activity of CatB, but not of CatL or CatS, is relevant to glioblastoma invasion, role of cathepsin B in glioma invasion by in vitro 3D spheroids migration modelling of in vivo glioma growth and invasion, overview
malfunction
-
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
-
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
-
blocking CTSB expression using CTSB siRNA suppresses inflammatory response but does not affect apoptosis markedly
malfunction
Cathepsin B silencing by RNAi in human colorectal cancer (CRC) cells inhibits their growth in soft agar, as well as their invasion capacity, tumoral expansion, and metastatic spread in immunodeficient mice
malfunction
-
CysC deletion in knockout mice leads to an enhanced CatB activity
malfunction
-
enhancing CatB activity by CysC deletion significantly lowers total amyloid-betaand amyloid-beta42 levels in human amyloid precursor protein wild-type mice, whereas CatB deletion increases amyloidbeta levels
malfunction
-
female Ctsb knockout mice, but not males, display a decrease of 31% in cholesterol absorption
malfunction
-
fine-mapping studies along with gene expression efforts and studies in knockout animals identified Ctsb as a gender-dependent modifier of cholesterol absorption from the intestine
malfunction
higher levels of the cell cycle inhibitor p27Kip1 are observed in cathepsin B-deficient tumors as well as an increase in cyclin B1
malfunction
reduced cathepsin B expression using RNA interference mimicks pharmacological inhibition of the enzyme and confirms the contribution of cathepsin B to apoptotic events induced by Dengue virus in HepG2 cells
malfunction
-
transgenic mice are generated overexpressing CatB under the control of a neuron-specific enolase promoter: Enhancing neuronal CatB activity in human amyloid precursor protein wild-type mice significantly lowers amyloidbeta42 levels
malfunction
silencing of cathepsin B significantly depresses coelomocytes apoptosis rate by 0.16fold
malfunction
silencing of cathepsin B significantly inhibits the development and hatching of Radopholus similis and greatly reduces its pathogenicity
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
-
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
-
genetic cathepsin B deficiency reduces beta-amyloid in transgenic mice expressing human wild-type amyloid precursor protein
-
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
-
metabolism
-
cathepsin B is involved in TNF-alpha-induced signal transduction pathways in lung cells
metabolism
-
cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death. ER-stress-induced programmed cell death (ERSID) is regulated positively by cathepsin B and negatively by proteasome subunit PBA1. Cathepsin B may execute its function after tonoplast rupture and works in parallel with vacuolar processing enzyme
metabolism
cathepsin B mediates radiation induced bystander effects. The enzyme seems to exert radiation induced bystander effects by acting through the insulin-like growth factor receptor DAF-2
metabolism
increase and leakage of CatB in microglia during aging are responsible for the increased generation of mitochondria-derived reactive oxygen species and proinflammatory mediators, culminating in memory impairment
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
-
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
-
BmCatB is involved in the programmed cell death of the fat body during metamorphosis, and CatB and CatD contribute to the metamorphosis
physiological function
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CatB is involved in but is not essential for antigen processing
physiological function
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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
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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
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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
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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
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cathepsins B and D drive hepatic stellate cell proliferation and promote their fibrogenic potential
physiological function
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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
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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
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CTSB is a lysosomal cysteine protease primarily involved in the degradation or processing of lysosomal proteins
physiological function
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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
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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
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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
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the cysteine protease CatB facilitates insects coping with dietary protease inhibitor challenge
physiological function
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the endopeptidase activity of cathepsin B is associated with the degradation of the extracellular matrix proteins, which is a process required for tumor cell invasion and metastasis, the activity can be inhibited by the 2A2 monoclonal antibody
physiological function
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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
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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
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TiO2-induced interleukin-1beta production depends on active cathepsin B and reactive oxygen species production
physiological function
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cathepsin B is involved in cuticle renewal
physiological function
cathepsin B is involved in host immune response during bacterial infection and vaccination
physiological function
cathepsin B is involved in the nutrient digestion of Meretrix meretrix
physiological function
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cathepsin B plays a role in doxorubicin-induced cell death
physiological function
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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
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cathepsin B proteinase plays roles in the early development of Ancylostoma caninum
physiological function
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the enzyme has stimulatory effects on embryonic development, metamorphosis, and larval growth during larval development
physiological function
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Atg7-induced CTSB overexpression contributes to an NLRP3-dependent proinflammatory response and subsequently impairs glucose-stimulated insulin secretion independently of apoptosis
physiological function
cathepsin B activates both caspase-9 and caspase-3
physiological function
cathepsin B is involved in hyperthermic injury-induced cardiomyocyte apoptosis in H9C2 cells and HSP-70 protects these cells from hyperthermic injury-induced cardiomyocyte apoptosis through cathepsin B pathways
physiological function
CsCBs are immune triggers during Clonorchis sinensis infection
physiological function
extracellular cathepsin B is involved in cell invasion whereas intracellular cathepsin B controls tumoral properties of colorectal cancer cells
physiological function
present results implicate cathepsin B activity as one of the possible pathways that are responsible for heat shock-induced apoptosis in bovine cumulus-oocyte complexes
physiological function
sensitivity to mHgIA is linked to an early cathepsin B regulated inflammatory response which is necessary for the subsequent adaptive autoimmune response leading to disease
physiological function
cathepsin B can modulate autophagy processes in adipocytes
physiological function
cathepsin B is essential for the development and pathogenesis of the plant parasitic nematode Radopholus similis
physiological function
exosomal cathepsin B regulates the receptor for advanced glycation end-products (RAGE) in type 1 alveolar cells under conditions of oxidative stress
physiological function
involved in tumour progression
physiological function
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role for maternal Ctsba in dorsoventral patterning and morphogenesis. Ctsba is required in distinct developmental processes to promote epiboly progression through modulation of the YCL cytoskeleton and promotes dorsoventral axial patterning upstream of BMP signaling. The role for Ctsba in morphogenesis is complex because Ctsba has BMP-dependent functions in DV patterning and probably also convergent-extension cell movements, but it also has BMP-independent functions necessary for the cytoskeletal organization underlying epiboly. Ctsba might modulate the ECM, regulate Ints6 or transcription factors such as Pou5f3, which have similar patterning and epiboly defects, or modulate other components to regulate early morphogenesis and epiboly
physiological function
the enzyme could be stable and highly active in the endolysosomal pathway degrading endocytosed peptides predigested by cathepsin L in the gut lumen whereas as a secreted protease it might be short lived but still stimulating an immune response. Due to its exopeptidase activity it could be involved in the regulative processing of other proteins. It is not involved in the immediate infection process
physiological function
the enzyme has critical role as activators of proinflammatory caspases-11 and the regulatory effect in LPS-induced caspases-11-dependent necrosis
physiological function
the enzyme is an important immune factor
physiological function
the enzyme is involved in intracellular proteolysis within lysosomes. Increased activity and expression are strongly associated with many pathological processes, including cancers
physiological function
the enzyme is likely to be involved in the immune reaction
physiological function
the enzyme is upregulated and mediates extracellular matrix degradation in colon adenocarcinoma HT29 cells overexpressing Snail (a key regulator of the extracellular matrix degradation). It is hypothesized that cathepsin B controls extracellular matrix proteolysis related to mesenchymal migration in colon cancer cells at early stages of the epithelial-to-mesenchymal transition
physiological function
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the enzyme might play an important role in defending against the pathogenes infection
physiological function
the main functions are the turnover of cellular proteins, the regulation of angiogenesis, invasion, tumor proliferation and immune resistance, neurogenesis, cellular differentiation and tumor response to hypoxia. Cathepsin B plays a protective role by degrading excessive amounts of misfolded protein inside the cell. In humans, the levels of cathepsin B correlates with hippocampal-dependent memory functions and can be increased by physical exercise. The decrease in the rate of neurogenesis in Alzheimer's disease can be secondary to the accumulation of the critical Alzheimer's disease proteins, which can be induced by inhibition of cathepsin B and the consequent the lysosomal dysfunction. The expression of cathepsin B is elevated in many, but not all, cancers
physiological function
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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
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physiological function
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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
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physiological function
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CTSB is a lysosomal cysteine protease primarily involved in the degradation or processing of lysosomal proteins
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physiological function
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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
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additional information
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based on the use of proteinase inhibitors, cell death changes from being principally caspase-dependent to being principally cathepsin B-dependent, overview
additional information
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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
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coordination between transcription factors CmHNF-4 and CmSvp is important in counter-defense gene regulation in insects, overview
additional information
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increased CatB expression in malignant ovarian tumors might be balanced by a corresponding increase in inhibitor CysC, overview
additional information
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relation between cathepsin B activity and the quality of in vitro matured cumulus-oocyte complexes, IVM COCs, and denuded oocytes, overview
additional information
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secreted cathepsin Bs are involved in the pathogenesis of clonorchiasis
additional information
secreted cathepsin Bs are involved in the pathogenesis of clonorchiasis
additional information
secreted cathepsin Bs are involved in the pathogenesis of clonorchiasis
additional information
secreted cathepsin Bs are involved in the pathogenesis of clonorchiasis
additional information
the substrate peptide bond cleaved by cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.15) is determined not by the amino acid contributing the carboxyl group to this bond as in the case of serine proteases but rather by the presence of a neighboring amino acid with a large hydrophobic side chain, active center differences between cathepsins L and B in the S1 binding region, overview
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