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Information on EC 3.4.22.15 - cathepsin L and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.15 cathepsin L
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity
Synonyms
cathepsin l, cathepsin l-like, cathepsin-l, human cathepsin l, cpl-1, cat l, cwp84, cathl, major excreted protein, smcl1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aldrichina grahami cysteine proteinase
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cat L
Cath L
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cath-L
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cathepsin L
cathepsin L isoform CRA-b
splice variant encoding a truncated form of cathepsin L
cathepsin L-A
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enzyme splicing variant
cathepsin L-A1
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enzyme splicing variant
cathepsin L-A2
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enzyme splicing variant
cathepsin L-A3
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enzyme splicing variant
cathepsin L-B
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enzyme splicing variant
cathepsin L-like protein
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cathepsin-L
cathepsin-L T2V
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CATL A IV
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human cathepsin L
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major excreted protein
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MEP
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PDP
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progesterone-dependent protein
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SMCL1
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
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hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
60616-82-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(benzyloxycarbonyl-Phe-Arg)2-R110 + H2O
?
show the reaction diagram
-
rhodamine-labeled substrate
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?
2-aminobenzoic acid-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ala + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
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-
-
-
?
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ala-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Asn-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gln-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
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?
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-His-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ile-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Leu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Leu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
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?
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Arg-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asn-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gln-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Glu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gly-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-His-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ile-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asn + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asp + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
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-
-
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?
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gln + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
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?
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Glu + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gly + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-His + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ile + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Lys + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Met + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Phe-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Phe + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Pro + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ser + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Thr + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Val + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Met-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Phe-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Pro-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ser-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Thr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Trp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Tyr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Val-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Trp-NH2 + H2O
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys + Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + 2-aminobenzoyl-Met-Ile-Ser-Leu-Met + Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + Ser-Ser-Arg-Ile-Trp-NH2
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Phe-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Phe-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Val-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
-
?
48 kDa intermediate of cathepsin D + H2O
34 kDa mature cathepsin D + ?
show the reaction diagram
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ala-3-nitrotyrosineamide
show the reaction diagram
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Gln-3-nitrotyrosineamide
show the reaction diagram
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ser-3-nitrotyrosineamide
show the reaction diagram
-
-
-
-
?
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp + H2O
?
show the reaction diagram
-
-
-
?
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp + H2O
?
show the reaction diagram
-
-
-
?
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp + H2O
?
show the reaction diagram
-
-
-
?
Abz-PRKQLATKAARKSAK-Dnp + H2O
?
show the reaction diagram
-
-
-
?
alpha-casein + H2O
?
show the reaction diagram
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
no activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-citrulline-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-L-citrulline 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methyl-coumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
cathepsin D + H2O
?
show the reaction diagram
-
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
CCAAT-displacement protein/cut homeobox protein + H2O
p90 isoform of CCAAT-displacement protein/cut homeobox protein + p110 isoform of CCAAT-displacement protein/cut homeobox protein + ?
show the reaction diagram
-
-
-
-
?
CCALNNGGGALVPRGSGTAK-(5-carboxyfluorescein)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
chromogranin A + H2O
catestatin fragments + ?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
substrate for cathepsin L mutant A205L
-
-
?
collagen XVIII + H2O
endostatin + ?
show the reaction diagram
-
-
-
-
?
CUX1 transcription factor + H2O
?
show the reaction diagram
-
-
-
-
?
CV-(L-Phe-Arg)2 + H2O
?
show the reaction diagram
-
-
-
?
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
dynamin + H2O
?
show the reaction diagram
CatL is highly reactive toward recombinant dynamin at pH 5.0 and 6.0
-
-
?
E-cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
GABARAP-II protein + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
H2N-Abz-DLVGDVRLAGV-3-nitroYA-CONH2 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H1 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H3 + H2O
?
show the reaction diagram
-
-
-
?
insulin receptor + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor-1 receptor + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-8 precursor + H2O
?
show the reaction diagram
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
LC3-II protein + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-2-(4-methoxynaphthylamide) + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Nipah virus fusion protein + H2O
?
show the reaction diagram
-
proteolytically processed within endosomes by cathepsin L
-
-
?
perforin + H2O
?
show the reaction diagram
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
precursor form 77IL-8 of interleukin-8 + H2O
precursor form 72IL-8 of interleukin-8 + ?
show the reaction diagram
-
cleavage between Arg5 and Ser6
-
?
pro-dipeptidyl peptidase I
?
show the reaction diagram
procathepsin L + H2O
cathepsin L + ?
show the reaction diagram
autoactivation
-
-
?
proheparanase + H2O
active form of heparanase + ?
show the reaction diagram
-
removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
-
-
?
secretory leukocyte protease inhibitor + H2O
?
show the reaction diagram
-
incubation of recombinant secretory leukocyte protease inhibitor with cathepsin L leads to complete loss of activity while encapsulation of recombinant secretory leukocyte protease inhibitor in 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine]-cholesterol liposomes retains 92.6% of its activity after challenge with cathepsin L
-
-
?
soluble type I collagen + H2O
?
show the reaction diagram
kinetics of collagen binding to cathepsin L, overview. The enzyme cleaves after residue Gln24, the recognition sequence is Gly-Phe-Gln-/-Gly-Pro-Pro (corresponding to positions P3 to P3')
-
-
?
thyroglobulin type-1 domain + H2O
?
show the reaction diagram
-
the thyroglobulin type-1 domain is a protein module that occurs in a variety of secreted and membrane proteins and is recognised as a potent inhibitor of cysteine proteases. Nevertheless, at high enzyme and inhibitor concentrations in the mircomolar range cathepsin L degrades thyroglobulin type-1 domain
-
-
?
topoisomerase-IIalpha + H2O
?
show the reaction diagram
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
show the reaction diagram
-
cathepsin L inactivates human trypsinogen, CTSL-induced cleavage of trypsinogen occurs 3 amino acids toward the C-terminus from the cathepsin B activation site and results in a truncated, inactive form of trypsin and an elongated propeptide (trypsinogen activation peptide)
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methyl-coumarin + H2O
?
show the reaction diagram
-
5 microM, pH 6.5, 28°C
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Z-Val-Val-Arg-AMC + H2O
Z-Val-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
a cathepsin L-specific substrate
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
show the reaction diagram
-
-
three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chromogranin A + H2O
catestatin fragments + ?
show the reaction diagram
-
-
-
-
?
collagen XVIII + H2O
endostatin + ?
show the reaction diagram
-
-
-
-
?
CUX1 transcription factor + H2O
?
show the reaction diagram
-
-
-
-
?
E-cadherin + H2O
?
show the reaction diagram
-
-
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
show the reaction diagram
-
recombinant endorepellin is an in vitro substrate. Inhibition of cathepsin L activity in endothelial cells exposed to pro-apoptotic stimuli prevents release of anti-apoptotic C-terminal fragment of endorepellin without modulating the development of apoptosis. Inhibition of caspase-3 activation in endothelial cells concomitantly prevents cathepsin L release, production of anti-apoptotic C-terminal fragment of endorepellin, and the development of paracrine anti-apoptotic activity
-
-
?
GABARAP-II protein + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
histone H1 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H3 + H2O
?
show the reaction diagram
-
-
-
?
interleukin-8 precursor + H2O
?
show the reaction diagram
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
high and low molecular weight kininogen
-
?
LC3-II protein + H2O
?
show the reaction diagram
-
-
-
-
?
Nipah virus fusion protein + H2O
?
show the reaction diagram
-
proteolytically processed within endosomes by cathepsin L
-
-
?
perforin + H2O
?
show the reaction diagram
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
pro-dipeptidyl peptidase I
?
show the reaction diagram
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
proheparanase + H2O
active form of heparanase + ?
show the reaction diagram
-
removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
-
-
?
secretory leukocyte protease inhibitor + H2O
?
show the reaction diagram
-
incubation of recombinant secretory leukocyte protease inhibitor with cathepsin L leads to complete loss of activity while encapsulation of recombinant secretory leukocyte protease inhibitor in 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine]-cholesterol liposomes retains 92.6% of its activity after challenge with cathepsin L
-
-
?
topoisomerase-IIalpha + H2O
?
show the reaction diagram
-
-
-
-
?
trypsinogen + H2O
trypsin + ?
show the reaction diagram
-
cathepsin L inactivates human trypsinogen, CTSL-induced cleavage of trypsinogen occurs 3 amino acids toward the C-terminus from the cathepsin B activation site and results in a truncated, inactive form of trypsin and an elongated propeptide (trypsinogen activation peptide)
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
show the reaction diagram
-
-
three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(((2S,3S)-epoxysuccinyl-(S)-leucyl)amino)-4-guanidinobutane
-
-
(13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oic acid
-
competitive inhibition
(13alpha,17alpha,20S,24Z)-3-oxolanosta-7,24-dien-26-oic acid
-
competitive inhibition
(2-fluorobenzophenone) thiosemicarbazone
-
(2E)-2-(6-bromo-1,1-dioxido-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-bromo-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-bromo-2,3-dihydroquinolin-4(1H)-ylidene)hydrazinecarbothioamide
-
(2E)-2-(6-nitro-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
-
(2E)-2-(7-bromo-3,4-dihydronaphthalen-1(2H)-ylidene)hydrazinecarbothioamide
-
-
(2E)-2-[(2-fluorophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,4,5-trifluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-dichlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3,5-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(3-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[3-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(4-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[6-(propan-2-yloxy)-2,3-dihydro-4H-thiochromen-4-ylidene]hydrazinecarbothioamide
-
(2E)-2-[[3,5-bis(trifluoromethyl)phenyl](3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2E)-[(3E)-28-methoxy-28-oxours-12-en-3-ylidene]acetic acid
-
competitive inhibition
(2R,3R)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
(2S,3S)-3-([(2S)-1-[(8-carbamimidamidooctyl)amino]-4-methyl-1-oxopentan-2-yl]carbamoyl)oxirane-2-carboxylic acid
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(R)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(S)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[biotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R+S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-pipecolyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]-aziridine-2,3-dicarboxylate
-
-
(2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide] 3-[[2-(4-hydroxy-phenyl)-ethyl]-amide]
-
i.e. CAA0225. Significantly inhibits degradation of long-lived proteins in HeLa and Huh-7 cells cultured under nutrient-deprived conditions. CAA0225 effectively inhibits degradation of microtubule-associated protein IA/IB light chain 3-II and gamma-aminobutyric acid (A) receptor-associated protein
(2S,3S+2R,3R)-dibenzyl-1-[desthiobiotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
(2Z)-1-[(12R)-22-amino-12-[(1S)-2-(4-benzoylphenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]-6,13,22-trioxo-17,20-dioxa-7,14-diazadocos-1-yl]-2-[(2E)-3-(1-ethyl-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)prop-2-en-1-ylidene]-3,3-dimethyl-2,3-dihydro-1H-indole-5-sulfonic acid
-
(2Z)-2-[(2-bromophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(2-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(2-fluorophenyl)(phenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromo-2-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromo-4-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3,4,5-tetrafluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,3-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2,6-difluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-chlorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(3-bromophenyl)(2-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[(4-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
(2Z)-2-[[3,5-bis(trifluoromethyl)phenyl](4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(3-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
-
(3-bromo-3'-hydroxybenzophenone) thiosemicarbazone
a slowly reversible inhibitor of cathepsin L
(3-hydroxybenzophenone) thiosemicarbazone
-
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
(3E)-3-(carboxymethylidene)olean-12-en-28-oic acid
-
competitive inhibition
(3E)-3-(carboxymethylidene)urs-12-en-28-oic acid
-
competitive inhibition
(4-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
-
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
selective towards cathepsin L over cathepsin B
(N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide)
-
(R)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
R-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
(S)-2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarboxylate
-
(S)-S-2-(2-ethylphenylamino)-2-oxoethyl 2-(2-(tert-butoxycarbonylamino)-3-(1H-indol-3-yl)propanoyl)hydrazinecarbothioate
S-enantiomer, thiol ester containing a diacyl hydrazine functionality and one stereogenic center
1,3,5-trisbenzoylbenzene thiosemicarbazone
-
1,3-bis(2-fluorobenzoyl)-5-bromobenzene thiosemicarbazone
molecular docking in the active site
1,3-bis(3-bromobenzoyl)-5-bromobenzene thiosemicarbazone
-
1,3-bis(3-bromobenzoyl)-5-hydroxybenzene thiosemicarbazone
-
1,3-bis(3-hydroxybenzoyl)-5-bromobenzene thiosemicarbazone
-
1,3-bis(3-methylbenzoyl)benzene thisosemicarbazone
-
1,3-bis(4-bromobenzoyl)benzene bis-thiosemicarbazone
-
1,3-bis(4-bromobenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-fluorobenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-hydroxybenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-isopropoxybenzoyl)benzene thiosemicarbazone
-
1,3-bis(4-methoxybenzoyl)benzene thiosemicarbazone
-
1,3-dihydro-pyrrolo[3,4-b]quinoline-2-carbonitrile
-
IC50: 0.00045 mM
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
1-cyano-3-azetidinyl cyclohexylmethyl ether
-
IC50: 0.00001 mM
1-cyanoazetidine
-
IC50: 0.00043 mM
1-cyanopyrrolidine
-
IC50: 0.004 mM
1-naphthalenesulfonyl-Ile-Trp-aldehyde
1-nathalenesulfonyl-Ile-Trp-CHO
-
treatment of cells results in suppression of cellular proliferation and the induction of a cell death with no detecable caspase-3 activation or DNA fragmentation. Cell death is associated with increased accumulation of cathepsin D, cellular vacuolization, expression of the mannose 6-phosphate recepto, and the autophagy marker LC-II
2,6-dimethoxy-4-[4-(4-phenoxyphenyl)-5-phenyl-1H-imidazol-2-yl]phenol
-
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
-
2-(1,3-benzodioxol-5-yl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylate
-
unreactive to transesterification by cysteine and dithiothreitol nucleophiles. Inhibitor remains intact for greater than 24 h when incubated with cathepsin L under stoichiometric conditions, and in the presence of assay buffer
2-(3,4-dimethoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(4-methoxyphenyl)-4-[8-[2-(4-methoxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
-
2-(4-methoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
-
2-(acetylamino)-N-[4-(6-[[2-(acetylamino)benzoyl]amino]-1H-benzimidazol-2-yl)phenyl]benzamide
-
2-(furan-2-yl)-4-[8-[2-(furan-2-yl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
-
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(1,4-dioxaspiro[4.5]dec-8-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(2-cyclopentylethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(6,8-dioxaspiro[3.5]non-7-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[(cyclohexylmethyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-difluorocyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[[(4,4-dimethylcyclohexyl)methyl]amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
-
2-cyano-4-[[1-(2-hydroxyethyl)piperidin-4-yl]methoxy]-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(2-phenylethyl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-(4,5-dimethoxybiphenyl-2-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-(piperidin-4-ylmethoxy)-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[4.5]dec-8-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[(spiro[3.5]non-7-ylmethyl)amino]-6-[(2,2,6,6-tetramethylpiperidin-4-yl)oxy]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-methyl-4-[[1-(1-methylethyl)piperidin-4-yl]methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
2-[bis(3-bromophenyl)methylidene]-N-ethylhydrazinecarbothioamide
-
-
2-[bis(3-bromophenyl)methylidene]-N-phenylhydrazinecarbothioamide
-
-
2-[bis(3-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[bis(4-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[bis(4-fluorophenyl)methylidene]hydrazinecarbothioamide
-
-
2-[cyclohexyl(methyl)amino]-4H-3,1-benzothiazin-4-one
-
selective towards cathepsin L over cathepsin G, chymotrypsin, trypsin, human angiotensin-converting enzyme, human leukocyte elastase, acetylcholinesterase
2RS,3RS)-2-benzyl-3-ethyl-1-[N-(benzyloxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
3-(benzyloxy)-1-cyanoazetidine
-
IC50: 0.00001 mM
3-(hydroxyimino)masticadienoic acid
-
competitive inhibition
3-(hydroxyimino)oleanolic acid
-
competitive inhibition
3-benzoylbenzhydrol thiosemicarbazone
-
3-chloro-N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
3-epiursolic acid
-
competitive inhibition
3-hydroxyolean-12-en-28-oic acid
-
competitive inhibition
3-hydroxyurs-12-en-28-oic acid
-
competitive inhibition
3-oxoolean-12-en-28-oic acid
-
competitive inhibition
3-oxours-12-en-28-oic acid
-
competitive inhibition
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
-
IC50: 0.00015 mM
3-[(E)-(4-[[4-([2-[([[3-cyclohexyl-N-(morpholin-4-ylcarbonyl)-L-alanyl]amino][(6-[(2Z)-2-[(2E,4E,6Z)-7-(1-ethyl-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)hepta-2,4,6-trien-1-ylidene]-3,3-dimethyl-5-sulfo-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]acetyl)amino]ethyl]amino)-4-oxobutyl](methyl)amino]phenyl)diazenyl]-7-(diethylamino)-5-phenylphenazin-5-ium
-
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
-
3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4,4'-[methanediylbis(1H-benzimidazole-5,2-diyl)]dianiline
-
4-(4-[8-[2-(4-carboxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)benzoic acid
-
4-(4-[8-[2-(4-hydroxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)phenol
-
4-amino-N-(4-[6-[(4-aminobenzoyl)amino]-1H-benzimidazol-2-yl]phenyl)benzamide
-
4-bromophenyl (1E,3S)-3-([N-[(benzyloxy)carbonyl]-L-phenylalanyl]amino)-5-methylhex-1-ene-1-sulfonate
i.e. KD-1
4-bromophenyl (S,E)-3-((S)-2-((((4-ethynylbenzyl)oxy)carbonyl)amino)-3-phenylpropanamido)-5-methylhex-1-ene-1-sulfonate
i.e. KDP-1, in vivo inhibition of cathepsin L. Inhibition of cathepsin L compared to other cathepsins, overview
4-[(1-acetylpiperidin-4-yl)methoxy]-2-cyano-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
-
4-[(E)-benzylideneamino]-N-[4-[6-([4-[(E)-benzylideneamino]benzoyl]amino)-1H-benzimidazol-2-yl]phenyl]benzamide
-
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
4-[4-(5,5-dioxidodibenzo[b,d]thiophen-2-yl)-5-phenyl-1H-imidazol-2-yl]-2,6-dimethoxyphenol
-
4-[5-(4-[[2-(4-aminophenyl)-1H-benzimidazol-6-yl]oxy]phenoxy)-1H-benzimidazol-2-yl]aniline
-
4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
-
4-[8-(2,4-diphenyl-1H-imidazol-5-yl)dibenzo[b,d]furan-2-yl]-2,5-diphenyl-1H-imidazole)
-
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]benzoic acid
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
-
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(2,4,5-trimethoxyphenyl)-1H-imidazole
-
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(3,4,5-trimethoxyphenyl)-1H-imidazole
-
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclooctylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(2-piperidin-1-ylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(3-cyclohexylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(4,4-dimethylpentyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P2 moieties
6-[[4-(1-acetyl-1,2,3,6-tetrahydropyridin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(1-acetylpiperidin-4-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
6-[[4-(4-acetyl-1,4-diazepan-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)-3-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
-
7-(2-cyclohexylethyl)-6-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-(phenoxymethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(phenylamino)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[(pyridin-2-ylsulfanyl)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
7-(2-cyclohexylethyl)-6-[[methyl(phenyl)amino]methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
acetyl-Leu-Leu-Tyr-CHN2
-
-
alpha2 cysteine-proteinase inhibitor
-
-
-
azepanone
-
-
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-naphthylen-2-yl)amide
-
-
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-phenyl-ethyl)amide
-
-
benzophenone thiosemicarbazone
-
benzoylbenzophenone thiosemicarbazone
molecular docking in the active site
benzyl 1-cyano-3-pyrrolidinylcarbamate
-
IC50: 0.000054 mM
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxo-3-(1,1':4',1''-terphenyl-4-yl)propan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(2'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(3'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(4'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-aminobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(3'-chlorobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyl [(2S)-3-(biphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
-
benzyloxycarbonyl-iodophenylalanine-Ala-CHN2
-
-
benzyloxycarbonyl-iodotyrosine-Ala-CHN2
-
-
benzyloxycarbonyl-L-Phe-L-Phe-fluoromethylketone
benzyloxycarbonyl-Leu-homophenylalanine-CHN2
-
-
benzyloxycarbonyl-Leu-Leu-Phe-CHN2
-
-
benzyloxycarbonyl-Leu-Leu-Tyr-CHN2
-
-
benzyloxycarbonyl-Leu-Met-CHN2
-
-
benzyloxycarbonyl-Leu-Trp-CHN2
-
-
benzyloxycarbonyl-Leu-Tyr-CHN2
-
-
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Phe-Ala-CNH2
-
-
benzyloxycarbonyl-Phe-Phe fluoromethylketone
-
cell-permeable irreversible cathepsin inhibitor
Benzyloxycarbonyl-Phe-Phe-CHN2
-
-
benzyloxycarbonyl-Phe-Phe-fluoromethyl ketone
-
benzyloxycarbonyl-Phe-Tyr-(tert-butyl)-diazomethylketone
benzyloxycarbonyl-Phe-Tyr-CHO
-
-
benzyloxycarbonyl-Tyr-Ala-CHN2
-
-
biphenyl-4-yl-acetylasparagine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylcysteine-D-Arg-Abu-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Arg-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylcysteine-D-Arg-Trp-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylcysteine-D-Arg-Tyr-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Leu-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Met-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
the inhibitor shows a 310fold and 210fold selectivity for cathepsin L over cathepsin K and B, respectively
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(3-phenylpropyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(benzyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-Phe-NH2
-
biphenyl-4-yl-acetylmethylcysteine-D-Orn-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylmethylcysteine-Gly-Phe-Phe-NH2
-
biphenyl-4-yl-acetylnorvaline-D-Arg-Phe-N-(2-phenylethyl)amide
-
biphenyl-4-yl-acetylserine-D-Arg-Phe-Phe-NH2
-
biphenylacetyl-(N6-biphenylacetyl)-Lys-D-Arg-Tyr-N-phenylethyl
-
biphenylacetyl-(N6-biphenylacetyl)Lys-D-Arg-Phe-N-phenylethyl
-
biphenylacetyl-MCys-D-Arg-Phe-N-phenylethyl
-
bis[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methanone
-
CA-074Me
-
-
CAA0225
-
i.e. (2S,3S)-oxirane-2,3-dicarboxylic acid 2-[((S)-1-benzylcarbamoyl-2-phenyl-ethyl)-amide]3-[[2-(4-hydroxy-phenyl)-ethyl]-amide], a cathepsin L-specific inhibitor
cathepsin K propeptide
-
-
-
cathepsin L inhibitor 1
-
cathepsin L propeptide
-
-
-
cathepsin S propeptide
-
-
-
chagasin
-
-
-
chagasin mutant delta T31-T32
-
-
-
chagasin mutant P30A
-
-
-
chagasin mutant T31A
-
-
-
chagasin mutant T31A/T32A
-
-
-
chagasin mutant T31S
-
-
-
chagasin mutant T31V
-
-
-
chagasin mutant T31Y
-
-
-
chagasin mutant T32A
-
-
-
chagasin mutant T32S
-
-
-
chagasin mutant T32V
-
-
-
chagasin mutant T32Y
-
-
-
chagasin mutant W93A
-
-
-
Chloroquine
-
chloroquine inhibits the infection with live Nipah virus and Hendra virus at a concentration of 1 microM in vitro. The mechanism for the antiviral action likely is the inhibition of cathepsin L, which is essential for the processing of the viral fusion glycoprotein and the maturation of newly budding virions
CID 16725315
-
2% inhibition at 0.025 mM
CID 23631927
-
38% inhibition at 0.025 mM, sub-nanomolar slow-binding, reversible inhibitor of human cathepsin L with cathepsin L/B selectivity of above 700fold that blocks SARS-CoV and Ebola pseudotype virus entry in human cells
CLICK148
-
-
CLIK-148
CLIK-181
cathepsin L-specific inhibitor
CLIK148
CLIK195
-
complete inhibition at 0.01 mM
cystatin
-
from chicken, activity with benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
cystatin A
-
-
-
cystatin B
-
cystatin C
-
-
-
cystatin D
-
-
-
cystatin F
-
-
-
cystatin M/E
-
-
-
diethyl-cyanamide
-
IC50 is above 0.1 mM
E64
inhibition of gelatinolytic activity
endopin 2
-
enodgenous inhibitor, present in pituitary gland
-
endopin 2C
-
endopin 2C inactivaties cathepsin L by binding to the enzyme, after dissociation from cathepsin L its activity is recovered within 60 min
-
Ep-460
-
-
Ep-475
ethanesulfonothioate
-
-
fragment p41 of major histocompatibility complex class II-associated invariant chain
inhibitory to human cathepsin V, cathepsin L, cathepsin K, cathepsin F with Ki values in the low nanomolar range. Ki values are sufficiently low to ensure complex formation at physiological concentrations. Regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation
-
glucose
-
high concentrations
HgCl2
-
-
JPM-565
-
cathepsin L irreversible binding
JPM-OEt
-
cathepsin L irreversible binding
KAPR-acetyl-K-QLATKAARKSAPA
-
KAPRKQLAT-acetyl-K-AARKSAPA
-
KAPRKQLATKAAR-dimethyl-K-SAPA
-
KAPRKQLATKAARKSAPA
-
kininogen domain 3
-
-
-
L-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane
E-64
L-trans-epoxysuccinylleucylamido-(4-guanidino)butane
i.e. E-64, complete inhibition at 0.26 mM
Leu-Leu-Tyr-CHN2
-
-
leupeptin
LFLRL
-
0.05 mM, 78% inhibition
LFLTR-NH2
-
IC50: 0.0008 mM
LKFTF
-
0.05 mM, 24% inhibition; 0.05 mM, 32% inhibition
LKFTR
-
0.05 mM, 78% inhibition
LKLFF
-
0.05 mM, 42% inhibition
LKLFW
-
0.05 mM, 22% inhibition
LKLLW
-
0.05 mM, 75% inhibition
LLFLW
-
0.05 mM, 52% inhibition
LLFRW
-
0.05 mM, 52% inhibition
LLLLR
-
0.05 mM, 62% inhibition
LLLLW
-
0.05 mM, 37% inhibition
LLLRW
-
0.05 mM, 83% inhibition
LLLTB
-
0.05 mM, 58% inhibition
LLLTL
-
0.05 mM, 67% inhibition
LLLTR-NH2
-
IC50: 0.0005 mM
LLLTW
-
0.05 mM, 62% inhibition
LLYLW
-
0.05 mM, 47% inhibition
LLYTB
-
0.05 mM, 25% inhibition
LLYTR
-
0.05 mM, 62% inhibition
LLYTW
-
0.05 mM, 30% inhibition
low-MW cysteine proteinase inhibitor
-
-
-
LRFTF
-
0.05 mM, 25% inhibition
LRLLW
-
0.05 mM, 73% inhibition
LWFFW
-
0.05 mM, 61% inhibition
LWFRQ
-
0.05 mM, 20% inhibition
LWFRW
-
0.05 mM, 20% inhibition
LWLFL
-
0.05 mM, 73% inhibition
LWLFW
-
0.05 mM, 31% inhibition
LWLLW
-
0.05 mM, 52% inhibition
MDL28170
-
-
methyl (13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oate
-
competitive inhibition
methyl (3Z,13alpha,17alpha,20S,24Z)-3-(hydroxyimino)lanosta-7,24-dien-26-oate
-
competitive inhibition
methyl 5-acetyloxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
furanquinone from Paulownia tomentosa stem, inhibitory to both cathepsin L and cathepsin K
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
-
furanquinone from Paulownia tomentosa stem, inhibitory to both cathepsin L and cathepsin K
N-(1-cyano-3-pyrrolidinyl)benzamide
-
IC50: 0.00175 mM
N-(1-cyano-3-pyrrolidinyl)benzenesulfonamide
-
IC50: 0.00008 mM
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
-
IC50: 0.00085 mM
N-(1-cyanopyrrolidin-3-yl)benzenesulfonamide
-
-
N-(2,6-dimethylbenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(2-chloro-5-nitrobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(3-phenylpropanoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-(4-biphenylacetyl)-S-methylcysteine-(D)-Arg-Phe-beta-phenethylamide
-
also called Cat L inhibitor 7, specific inhibitor
N-(4-bromobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(4-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)propanamide
-
pyrrolopyrimidine inhibitor by modification of the P3 moieties
N-(biphenyl-4-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(cyclopent-1-en-1-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(pentafluorobenzoyl)-L-phenylalanyl-L-lysinamide
-
-
N-(piperidin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-(pyridin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
-
N-acetyl-Leu-Leumethional
inhibition of gelatinolytic activity
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-benzyl-2-[bis(3-bromophenyl)methylidene]hydrazinecarbothioamide
-
-
N-benzyloxycarbonyl-Phe-Phe-fluoromethylketone
-
-
N-benzyloxycarbonyl-phenylalanyl-phenylalanine-fluoromethyl ketone
an irreversible cathepsin inhibitor
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
-
IC50: 0.023 mM
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
-
IC50: 0.0115 mM
N-[(1-cyano-3-azetidinyl)methyl]benzamide
-
IC50: 0.00065 mM
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
-
IC50: 0.00005 mM
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
-
IC50: 0.000006 mM
N-[(1-cyano-3-pyrrolidinyl)methyl]benzenesulfonamide
-
IC50: 0.00035 mM
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
-
N-[(2R)-2-[(2-amino-2-oxoethyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[(3-aminopropyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(3a,7a-dihydro-1H-indol-3-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(propan-2-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-[(2-carbamimidamidoethyl)amino]acetyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(2S)-1-(1H-indol-3-yl)-3-oxopropan-2-yl]-N2-(naphthalen-1-ylsulfonyl)-L-isoleucinamide
-
-
N-[(2S)-1-(3-chlorophenyl)-3-[(cyanomethyl)amino]but-3-en-2-yl]benzamide
-
-
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1,3-dimethyl-1H-pyrazole-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1,3-dimethyl-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-1-methyl-3-(propan-2-yl)-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,3-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,4-dimethyl-1,3-thiazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethyl-1,3-oxazole-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2,5-dimethylthiophene-3-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-2-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3,5-dimethylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3,7-dimethylnaphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3-ethyl-1-methyl-1H-pyrazole-5-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-3-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-4-methylbenzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]-5,6,7,8-tetrahydronaphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cycloheptanecarboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cyclohex-1-ene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]cyclohexanecarboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]naphthalene-1-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]quinoline-4-carboxamide
-
pH and temperature not specified in the publication
N-[(2S)-4-methyl-1-oxo-1-[[(4S)-3-oxo-1-(pyridin-2-ylsulfonyl)azepan-4-yl]amino]pentan-2-yl]-1-benzofuran-2-carboxamide
-
-
N-[(4'-carboxy-2,2'-bipyridin-4-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(6-aminopyridin-3-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-3-(1H-indazol-1-yl)-L-alanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-3-(1H-indol-1-yl)-L-alanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-4-(thiophen-2-yl)-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N-[(benzyloxy)carbonyl]-L-phenylalanyl-3-(1H-imidazol-1-yl)-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-4-amino-L-phenylalaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-hydroxy-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-argininamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-leucinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-methioninamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-ornithinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-valinamide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N6-methyl-L-lysinamide
-
-
N-[(benzyloxy)carbonyl]-L-tryptophyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N-[(benzyloxy)carbonyl]-L-tyrosyl-L-lysinamide
-
-
N-[3-(4-hydroxyphenyl)propanoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[3-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-2,2-diphenylacetamide
-
N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide
-
N-[4-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(dimethylamino)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[4-(trifluoromethyl)benzoyl]-L-phenylalanyl-L-lysinamide
-
-
N-[6-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]hexanoyl]-L-histidyl-L-threonyl-N-[(2R)-1-(benzylsulfanyl)-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]-2,3,4,5,6-pentafluoro-L-phenylalaninamide
-
N2-acetyl-L-arginyl-L-lysyl-L-leucyl-L-leucyl-L-tryptophanamide
-
potent inhibitor
N2-[(benzyloxy)carbonyl]-L-arginyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-L-lysyl-N-[4-([[(5-methyl-7-oxo-7,8-dihydronaphthalen-2-yl)carbamoyl]oxy]methyl)phenyl]-L-lysinamide
-
N2-[(benzyloxy)carbonyl]-L-ornithyl-N-[(3S)-7-amino-1-[(2,6-dimethylbenzoyl)oxy]-2-oxoheptan-3-yl]-L-phenylalaninamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-N-[(3S)-1-cyanopyrrolidin-3-yl]-L-leucinamide
-
-
Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-3-chloro-N-(cyanomethyl)-L-phenylalaninamide
-
pH and temperature not specified in the publication
Nalpha-[(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)carbonyl]-N-(cyanomethyl)-3-methyl-L-phenylalaninamide
-
pH and temperature not specified in the publication
Nalpha-[(benzyloxy)carbonyl]-N-[(1R)-1,2-diamino-2-oxoethyl]-L-phenylalaninamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3S)-7-[(6-[(2Z)-3,3-dimethyl-5-sulfo-2-[(2E,4E)-5-(1,3,3-trimethyl-5-sulfo-2,3-dihydro-1H-indol-2-yl)penta-2,4-dien-1-ylidene]-2,3-dihydro-1H-indol-1-yl]hexanoyl)amino]-2-oxo-1-(2,3,5,6-tetrafluoro-4-[[2-([[1-(2-[(3E)-3-(5-sulfo-2,3-dihydro-1H-indolium-1-ylidene)-6-(5-sulfo-2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]benzene-1-sulfonyl)piperidin-4-yl]carbonyl]amino)ethyl]carbamoyl]phenoxy)heptan-3-yl]-L-phenylalaninamide
-
naphthalene-2-carboxylic acid ((S)-2-naphthalen-2-yl-1-[(S)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]ethyl)amide
-
-
naphthoic-1-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
efficient cathepsin L inhibitor
ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
p41 fragment
-
-
-
p41-fragment-human
64 residues present in the p41 form of the human major histocompatibility complex II (MHCII)-associated invariant chain
-
P41icf
-
synthesis and NMR structure of the potent inhibitor
-
Phe-Tyr-(OBut)-COCHO
potent, reversible, synthetic peptidyl inhibitor of cathepsin L
Phe-Tyr-(tert-Bu)-diazomethylketone
irreversible inhibitor that can inactivate cathepsin L at micromolar concentrations
phenylmethanesulfonyl fluoride
-
-
Protein C inhibitor
-
inhibits cathepsin L with an inhibition rate (k2) of 30000 0 M-1 s-1
-
quinoline-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
quinoline-8-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
RFLRW
-
0.05 mM, 21% inhibition
RFLYR
-
0.05 mM, 64% inhibition
RKLFL
-
0.05 mM, 79% inhibition
RKLLW-NH2
-
IC50: 0.0006 mM
RKLWD-NH2
-
IC50: 0.014 mM
RKLWF
-
0.05 mM, 52% inhibition
RKLWL-NH2
-
IC50: 0.0008 mM
RKLWV
-
0.05 mM, 41% inhibition
RLLLW
-
0.05 mM, 75% inhibition
RLLYW
-
0.05 mM, 29% inhibition
RRFYV
-
0.05 mM, 24% inhibition
RRLTW
-
0.05 mM, 38% inhibition
RRYLB
-
0.05 mM, 33% inhibition
RWLTL
-
0.05 mM, 61% inhibition
RWLYL
-
0.05 mM, 65% inhibition
S-(2-oxo-1-phenylpyrrolidin-3-yl) 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
-
S-[2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
-
-
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropanoyl]hydrazinecarbothioate
-
-
serpin B3
-
about 35% inhibition at 7.5 nM, the presence of heparin accelerates inhibition of cathepsin L by serpin B3 (4.1fold increase in rate of inhibition)
-
serpin B4
-
about 70% inhibition at 100 nM, the presence of 50 nM heparin accelerates inhibition of cathepsin L by serpin B4 (4.1fold increase in rate of inhibition)
-
soluble type I collagen
inhibitory against cathepsin L, Ki is 0.36 mg/ml, collagen is also a substrate for the enzyme
-
Stefin A
-
-
-
Stefin B
a potent cathepsin L inhibitor, colorectal carcinoma cells reveal only very faint amounts of immunolabeled stefin B within their nuclei, while it is prominently present within the cytoplasm of Caco-2 and SW-620 cells, and mostly associated with the cytoplasmic face of vesicles in HCT-116 cells
-
tert-butyloxycarbonyl-Lys(epsilon-9-fluorenylmethoxycarbonyl)-Leu-Tyr-CHN2
-
-
tert-butyloxycarbonyl-Lys-Leu-Tyr-CHN2
-
-
tert-butyloxycarbonyl-Val-Lys(epsilon-benzyloxycarbonyl)-Leu-Tyr-CHN2
-
-
testican-1
-
strong competitive inhibitor, inhibition is independent of its chondroitin sulfate chains and is effective at both pH 5.5 and pH 7.2, does not inhibit the structurally related lysosomal cysteine protease cathepsin B
-
Tg1 domain of testican-1
-
-
-
thyroglobulin type-1 domain
-
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
YFLLR
-
0.05 mM, 30% inhibition
YFLTF
-
0.05 mM, 29% inhibition
YKLLR
-
0.05 mM, 72% inhibition
YLLFW
-
0.05 mM, 37% inhibition
YLYLF
-
0.05 mM, 40% inhibition
YWFTF
-
0.05 mM, 43% inhibition
YWLLR
-
0.05 mM, 73% inhibition
YWYYL
-
0.05 mM, 20% inhibition
YYLLR
-
0.05 mM, 56% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7beta-hydroxycholesterol
-
significantly enhances cathepsin L in cells from healthy donors but not in cells from coronary artery disease patients
dibutyryl-cAMP
-
treatment of cells for identification of formerly N-linked glycopeptides. Treatment results in upregulation of follistatin-related protein 1, cathepsin L, and neuroblastoma suppressor of tumorigenicity, and the downregulation of tenascin C and cationin-dependent mannose-6-phosphate receptor
protegrin-3
-
a porcine cathelicidin, molecular weight 11.7 kDa. The cathelin-like domain efficiently activates human cathepsin L. Partial deletion of the L2 loop of cathelin-like domain, a structurally equivalent region important ininteraction of cystatins with proteases, significantly decreases its activating effect on cathepsin L. Proposal of a complex model based on this functional loop, with the cathelin-like domain fitting into the active cleft of the enzyme in an analogous way as cystatin B does
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00016
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00071
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00075
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0025
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0022
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0011
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0023
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00035
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00023
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0026
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.005
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.035
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0085
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0097
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0096
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0034
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00017
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00095
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00018
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0002
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00027
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0017
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00017
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0002
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0004
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00023
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00017
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00019
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00019
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00072
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00024
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00014
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00013
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00035
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00015
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00013
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00023
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0015
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0038
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00056
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0055
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00026
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00021
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00017
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00017
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00047
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.006
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0011
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00055
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00028
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0006
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0028
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00026
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0067
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.012
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0049
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0038
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00042
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00059
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0034
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.00153
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
0.00104
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
0.00027
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
0.00016
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp
pH and temperature not specified in the publication
0.000037
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp
pH and temperature not specified in the publication
0.000073
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp
pH and temperature not specified in the publication
0.000063
Abz-PRKQLATKAARKSAK-Dnp
pH and temperature not specified in the publication
0.014 - 0.081
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
0.0013 - 0.0098
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.0011 - 0.0024
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
0.0011 - 0.0087
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.3
2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.8
2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.5
2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.8
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4
2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.2
2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.1
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.9
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.2
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.7
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.5
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.1
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.7
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6.3
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.8
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.9
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.4
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
7.3
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.9
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.1
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.3
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.2
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.1
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.8
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.7
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.4
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4.6
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.2
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
5.5
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.1
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.2
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.9
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.6
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
3.1
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.1
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.5
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.3
2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.5
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
4
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
13.5
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.2
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
0.4
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
1.9
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
7.8
2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
6.4
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
2.1
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
50 mM Na-acetate, 100 mM NaCl, 2.5 mM EDTA, pH 5.5, 37°C
17.4
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
27
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
5.01
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
0.49
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp
pH and temperature not specified in the publication
0.37
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp
pH and temperature not specified in the publication
0.51
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp
pH and temperature not specified in the publication
0.46
Abz-PRKQLATKAARKSAK-Dnp
pH and temperature not specified in the publication
0.01 - 0.5
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
17.6 - 27.2
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
10 - 50
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
5.4 - 46
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11400
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
26000
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
18600
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2
-
in 50 mM Mes buffer (pH 6.0) containing 5 mM dithiothreitol, at 37°C
2900
Abz-PR-acetyl-K-QLATKAARKSAK-Dnp
pH and temperature not specified in the publication
6700
Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp
pH and temperature not specified in the publication
5300
Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp
pH and temperature not specified in the publication
6100
Abz-PRKQLATKAARKSAK-Dnp
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
(2R,3R)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0048
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0059
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0048
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0059
(2R,3R)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0529
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.026
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0101
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0101
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0187
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
0.0178
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-isonipecotyl]aziridine-2,3-dicarboxylic acid
-
-
0.0178
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0153
(2S,3S)-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylic acid
-
-
0.0159
(2S,3S)-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylic acid
-
-
0.0064
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(R)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.000013
(2S,3S)-dibenzyl-1-[1-[N-(tert-butoxycarbonyl)-(S)-leucyl]-(S)-aziridine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0014
(2S,3S)-dibenzyl-1-[biotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
0.0042
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0042
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.004
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-leucyl-(S)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0216
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0147
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(R)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0038
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0044
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.006
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-prolyl]-aziridine-2,3-dicarboxylate
-
-
0.0038
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-azetidine-2-carbonyl]aziridine-2,3-dicarboxylate
-
-
0.0044
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0152
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(R)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0166
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-(S)-phenylalanyl-(S)-alanyl]aziridine-2,3-dicarboxylate
-
-
0.0058
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0071
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0058
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(R+S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0064
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-pipecolyl]-aziridine-2,3-dicarboxylate
-
-
0.0158
(2S,3S)-dibenzyl-1-[N-(tert-butoxycarbonyl)-glycyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0024
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(R)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0024
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-nipecotyl]aziridine-2,3-dicarboxylate
-
-
0.0077
(2S,3S)-diethyl-1-[N-(tert-butoxycarbonyl)-(S)-leucyl-(S)-prolyl]aziridine-2,3-dicarboxylate
-
-
0.0079
(2S,3S+2R,3R)-dibenzyl-1-[desthiobiotinyl-6-aminohexanoyl]-aziridine-2,3-dicarboxylate
-
-
0.0053
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
23°C, pH 6.0
0.023
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([2-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.002
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0023
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-methyl-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0025
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([3-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.012
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-3-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(pyridin-4-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.013
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[(thiophen-2-ylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([4-[methyl(methylsulfonyl)amino]phenyl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(methylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.031
1,4-anhydro-3,5,6-trideoxy-3-([(2S)-3-(1-methylcyclopentyl)-2-[([6-[(phenylsulfonyl)amino]pyridin-3-yl]carbonyl)amino]propanoyl]amino)-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.016
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-([[4-([[(dimethylamino)methyl]sulfonyl]amino)phenyl]carbonyl]amino)-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.029
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([2-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0078
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-fluoro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0072
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([3-methoxy-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.017
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[([4-[(ethylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.016
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2,4-dimethyl-1,3-thiazol-5-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(2-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0078
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.014
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(3-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0059
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-fluorophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.011
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-2-[[(4-[[(4-methoxyphenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-(methylsulfamoyl)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0091
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-([[4-([[4-(1-methylethyl)-1,3-thiazol-2-yl]sulfonyl]amino)phenyl]carbonyl]amino)propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.027
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-sulfamoylphenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.024
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methyl-1H-imidazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(1-methylethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2,2,2-trifluoroethyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0084
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(2-methylphenyl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.027
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0087
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(4-methylpyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.017
1,4-anhydro-3,5,6-trideoxy-3-[[(2S)-3-(1-methylcyclopentyl)-2-[[(4-[[(5-methyl-1,3-thiazol-2-yl)sulfonyl]amino]phenyl)carbonyl]amino]propanoyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.01
1,4-anhydro-3,5,6-trideoxy-3-[[4-methyl-N-(thiophen-3-ylcarbonyl)-L-leucyl]amino]-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.00097
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0011
1,4-anhydro-3-[[(2S)-2-[([3-chloro-4-[(phenylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.015
1,4-anhydro-3-[[(2S)-2-[([4-[(benzylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.021
1,4-anhydro-3-[[(2S)-2-[([4-[(butylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.012
1,4-anhydro-3-[[(2S)-2-[([4-[(cyclopropylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.023
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-chloropyridin-3-yl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0085
1,4-anhydro-3-[[(2S)-2-[[(4-[[(2-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0068
1,4-anhydro-3-[[(2S)-2-[[(4-[[(3-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0079
1,4-anhydro-3-[[(2S)-2-[[(4-[[(4-cyanophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.064
1,4-anhydro-3-[[(2S)-2-[[(4-[[(cyclohexylmethyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.00923
3-(hydroxyimino)masticadienoic acid
-
at pH 5.5 and 37°C
0.002
3-(hydroxyimino)oleanolic acid
-
at pH 5.5 and 37°C
0.0195
3-epiursolic acid
-
at pH 5.5 and 37°C
0.0095
3-[[(2S)-2-[([3-acetyl-4-[(methylsulfonyl)amino]phenyl]carbonyl)amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0091
3-[[(2S)-2-[[(4-[[(4-aminophenyl)sulfonyl]amino]phenyl)carbonyl]amino]-3-(1-methylcyclopentyl)propanoyl]amino]-1,4-anhydro-3,5,6-trideoxy-L-glycero-hex-2-ulose
-
100 mM sodium acetate, 1 mM EDTA, 1 mM DTT, 0.1% PEG 4000, pH 5.5
0.0000022
azepanone
-
-
0.00000057
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-naphthylen-2-yl)amide
-
-
0.0000017
benzofuran-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-2-phenyl-ethyl)amide
-
-
0.0026
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxo-3-(1,1':4',1''-terphenyl-4-yl)propan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.023
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(2'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0025
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(3'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0017
benzyl [(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(4'-methylbiphenyl-4-yl)-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0018
benzyl [(2S)-3-(3'-aminobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0017
benzyl [(2S)-3-(3'-chlorobiphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0024
benzyl [(2S)-3-(biphenyl-4-yl)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]carbamate
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.03
biphenyl-4-yl-acetylasparagine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.00021
biphenyl-4-yl-acetylcysteine-D-Arg-Abu-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.0039
biphenyl-4-yl-acetylcysteine-D-Arg-Arg-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.081
biphenyl-4-yl-acetylcysteine-D-Arg-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000021
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00017
biphenyl-4-yl-acetylcysteine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.000067
biphenyl-4-yl-acetylcysteine-D-Arg-Trp-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000045
biphenyl-4-yl-acetylcysteine-D-Arg-Tyr-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00027
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Leu-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00024
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Met-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.000019
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00021
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(3-phenylpropyl)amide
pH 5.5, 25°C
0.0066
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-N-(benzyl)amide
pH 5.5, 25°C
0.00007
biphenyl-4-yl-acetylmethylcysteine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.0002
biphenyl-4-yl-acetylmethylcysteine-D-Orn-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.00093
biphenyl-4-yl-acetylmethylcysteine-Gly-Phe-Phe-NH2
pH 5.5, 25°C
0.00049
biphenyl-4-yl-acetylnorvaline-D-Arg-Phe-N-(2-phenylethyl)amide
pH 5.5, 25°C
0.07
biphenyl-4-yl-acetylserine-D-Arg-Phe-Phe-NH2
pH 5.5, 25°C
0.000023
biphenylacetyl-(N6-biphenylacetyl)-Lys-D-Arg-Tyr-N-phenylethyl
pH and temperature not specified in the publication
0.000511
biphenylacetyl-(N6-biphenylacetyl)Lys-D-Arg-Phe-N-phenylethyl
pH and temperature not specified in the publication
0.000019
biphenylacetyl-MCys-D-Arg-Phe-N-phenylethyl
pH and temperature not specified in the publication
0.0000026
cathepsin K propeptide
-
pH 5.5, room temperature
-
0.00000012
cathepsin L propeptide
-
pH 5.5, room temperature
-
0.00000046
cathepsin S propeptide
-
pH 5.5, room temperature
-
0.0000000073
chagasin
-
-
-
0.0000022
chagasin mutant deltaT31-T32
-
-
-
0.000000045
chagasin mutant P30A
-
-
-
0.0000000039
chagasin mutant T31A
-
-
-
0.0000000018
chagasin mutant T31A/T32A
-
-
-
0.0000000049
chagasin mutant T31S
-
-
-
0.0000000097
chagasin mutant T31V
-
-
-
0.0000000068
chagasin mutant T31Y
-
-
-
0.000000014
chagasin mutant T32A
-
-
-
0.000000032
chagasin mutant T32S
-
-
-
0.00000002
chagasin mutant T32V
-
-
-
0.0000000027
chagasin mutant T32Y
-
-
-
0.000000825
chagasin mutant W93A
-
-
-
0.00000005
cystatin A, cystatin B
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000008
cystatin C
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000281
cystatin D
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000049
cystatin F
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.00000178
cystatin M/E
-
0.1 M acetate pH 5.5, 1 mM EDTA, 2 mM dithiothreitol, 100 mg/ml bovine serum albumin, 10 min
-
0.0000000101
fragment p41 of major histocompatibility complex class II-associated invariant chain
pH 6.0, 25°C
-
0.0107
KAPR-acetyl-K-QLATKAARKSAPA
pH and temperature not specified in the publication
0.00502
KAPRKQLAT-acetyl-K-AARKSAPA
pH and temperature not specified in the publication
0.00455
KAPRKQLATKAAR-dimethyl-K-SAPA
pH and temperature not specified in the publication
0.0045
KAPRKQLATKAARKSAPA
pH and temperature not specified in the publication
0.02
N-(2,6-dimethylbenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0027
N-(2-chloro-5-nitrobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0032
N-(3-phenylpropanoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0043
N-(4-biphenylacetyl)-S-methylcysteine-(D)-Arg-Phe-beta-phenethylamide
-
wild type enzyme
0.0023
N-(4-bromobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.009
N-(biphenyl-4-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0078
N-(cyclopent-1-en-1-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.001
N-(naphthalen-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0068
N-(pentafluorobenzoyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0061
N-(piperidin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0055
N-(pyridin-2-ylcarbonyl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.007
N-[(2R)-2-[(2-amino-2-oxoethyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00089
N-[(2R)-2-[(3-aminopropyl)amino]-2-[[(benzyloxy)carbonyl]amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00039
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(3a,7a-dihydro-1H-indol-3-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00045
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-(propan-2-ylamino)acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00074
N-[(2R)-2-[[(benzyloxy)carbonyl]amino]-2-[(2-carbamimidamidoethyl)amino]acetyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0046
N-[(4'-carboxy-2,2'-bipyridin-4-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.005
N-[(6-aminopyridin-3-yl)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0031
N-[(benzyloxy)carbonyl]-3-(1H-indazol-1-yl)-L-alanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0042
N-[(benzyloxy)carbonyl]-3-(1H-indol-1-yl)-L-alanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00012
N-[(benzyloxy)carbonyl]-4-(thiophen-2-yl)-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.014
N-[(benzyloxy)carbonyl]-L-phenylalanyl-3-(1H-imidazol-1-yl)-L-alaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.026
N-[(benzyloxy)carbonyl]-L-phenylalanyl-4-amino-L-phenylalaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.027
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-hydroxy-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.016
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-alaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.028
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-argininamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.014
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-leucinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0042
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.064
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-methioninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0035
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-ornithinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.017
N-[(benzyloxy)carbonyl]-L-phenylalanyl-L-valinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0026
N-[(benzyloxy)carbonyl]-L-phenylalanyl-N6-methyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0014
N-[(benzyloxy)carbonyl]-L-tyrosyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0025
N-[3-(4-hydroxyphenyl)propanoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0024
N-[3-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0026
N-[4-(acetyloxy)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.0029
N-[4-(dimethylamino)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.001
N-[4-(trifluoromethyl)benzoyl]-L-phenylalanyl-L-lysinamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.028
Nalpha-[(benzyloxy)carbonyl]-N-[(1R)-1,2-diamino-2-oxoethyl]-L-phenylalaninamide
-
100 mM phosphate buffer, pH 6.0, 2 mM EDTA, temperature not specified in the publication
0.00000043
naphthalene-2-carboxylic acid ((S)-2-naphthalen-2-yl-1-[(S)-3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]ethyl)amide
-
-
0.0000014
naphthoic-1-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.0095
ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.005
ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.0002
ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.01
ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
0.00000000552 - 0.0000000101
p41-fragment-human
-
0.0000006
Phe-Tyr-(OBut)-COCHO
pH and temperature not specified in the publication
0.000005
quinoline-2-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.0000082
quinoline-8-carboxylic acid ((S)-1-[3-oxo-1-(pyridine-2-sulfonyl)azepan-4-ylcarbamoyl]-3-methyl-butyl)amide
-
-
0.00013
RKLLW-NH2
-
pH 5.5, 37°C
0.0000007
testican-1
-
-
-
0.00000014
thyroglobulin type-1 domain
-
0.1 M sodium acetate, 1 mM EDTA, 24°C
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082
(13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0091
(13alpha,17alpha,20S,24Z)-3-oxolanosta-7,24-dien-26-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.01
(2-fluorobenzophenone) thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.000574
(2E)-2-(6-bromo-1,1-dioxido-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000152
(2E)-2-(6-bromo-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000164
(2E)-2-(6-bromo-2,3-dihydroquinolin-4(1H)-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.000068
(2E)-2-(6-nitro-2,3-dihydro-4H-thiochromen-4-ylidene)hydrazinecarbothioamide
Homo sapiens
pH 6.0, 37°C
0.00246
(2E)-2-[(2-fluorophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000118
(2E)-2-[(3-bromophenyl)(3,4,5-trifluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000415
(2E)-2-[(3-bromophenyl)(3,5-dichlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000594
(2E)-2-[(3-bromophenyl)(3,5-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000131
(2E)-2-[(3-bromophenyl)(3-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
(2E)-2-[(3-bromophenyl)(3-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000224
(2E)-2-[(3-bromophenyl)(3-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(3-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000327
(2E)-2-[(3-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000796
(2E)-2-[(3-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00216
(2E)-2-[(3-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000465
(2E)-2-[(3-bromophenyl)[3-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000521
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(4-bromophenyl)(4-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00332
(2E)-2-[(4-bromophenyl)(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00457
(2E)-2-[(4-bromophenyl)(4-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2E)-2-[(4-bromophenyl)[4-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
(2E)-2-[6-(propan-2-yloxy)-2,3-dihydro-4H-thiochromen-4-ylidene]hydrazinecarbothioamide
Homo sapiens
above, pH 6.0, 37°C
0.000096
(2E)-2-[[3,5-bis(trifluoromethyl)phenyl](3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
(2E)-[(3E)-28-methoxy-28-oxours-12-en-3-ylidene]acetic acid
Homo sapiens
-
IC50 above 0.5 mM, at pH 5.5 and 37°C
0.0026
(2Z)-2-[(2-bromophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2Z)-2-[(2-bromophenyl)(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
(2Z)-2-[(2-fluorophenyl)(phenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000233
(2Z)-2-[(3-bromo-2-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000114
(2Z)-2-[(3-bromo-4-fluorophenyl)(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000632
(2Z)-2-[(3-bromophenyl)(2,3,4,5-tetrafluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000838
(2Z)-2-[(3-bromophenyl)(2,3-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00061
(2Z)-2-[(3-bromophenyl)(2,6-difluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00161
(2Z)-2-[(3-bromophenyl)(2-chlorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000305
(2Z)-2-[(3-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
(2Z)-2-[(3-bromophenyl)(2-methylphenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00222
(2Z)-2-[(4-bromophenyl)(2-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000305
(3-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0001314
(3-bromo-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
(3-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.0097
(3E)-3-(carboxymethylidene)olean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0123
(3E)-3-(carboxymethylidene)urs-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.00222
(4-bromo-2'-fluoro-3'-hydroxybenzophenone) thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.000056
1,3,5-trisbenzoylbenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000081
1,3-bis(2-fluorobenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01035
1,3-bis(3-bromobenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(3-bromobenzoyl)-5-hydroxybenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000716
1,3-bis(3-hydroxybenzoyl)-5-bromobenzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.000654
1,3-bis(3-methylbenzoyl)benzene thisosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(4-bromobenzoyl)benzene bis-thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.001522
1,3-bis(4-bromobenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0000144
1,3-bis(4-fluorobenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.00034
1,3-bis(4-hydroxybenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.01
1,3-bis(4-isopropoxybenzoyl)benzene thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.005117
1,3-bis(4-methoxybenzoyl)benzene thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.00045
1,3-dihydro-pyrrolo[3,4-b]quinoline-2-carbonitrile
Homo sapiens
-
IC50: 0.00045 mM
0.00001
1-cyano-3-azetidinyl cyclohexylmethyl ether
Homo sapiens
-
IC50: 0.00001 mM
0.00043
1-cyanoazetidine
Homo sapiens
-
IC50: 0.00043 mM
0.004
1-cyanopyrrolidine
Homo sapiens
-
IC50: 0.004 mM
0.109
2,6-dimethoxy-4-[4-(4-phenoxyphenyl)-5-phenyl-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.087
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.0808
2-(1,3-benzodioxol-5-yl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.000007
2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylate
Homo sapiens
-
-
0.0863
2-(3,4-dimethoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.074
2-(4-methoxyphenyl)-4-[8-[2-(4-methoxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0818
2-(4-methoxyphenyl)-5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0927
2-(acetylamino)-N-[4-(6-[[2-(acetylamino)benzoyl]amino]-1H-benzimidazol-2-yl)phenyl]benzamide
Homo sapiens
pH 7.4, 37°C
0.0402
2-(furan-2-yl)-4-[8-[2-(furan-2-yl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0012
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0011
2-cyano-4-(cyclohexylamino)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00078
2-cyano-4-(cyclohexylmethoxy)-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000426
2-cyano-4-[(1,4-dioxaspiro[4.5]dec-8-ylmethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0004
2-cyano-4-[(2-cyclopentylethyl)amino]-N-methyl-6-[(1-methylpiperidin-4-yl)methoxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.002
2-cyano-4-[(cyclohexylmethyl)(methyl)amino]-N-(2-phenylethyl)pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00001
2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-N-(2-phenylethyl)-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0003
2-cyano-4-[[1-(2-hydroxyethyl)piperidin-4-yl]methoxy]-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00051
2-cyano-N-(1-methyl-4-phenylpiperidin-4-yl)-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00046
2-cyano-N-methyl-4-(piperidin-4-ylmethoxy)-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00036
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000276
2-cyano-N-methyl-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[4.5]dec-8-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00139
2-cyano-N-methyl-4-[(spiro[3.5]non-7-ylmethyl)amino]-6-[(2,2,6,6-tetramethylpiperidin-4-yl)oxy]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00012
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
0.00044
2-cyano-N-methyl-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00033
2-cyano-N-methyl-4-[[1-(1-methylethyl)piperidin-4-yl]methoxy]-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0007
2-cyano-N-[(1-methyl-4-phenylpiperidin-4-yl)methyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00048
2-cyano-N-[(1R)-2-pyridin-2-yl-1-(pyrrolidin-1-ylmethyl)ethyl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00084
2-cyano-N-[5-[(1-methylpiperidin-4-yl)oxy]biphenyl-2-yl]-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000007
2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarboxylic 3,4-dihydroquinoline-1(2H)-carboxylic anhydride
Homo sapiens
in 1 mM EDTA, 5 mM cysteine at pH 5.5
0.01
2-[bis(3-bromophenyl)methylidene]-N-ethylhydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
2-[bis(3-bromophenyl)methylidene]-N-phenylhydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00487
2-[bis(3-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
pH and temperature not specified in the publication
0.01
2-[bis(4-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.01
2-[bis(4-fluorophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.00893
2-[cyclohexyl(methyl)amino]-4H-3,1-benzothiazin-4-one
Homo sapiens
-
37°C, pH 6.0
0.00001
3-(benzyloxy)-1-cyanoazetidine
Homo sapiens
-
IC50: 0.00001 mM
0.0026
3-(hydroxyimino)masticadienoic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0024
3-(hydroxyimino)oleanolic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0000238
3-benzoylbenzhydrol thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.0065
3-epiursolic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0072
3-hydroxyolean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0395
3-hydroxyurs-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0147
3-oxoolean-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.0083
3-oxours-12-en-28-oic acid
Homo sapiens
-
at pH 5.5 and 37°C
0.00015
3-[(benzyloxy)methyl]-1-cyanopyrrolidine
Homo sapiens
-
IC50: 0.00015 mM
0.0847
4,4'-[methanediylbis(1H-benzimidazole-5,2-diyl)]dianiline
Homo sapiens
pH 7.4, 37°C
0.0865
4-(4-[8-[2-(4-carboxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0621
4-(4-[8-[2-(4-hydroxyphenyl)-4-phenyl-1H-imidazol-5-yl]dibenzo[b,d]furan-2-yl]-5-phenyl-1H-imidazol-2-yl)phenol
Homo sapiens
pH 7.4, 37°C
0.0834
4-amino-N-(4-[6-[(4-aminobenzoyl)amino]-1H-benzimidazol-2-yl]phenyl)benzamide
Homo sapiens
pH 7.4, 37°C
0.0025
4-[(1-acetylpiperidin-4-yl)methoxy]-2-cyano-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
determined by a fluorometric assay with recombinant catL employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0922
4-[(E)-benzylideneamino]-N-[4-[6-([4-[(E)-benzylideneamino]benzoyl]amino)-1H-benzimidazol-2-yl]phenyl]benzamide
Homo sapiens
pH 7.4, 37°C
0.00087
4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.08835
4-[4-(5,5-dioxidodibenzo[b,d]thiophen-2-yl)-5-phenyl-1H-imidazol-2-yl]-2,6-dimethoxyphenol
Homo sapiens
pH 7.4, 37°C
0.0997
4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
Homo sapiens
pH 7.4, 37°C
0.0655
4-[8-(2,4-diphenyl-1H-imidazol-5-yl)dibenzo[b,d]furan-2-yl]-2,5-diphenyl-1H-imidazole)
Homo sapiens
pH 7.4, 37°C
0.00028
5-bromo-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-2-carbonitrile
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0981
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(2,4,5-trimethoxyphenyl)-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.0888
5-phenyl-4-[4-(phenylsulfanyl)phenyl]-2-(3,4,5-trimethoxyphenyl)-1H-imidazole
Homo sapiens
pH 7.4, 37°C
0.000096
6-(4-chlorobenzyl)-7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00084
6-(4-chlorobenzyl)-7-(2-cycloheptylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00032
6-(4-chlorobenzyl)-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00026
6-(4-chlorobenzyl)-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000023
6-(4-chlorobenzyl)-7-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000018
6-(4-chlorobenzyl)-7-(3,3-dimethylbutyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00037
6-(4-chlorobenzyl)-7-(cyclohexylmethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.00004
6-(4-chlorobenzyl)-7-[2-(3-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.000086
6-(4-chlorobenzyl)-7-[2-(4-chlorophenyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT L employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.0068
6-[[4-(4-acetylpiperazin-1-yl)-2-fluorophenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0052
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0023
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-(2-cyclopentylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.0062
6-[[4-(4-acetylpiperazin-1-yl)phenoxy]methyl]-7-[2-(4,4-difluorocyclohexyl)ethyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
with Z-Phe-Arg-7-amido-4-methylcoumarin as substrate
0.00079
7-(2-cyclohexylethyl)-6-[(pyridin-2-yloxy)methyl]-7H-pyrrolo[2,3-d]pyrimidine-2-carbonitrile
Homo sapiens
-
inhibition profiles are determined by a fluorometric assay with recombinant CAT K employing Z-Phe-Arg-7-amido-4-methylcoumarin as synthetic substrate
0.01
benzophenone thiosemicarbazone
Homo sapiens
above, pH 6.0, 37°C
0.0000099
benzoylbenzophenone thiosemicarbazone
Homo sapiens
pH 6.0, 37°C
0.000054
benzyl 1-cyano-3-pyrrolidinylcarbamate
Homo sapiens
-
IC50: 0.000054 mM
0.0972
bis[2-(4-aminophenyl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH 7.4, 37°C
0.000056
cathepsin L inhibitor 1
Homo sapiens
thiocarbazate cathepsin L inhibitor, 20 mM sodium acetate, 1 mM EDTA, 5 mM cysteine at pH 5.5
0.000056
CID 16725315
Homo sapiens
-
pH and temperature not specified in the publication
0.0000069
CID 23631927
Homo sapiens
-
pH and temperature not specified in the publication
0.1
diethyl-cyanamide
Homo sapiens
-
IC50 is above 0.1 mM
0.00003
E-64
Homo sapiens
-
at pH 5.5 and 37°C
0.0008
LFLTR-NH2
Homo sapiens
-
IC50: 0.0008 mM
0.0005
LLLTR-NH2
Homo sapiens
-
IC50: 0.0005 mM
0.25
methyl (13alpha,17alpha,20S,24Z)-3-hydroxylanosta-7,24-dien-26-oate
Homo sapiens
-
IC50 above 0.25 mM, at pH 5.5 and 37°C
0.5
methyl (3Z,13alpha,17alpha,20S,24Z)-3-(hydroxyimino)lanosta-7,24-dien-26-oate
Homo sapiens
-
IC50 above 0.5 mM, at pH 5.5 and 37°C
0.0386
methyl 5-acetyloxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C
0.0616
methyl 5-hydroxy-dinaphtho[1,2-2'3']furan-7,12-dione-6-carboxylate
Homo sapiens
-
pH 5.5, 22°C
0.00175
N-(1-cyano-3-pyrrolidinyl)benzamide
Homo sapiens
-
IC50: 0.00175 mM
0.00008
N-(1-cyano-3-pyrrolidinyl)benzenesulfonamide
Homo sapiens
-
IC50: 0.00008 mM
0.00085
N-(1-cyano-3-pyrrolidinyl)[1,1'-biphenyl]-4-carboxamide
Homo sapiens
-
IC50: 0.00085 mM
0.00018
N-(4-benzyl-1-methylpiperidin-4-yl)-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.000064
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)methoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0001
N-benzyl-2-cyano-4-[(1-methylpiperidin-4-yl)oxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00027
N-benzyl-2-cyano-4-[2-(1-methylpiperidin-4-yl)ethoxy]-6-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.01
N-benzyl-2-[bis(3-bromophenyl)methylidene]hydrazinecarbothioamide
Homo sapiens
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.023
N-[(1-cyano-2-pyrrolidinyl)methyl]benzamide
Homo sapiens
-
IC50: 0.023 mM
0.0115
N-[(1-cyano-2-pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.0115 mM
0.00065
N-[(1-cyano-3-azetidinyl)methyl]benzamide
Homo sapiens
-
IC50: 0.00065 mM
0.00005
N-[(1-cyano-3-azetidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.00005 mM
0.000006
N-[(1-cyano-3-azetidinyl)methyl]cyclohexanecarboxamide
Homo sapiens
-
IC50: 0.000006 mM
0.00035
N-[(1-cyano-3-pyrrolidinyl)methyl]benzenesulfonamide
Homo sapiens
-
IC50: 0.00035 mM
0.00015
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.00084
N-[(1R)-1-benzyl-2-pyrrolidin-1-ylpropyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0015
N-[(1S)-1-benzyl-2-pyrrolidin-1-ylethyl]-2-cyano-4-[(spiro[2.5]oct-6-ylmethyl)amino]pyrimidine-5-carboxamide
Homo sapiens
inhibition are determined by a fluorometric assay with recombinant Cat L
0.0625
N-[4-(1H-benzimidazol-2-yl)phenyl]-2,2-diphenylacetamide
Homo sapiens
pH 7.4, 37°C
0.0862
N-[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl]-2-chlorobenzamide
Homo sapiens
pH 7.4, 37°C
0.0006
RKLLW-NH2
Homo sapiens
-
IC50: 0.0006 mM
0.014
RKLWD-NH2
Homo sapiens
-
IC50: 0.014 mM
0.0008
RKLWL-NH2
Homo sapiens
-
IC50: 0.0008 mM
0.00011
S-(2-oxo-1-phenylpyrrolidin-3-yl) 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.000041
S-[2-(3,4-dihydroquinolin-1(2H)-yl)-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.000001 - 0.000056
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
0.000115
S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropanoyl]hydrazinecarbothioate
Homo sapiens
-
-
0.033
S-{2-[(2-ethylphenyl)amino]-2-oxoethyl} 2-[(2R)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate
Homo sapiens
thiocarbazate cathepsin L inhibitor, 1 mM EDTA, 5 mM cysteine at pH 5.5
additional information
(3-[[2-cyano-7-(2-cyclohexylethyl)-7H-pyrrolo[2,3-d]pyrimidin-6-yl]methoxy]phenyl)acetic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5.5
-
hydrolysis of elastin
4.8
gelatinolytic activity
5.6
assay at
6.5
-
assay at 28°C
7.4
in vivo assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
pH 4.0: about 50% of maximal activity, pH 6.0: about 15% of maximal activity
4 - 7
4.2 - 4.8
-
the rate of trypsin inactivation is strongly pH dependent in the range between 4.2 and 4.8 in the presence of Ca2+
5.2 - 5.8
-
the rate of trypsin inactivation is strongly pH dependent in the range between 5.2 and 5.8 in the absence of Ca2+
5.5 - 6.8
the activity is higher at pH 5.5 compared to pH 6.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
calculated value from mature cathepsin L
5.3
calculated value from procathepsin L
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from lungs of healthy adults
Manually annotated by BRENDA team
-
increased level of cathepsin L in atherosclerotic lesions compared with healthy aortas
Manually annotated by BRENDA team
-
cathepsin L is highly expressed in endothelial progenitor cells compared to mature endothelial cells
Manually annotated by BRENDA team
-
carotid atherosclerotic lesions. Expression of lysosomal cathepsin L is significantly increased in atherosclerotic plaques with formation of the necrotic core and rupture of the cap. In those plaques, cathepsin L is associated mainly with CD68-positive macrophages, whereas significant lower levels of smooth muscle cell actin are detected. The expression of cathepsin L in these plaques is also correlated with apoptosis and the stress protein ferritin. Plaques from symptomatic patients show greater increased levels of cathepsin L than those from asymptomatic patients. Human monocyte-derived macrophages from coronary artery disease patients show significantly higher levels of cathepsin L, cellular lipids and apoptosis versus cells from matched healthy donors. 7beta-hydroxycholesterol significantly enhances cathepsin L in cells from healthy donors but not in cells from coronary artery disease patients. Macrophage apoptosis is significantly correlated with expression of cathepsin L in cell nuclei and membranes
Manually annotated by BRENDA team
-
of non-small-cell lung cancer cell line EPLC 32M1
Manually annotated by BRENDA team
-
incubation of endothelial progenitor cells with high levels of glucose dose-dependently decreases cathepsin L activity and protein expression, while other proteases such as cathepsins D and O, and matrix metalloproteases MMP-2 and MMP-9, are not altered. Cathepsin L mRNA level is not affected
Manually annotated by BRENDA team
tial expression of cathepsin L during the cell cycle of HCT116 cells.Cathepsin L amounts are highest in nuclear fractions compared to lysosomal preparations of G1/G0-arrested cells, whereas lysosomal levels of cathepsin L protein exceed those of the nuclear fractions when cells are inspected in either S or G2/M phase
Manually annotated by BRENDA team
-
infection with Anaplasma phagocytophilum results in elevated cathepsin L activity and the proteolysis of CDP
Manually annotated by BRENDA team
-
choriocarcinoma cell
Manually annotated by BRENDA team
-
metastatic cervical lymph node
Manually annotated by BRENDA team
-
inhibition of cathepsin L by an inhibitor or siRNA reverses drug resistance and induces senescence in drug resistant neuroblastoma cells
Manually annotated by BRENDA team
-
cheek and forearm stratum corneum
Manually annotated by BRENDA team
-
detectable by immunohistochemistry in malignant cells but not in normal skin cells
Manually annotated by BRENDA team
-
detectable by immunohistochemistry in malignant cells but not in normal skin cells
Manually annotated by BRENDA team
-
from patients with osteoarthritis, rheumatoid arthritis, calcium phosphate crystal-induced synovitis
Manually annotated by BRENDA team
additional information
enzyme expression levels in normal epithelial and in proliferating cancer cells, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
cathepsin L isoform CRA-b
Manually annotated by BRENDA team
cathepsin L isoform CRA-b
-
Manually annotated by BRENDA team
-
procathepsin L
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
cathepsin L is a member of the cysteine cathepsin protease family
malfunction
metabolism
CathL acts as an extracellular ligand and plays an important pro-angiogenic, and thus pro-metastatic, role during epithelial ovarian cancer metastasis to the omentum, by activating the omental microvasculature
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATL1_HUMAN
333
0
37564
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q9HBQ7_HUMAN
151
0
16839
TrEMBL
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
x * 14000 + x * 32000, under reducing conditions detection of three bands, SDS PAGE under non-reducing conditions
21000
-
1 * 21000 + 1 * 5000, active form
25000
27000
-
mature cathepsin L, SDS-PAGE
27000 - 29000
-
SDS-PAGE, enzyme from pituitary gland
29000
recombinant enzyme, SDS-PAGE
30000
31000
32000
-
x * 14000 + x * 32000, under reducing conditions detection of three bands, SDS PAGE under non-reducing conditions
40000
-
gel filtration
42000
-
pro-cathepsin L, SDS-PAGE
50000
60000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
investigation of the phosphorylation status of the secreted and lysosomal cathepsin L forms by treatment with alkaline phosphatase (ALP). The 32-kDa form of cathepsin L is phosphorylated, while the 34-kDa form is already dephosphorylated. The 32-kDa form might migrate to the anode faster than the dephosphorylated 34-kDa form because of the retention of the negative charge by the phosphate moiety. Acid phosphatase might remove the phosphorus group from the 32-kDa form as soon as it enters the lysosomes, thereby converting it to the 34-kDa form. The phosphorylated status of 32-kDa cathepsin L suggests that the secreted form has never enters lysosomes
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimera C25S/S24A/W26Y/M161L/D162N/G164A/V165M/E159S/D160S/E153S/P154S plus 173ESTESDNN180 to ISNNQ to 1.5 A resolution. Structure is almost identical to cathepsin L
crystal structure of the major histocompatibility complex class II-associated p41 li fragment bound to cathepsin L
-
docking studies using inhibitor S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate reveal the simultaneous occupation of the S2, S3, and S1' subsites by hydrophobic and aromatic functionalities of the thiocarbazate. A key hydrogen bond is observed between the Gly66 backbone NH and the amino acid derived carbonyl of the diacyl hydrazine
-
enzyme complexed with E-64
-
hanging drop vapor diffusion method, 1.9 A X-ray structure of the complex of cathepsin L with the inhibitor 13
hanging drop vapour diffusion method with 17% (w/v) polyethylene glycol 8000 and 0.2 M ammonium sulfate
-
in complex with inhibitor biphenylacetyl-(Nepsilon-biphenylacetyl)-L-Lys-D-Arg-L-Tyr-N-phenylethyl, hanging drop vapor diffusion method, using 19%(w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate, or in complex with inhibitor biphenylacetyl-(Nepsilon-biphenylacetyl)L-Lys-D-Arg-L-Phe-N-phenylethyl hanging drop vapor diffusion method, using 25% (w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate, or in complex with biphenylacetyl-M-Cys-D-Arg-L-Phe-N-phenylethyl, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate
in complex with inhibitor Phe-Tyr-(OBut)-COCHO, hanging drop vapor diffusion method, using 15% (w/v) PEG 8K and 200 mM ammonium sulfate, pH 4.8. In complex with inhibitor Phe-Tyr-(tert-Bu)-diazomethylketone, hanging drop vapor diffusion method, using 30% (w/v) PEG 8K and 200 mM ammonium sulfate, pH 5.2
modelling 3D-structure of cathepsin L (PDB entry 1ICF), analysing residues binding the inhibitor p41-fragment, comparing binding sites of different Cathepsins
molecular docking study with inhibitor S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate using the structure of papain/CLIK-148, PDB entry 1cvz
-
molecular modeling of complex with fragment p41 of major histocompatibility complex class II-associated invariant chain
purified inactivated cathepsin L mutant C25S, method optimization, rod-shaped crystals grow within 2 weeks in 0.1 M bis-Tris-HCl, pH 5.5, and 2 M ammonium sulfate, cube-shaped crystals grow within 2 weeks in 0.11 M HEPES-NaOH, pH 7.5, and 2.14 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.42 A resolution. The cathepsin L molecule is cleaved autocatalytically, with the cleaved region trapped in the active site cleft of the neighboring molecule demonstrated remaining low levels of catalytic activity
the inactive C25A cathepsin L mutant is cocrystallized with a histone H3 peptide covering residues 19-33 of the human histone H3 tail (QLATKAARKSAPATG), sitting drop vapor diffusion method, using 10% (v/v) isopropanol, 0.1 M sodium acetate trihydrate, pH 4.0, 22% polyethylene glycol 6000. The final crystallization condition for the apo-mC25A crystals is 0.2 M ammonium sulfate, 0.1 M sodium acetate trihydrate, pH 4.6, 30% (w/v) polyethylene glycol 2000 monomethylether
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A205L
-
mutant shows an effective cathepsin K-like preference for Leu and Pro
C25A
inactive
C25S/S24A/W26Y
mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity
C25S/S24A/W26Y/M161L/D162N/G164A/V165M
mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity, but less than mutant C25S/S24A/W26Y
G139R
L67Y/A205L
-
mutation induces a switch of the enzymatic specificity toward small selective inhibitors and peptidyl substrates
T223V
T223V/C138S
the mutations prevent catalytic activity
T223V/C138S/K99A/K104A
the mutations disrupt the putative heparin binding site
T223V/DELTAE286-E289
the mutation shows reduced enzyme activity
T223V/DELTAE286-N293
the mutation shows reduced enzyme activity
T223V/M274L/D275N/G277A/V278M
the mutation shows reduced enzyme activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6 - 6.2
-
activity of cathepsin L increases from pH 3.6 to 6.2 and is independent of the calcium concentration, The rate of trypsin inactivation by cathepsin L is thus approximately 10 times faster at pH 4.0 than at pH 5.5
712089
4.5 - 5.5
-
37°C, 24 h, more than 70% of the activity is retained
647919
7
-
15 min, 85% loss of activity
647919
8
the mature form of cathepsin L exhibits very little activity at pH 8.0 and is largely unfolded
677987
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
pH 4.5-5.5, 24 h, more than 70% of the activity is retained
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heparin reduces the stability of the pro form of cathepsin L at pH 5 by binding to a putative heparin binding motif (BBXB) in the pro-domain, in contrast heparin only slightly destabilizes the mature cathepsin L domain
MHC class II-associated invariant chain fragment from human kidney that has stabilizing effect on the enzyme
-
testican-1 stabilizes at neutral pH
-
when no reducing agents are present in the assay environment, the activity of cathepsin L is markedly slowed down, and the rate of product formation is reduced by about half
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Phenyl-Sepharose column chromatography, and SP-Sepharose column chromatography
butyl-Sepharose column chromatography
-
CM Sepharose column chromatography
complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney that has stabilizing and inhibitory effect
-
heparin-Sepharose chromatography
Ni-Sepharose 6 Fast Flow column, eluted with binding buffer containing 500 mM imidazole, activation of immature cathepsin L by dialysis, Sephadex-75 HR column, dialysis, blocked with 10-fold molar excess of methyl-methanethiosulfonate
partial
-
partial purification by Superdex-75 gel filtration
-
the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplification of cDNA by PCR, PCR-products cloned into Pichia pastoris expression vector pPIC9K with His-tag, transformation of Pichia pastoris strain GS115, 4 days of expression
cardiac over-expression in mice
-
cell culture of endothelial progenitor cells, inhibitor glucose at higher concentrations dose-dependently decreases endothelial progenitor cells invasion, coincubation of glucose in higher concentrations and inhibitor N-benzyloxycarbonyl-Phe-Phe-fluoromethylketone does not decrease further endothelial progenitor cell invasion, high glucose concentrations decreases cathepsin L expression level but not cathepsin L mRNA level, reduced cathepsin L expression in patients with diabetes mellitus
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in mouse thymus
-
expressed in Mus musculus
expressed in Mus musculus 3T3-L1 pre-adipocytes
-
expressed in Mus musculus heart
-
expressed in Pichia pastoris
expressed in Pichia pastoris strain X-33
expression in Pichia pastoris
mutants expressed in Pichia pastoris
-
pro-(cathepsin L)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significantly increased extracellular release of cathepsin L is observed after repeated irradiation with UVA up to four times
-
cathepsin L increased level follows active Ras overexpression, the p38 MAPK inhibitor SB203580 produces an increase of cathepsin L content
-
chronic sun exposure causes an increase in Cat L activity
-
expression of cathepsin L is elevated in cancer
-
expression of cathepsin L is not elevated in non-malignant tumor cells
-
the protein of cathepsin L is overexpressed in 47% primary tumor tissues, and in 89% metastatic cervical lymph node samples
-
upregulation of osteoclast cathepsin L activity and secretion occurs by cytokines promoting bone resorption, c-Src tyrosine kinase, interleukin-1alpha, interleukin-6, and tumor necrosis factor-alpha. Intracellular expression levels of cathepsin L are upregulated in many human tumors. In U-87MG glioblastoma cells, vascular endothelial growth factor upregulates at transcriptional level cathepsin L
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the optimum cathepsin L renaturation buffer consists of 50 mM Tris, 4 mM GSH, 0.5 mM GSSG, 300 mM MgSO4, 0.05% (w/v) 3-(3-cholamidopropyl)-dimethylammonio-1-propane sulfonate, 0.04 mM propetide, at pH 7.75 and 16°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
specificity and sensitivity of cathepsin L activity is a diagnostic biomarker for proteinuria
drug development
a clickable and tagless activity-based probe of cathepsin L probe is a highly effective tool in dissecting cathepsin L biology at the proteome levels in both normal physiology and human diseases, thereby facilitating drug-discovery efforts targeting cathepsin L
medicine
pharmacology
-
chloroquine inhibits the infection with live Nipah virus and Hendra virus at a concentration of 1 microM in vitro. The mechanism for the antiviral action likely is the inhibition of cathepsin L, which is essential for the processing of the viral fusion glycoprotein and the maturation of newly budding virions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baricos, W.H.; Zhou, Y.; Mason, R.W.; Barrett, A.J.
Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane
Biochem. J.
252
301-304
1988
Homo sapiens
Manually annotated by BRENDA team
Reilly, J.J.; Mason, R.W.; Chen, P.; Joseph, L.J.; Sukhatme, V.P.; Yee, R.; Chapman, H.A.
Synthesis and processing of cathepsin L, an elastase, by human alveolar macrophages
Biochem. J.
257
493-498
1989
Homo sapiens
Manually annotated by BRENDA team
Crawford, C.; Mason, R.W.; Wikstrom, P.; Shaw, E.
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
Biochem. J.
253
751-758
1988
Homo sapiens
Manually annotated by BRENDA team
Maciewicz, R.E.; Etherington, D.J.
Enzyme immunoassay for cathepsin B and L in synovial fluids from patients with arthritis
Biochem. Soc. Trans.
16
812-813
1988
Homo sapiens
-
Manually annotated by BRENDA team
Mason, R.W.
Species variants of cathepsin L and their immunological identification
Biochem. J.
240
285-288
1986
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Mason, R.W.; Johnson, D.A.; Barrett, A.J.; Chapman, H.A.
Elastinolytic activity of human cathepsin L
Biochem. J.
233
925-927
1986
Homo sapiens
Manually annotated by BRENDA team
Mason, R.W.; Green, G.D.J.; Barrett, A.J.
Human liver cathepsin L
Biochem. J.
226
233-241
1985
Homo sapiens
Manually annotated by BRENDA team
Guncar, G.; Pungercic, G.; Klemencic, I.; Turk, V.; Turk, D.
Crystal structure of HMC class II-associated p41 li fragment bound to cathepsin I reveals the structural basis for differentiation between cathepsin L and S
EMBO J.
18
793-803
1999
Homo sapiens
Manually annotated by BRENDA team
Pagano, M.; Esnard, F.; Engler, R.; Gauthier, F.
Inhibition of human liver cathepsin L by alpha 2 cysteine-proteinase inhibitor and the low-Mr cysteine proteinase inhibitor from human serum
Biochem. J.
220
147-155
1984
Homo sapiens
Manually annotated by BRENDA team
Gal, S.; Gottesman, M.M.
Isolation and sequence of a cDNA for human pro-(cathepsin L)
Biochem. J.
253
303-306
1988
Homo sapiens
Manually annotated by BRENDA team
Fujishima, A.; Imai, Y.; Nomura, T.; Fujisawa, Y.; Yamamoto, Y.; Sugawara, T.
The crystal structure of human cathepsin L complexed with E-64
FEBS Lett.
407
47-50
1997
Homo sapiens
Manually annotated by BRENDA team
Ogrinc, T.; Dolenc, I.; Ritonja, A.; Turk, V.
Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney
FEBS Lett.
336
555-559
1993
Homo sapiens
Manually annotated by BRENDA team
Nomura, T.; Fujishima, A.; Fujisawa, Y.
Characterization and crystallization of recombinant human cathepsin L
Biochem. Biophys. Res. Commun.
228
792-796
1996
Homo sapiens
Manually annotated by BRENDA team
Dahl, S.W.; Halkier, T.; Lauritzen, C.; Dolenc, I.; Pedersen, J.; Turk, V.; Turk, B.
Human recombinant Pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
Biochemistry
40
1671-1678
2001
Homo sapiens
Manually annotated by BRENDA team
Guay, J.; Falgueyret, J.P.; Ducret, A.; Percival, M.D.; Mancini, J.A.
Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
Eur. J. Biochem.
267
6311-6318
2000
Homo sapiens
Manually annotated by BRENDA team
Ohashi, K.; Naruto, M.; Nakaki, T.; Sano, E.
Identification of interleukin-8 converting enzyme as cathepsin L
Biochim. Biophys. Acta
1649
30-39
2003
Homo sapiens
Manually annotated by BRENDA team
Desmazes, C.; Gauthier, F.; Lalmanach, G.
Cathepsin L, but not cathepsin B, is a potential kininogenase
Biol. Chem.
382
811-815
2001
Homo sapiens
Manually annotated by BRENDA team
Brinker, A.; Weber, E.; Stoll, D.; Voigt, J.; Muller, A.; Sewald, N.; Jung, G.; Wiesmuller, K.H.; Bohley, P.
Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections
Eur. J. Biochem.
267
5085-5092
2000
Homo sapiens
Manually annotated by BRENDA team
Bocock, J.P.; Edgell, C.J.; Marr, H.S.; Erickson, A.H.
Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L
Eur. J. Biochem.
270
4008-4015
2003
Homo sapiens
Manually annotated by BRENDA team
Chiva, C.; Barthe, P.; Codina, A.; Gairi, M.; Molina, F.; Granier, C.; Pugniere, M.; Inui, T.; Nishio, H.; Nishiuchi, Y.; Kimura, T.; Sakakibara, S.; Albericio, F.; Giralt, E.
Synthesis and NMR structure of p41icf, a potent inhibitor of human cathepsin L
J. Am. Chem. Soc.
125
1508-1517
2003
Homo sapiens
Manually annotated by BRENDA team
Falgueyret, J.P.; Oballa, R.M.; Okamoto, O.; Wesolowski, G.; Aubin, Y.; Rydzewski, R.M.; Prasit, P.; Riendeau, D.; Rodan, S.B.; Percival, M.D.
Novel, nonpeptidic cyanamides as potent and reversible inhibitors of human cathepsins K and L
J. Med. Chem.
44
94-104
2001
Homo sapiens
Manually annotated by BRENDA team
Chowdhury, S.F.; Sivaraman, J.; Wang, J.; Devanathan, G.; Lachance, P.; Qi, H.; Menard, R.; Lefebvre, J.; Konishi, Y.; Cygler, M.; Sulea, T.; Purisima, E.O.
Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides
J. Med. Chem.
45
5321-5329
2002
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Klose, A.; Zigrino, P.; Dennhoefer, R.; Mauch, C.; Hunzelmann, N.
Identification and discrimination of extracellularly active cathepsins B and L in high-invasive melanoma cells
Anal. Biochem.
353
57-62
2006
Homo sapiens
Manually annotated by BRENDA team
Puzer, L.; Cotrin, S.S.; Alves, M.F.; Egborge, T.; Araujo, M.S.; Juliano, M.A.; Juliano, L.; Broemme, D.; Carmona, A.K.
Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L
Arch. Biochem. Biophys.
430
274-283
2004
Homo sapiens
Manually annotated by BRENDA team
Hwang, S.R.; Stoka, V.; Turk, V.; Hook, V.
Resistance of cathepsin L compared to elastase to proteolysis when complexed with the serpin endopin 2C, and recovery of cathepsin L activity
Biochem. Biophys. Res. Commun.
340
1238-1243
2006
Homo sapiens
Manually annotated by BRENDA team
Meh, P.; Pavsic, M.; Turk, V.; Baici, A.; Lenarcic, B.
Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: specific inhibitor and substrate of cathepsin L
Biol. Chem.
386
75-83
2005
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Chou, P.M.; Mirkin, B.L.; Rebbaa, A.
Senescence-initiated reversal of drug resistance: specific role of cathepsin L
Cancer Res.
64
1773-1780
2004
Homo sapiens
Manually annotated by BRENDA team
Bylaite, M.; Moussali, H.; Marciukaitiene, I.; Ruzicka, T.; Walz, M.
Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases
Exp. Dermatol.
15
110-118
2006
Homo sapiens
Manually annotated by BRENDA team
Laurent-Matha, V.; Derocq, D.; Prebois, C.; Katunuma, N.; Liaudet-Coopman, E.
Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B
J. Biochem.
139
363-371
2006
Homo sapiens
Manually annotated by BRENDA team
Cheng, T.; Hitomi, K.; van Vlijmen-Willems, I.M.; de Jongh, G.J.; Yamamoto, K.; Nishi, K.; Watts, C.; Reinheckel, T.; Schalkwijk, J.; Zeeuwen, P.L.
Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification
J. Biol. Chem.
281
15893-15899
2006
Homo sapiens
Manually annotated by BRENDA team
Marquis, R.W.; James, I.; Zeng, J.; Trout, R.E.; Thompson, S.; Rahman, A.; Yamashita, D.S.; Xie, R.; Ru, Y.; Gress, C.J.; Blake, S.; Lark, M.A.; Hwang, S.M.; Tomaszek, T.; Offen, P.; Head, M.S.; Cummings, M.D.; Veber, D.F.
Azepanone-based inhibitors of human cathepsin L
J. Med. Chem.
48
6870-6878
2005
Homo sapiens
Manually annotated by BRENDA team
Urbich, C.; Heeschen, C.; Aicher, A.; Sasaki, K.; Bruhl, T.; Farhadi, MR.; Vajkoczy, P.; Hofmann, W.K.; Peters, C.; Pennacchio, L.A.; Abolmaali, N.D.; Chavakis, E.; Reinheckel, T.; Zeiher, A.M.; Dimmeler, S.
Cathepsin L is required for endothelial progenitor cell-induced neovascularization
Nat. Med.
11
206-213
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Wang, S.Q.; Du, Q.S.; Zhao, K.; Li, A.X.; Wei, D.Q.; Chou, K.C.
Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy
Amino Acids
33
129-135
2007
Homo sapiens
Manually annotated by BRENDA team
Fairhead, M.; Kelly, S.M.; van der Walle, C.F.
A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
Biochem. Biophys. Res. Commun.
366
862-867
2008
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Goulet, B.; Truscott, M.; Nepveu, A.
A novel proteolytically processed CDP/Cux isoform of 90 kDa is generated by cathepsin L
Biol. Chem.
387
1285-1293
2006
Homo sapiens
Manually annotated by BRENDA team
Caserman, S.; Kenig, S.; Sloane, B.F.; Lah, T.T.
Cathepsin L splice variants in human breast cell lines
Biol. Chem.
387
629-634
2006
Homo sapiens
Manually annotated by BRENDA team
Sevenich, L.; Pennacchio, L.A.; Peters, C.; Reinheckel, T.
Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice
Biol. Chem.
387
885-891
2006
Homo sapiens
Manually annotated by BRENDA team
Vicik, R.; Busemann, M.; Gelhaus, C.; Stiefl, N.; Scheiber, J.; Schmitz, W.; Schulz, F.; Mladenovic, M.; Engels, B.; Leippe, M.; Baumann, K.; Schirmeister, T.
Aziridide-based inhibitors of cathepsin L: synthesis, inhibition activity, and docking studies
ChemMedChem
1
1126-1141
2006
Homo sapiens
Manually annotated by BRENDA team
Spira, D.; Stypmann, J.; Tobin, D.J.; Petermann, I.; Mayer, C.; Hagemann, S.; Vasiljeva, O.; Guenther, T.; Schuele, R.; Peters, C.; Reinheckel, T.
Cell type-specific functions of the lysosomal protease cathepsin L in the heart
J. Biol. Chem.
282
37045-37052
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Novinec, M.; Grass, R.N.; Stark, W.J.; Turk, V.; Baici, A.; Lenarcic, B.
Interaction between human cathepsins K, L, and S and elastins: mechanism of elastinolysis and inhibition by macromolecular inhibitors
J. Biol. Chem.
282
7893-7902
2007
Homo sapiens
Manually annotated by BRENDA team
Sever, S.; Altintas, M.M.; Nankoe, S.R.; Moeller, C.C.; Ko, D.; Wei, C.; Henderson, J.; del Re, E.C.; Hsing, L.; Erickson, A.; Cohen, C.D.; Kretzler, M.; Kerjaschki, D.; Rudensky, A.; Nikolic, B.; Reiser, J.
Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease
J. Clin. Invest.
117
2095-2104
2007
Homo sapiens (P07711)
Manually annotated by BRENDA team
Chowdhury, S.F.; Joseph, L.; Kumar, S.; Tulsidas, S.R.; Bhat, S.; Ziomek, E.; Menard, R.; Sivaraman, J.; Purisima, E.O.
Exploring inhibitor binding at the S subsites of cathepsin L
J. Med. Chem.
51
1361-1368
2008
Homo sapiens
Manually annotated by BRENDA team
Yang, M.; Zhang, Y.; Pan, J.; Sun, J.; Liu, J.; Libby, P.; Sukhova, G.K.; Doria, A.; Katunuma, N.; Peroni, O.D.; Guerre-Millo, M.; Kahn, B.B.; Clement, K.; Shi, G.P.
Cathepsin L activity controls adipogenesis and glucose tolerance
Nat. Cell Biol.
9
970-977
2007
Homo sapiens
Manually annotated by BRENDA team
Fairhead, M.; van der Walle, C.F.
The heavy-light chain loop of human cathepsin-L modulates its activity and stability
Protein Pept. Lett.
15
47-53
2008
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Lecaille, F.; Chowdhury, S.; Purisima, E.; Broemme, D.; Lalmanach, G.
The S2 subsites of cathepsins K and L and their contribution to collagen degradation
Protein Sci.
16
662-670
2007
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Li, X.; Peng, D.; Tan, Z.; Liu, H.; Qing, Y.; Xue, Y.; Shi, G.P.
Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease
Am. J. Cardiol.
103
476-481
2009
Homo sapiens
Manually annotated by BRENDA team
Li, W.; Kornmark, L.; Jonasson, L.; Forssell, C.; Yuan, X.M.
Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
Atherosclerosis
202
92-102
2009
Homo sapiens
Manually annotated by BRENDA team
Jean, D.; Rousselet, N.; Frade, R.
Cathepsin L expression is up-regulated by hypoxia in human melanoma cells: role of its 5-untranslated region
Biochem. J.
413
125-134
2008
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Chu, F.; Mirkin, B.L.; Sudha, T.; Mousa, S.A.; Rebbaa, A.
Role of the proteolytic hierarchy between cathepsin L, cathepsin D and caspase-3 in regulation of cellular susceptibility to apoptosis and autophagy
Biochim. Biophys. Acta
1783
2294-2300
2008
Homo sapiens
Manually annotated by BRENDA team
Takahashi, K.; Ueno, T.; Tanida, I.; Minematsu-Ikeguchi, N.; Murata, M.; Kominami, E.
Characterization of CAA0225, a novel inhibitor specific for cathepsin L, as a probe for autophagic proteolysis
Biol. Pharm. Bull.
32
475-479
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Myers, M.C.; Shah, P.P.; Beavers, M.P.; Napper, A.D.; Diamond, S.L.; Smith, A.B.; Huryn, D.M.
Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype
Bioorg. Med. Chem. Lett.
18
3646-3651
2008
Homo sapiens
Manually annotated by BRENDA team
Irie, O.; Ehara, T.; Iwasaki, A.; Yokokawa, F.; Sakaki, J.; Hirao, H.; Kanazawa, T.; Teno, N.; Horiuchi, M.; Umemura, I.; Gunji, H.; Masuya, K.; Hitomi, Y.; Iwasaki, G.; Nonomura, K.; Tanabe, K.; Fukaya, H.; Kosaka, T.; Snell, C.R.; Hallett, A.
Discovery of selective and nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
3959-3962
2008
Homo sapiens
Manually annotated by BRENDA team
Irie, O.; Yokokawa, F.; Ehara, T.; Iwasaki, A.; Iwaki, Y.; Hitomi, Y.; Konishi, K.; Kishida, M.; Toyao, A.; Masuya, K.; Gunji, H.; Sakaki, J.; Iwasaki, G.; Hirao, H.; Kanazawa, T.; Tanabe, K.; Kosaka, T.; Hart, T.W.; Hallett, A.
4-Amino-2-cyanopyrimidines: novel scaffold for nonpeptidic cathepsin S inhibitors
Bioorg. Med. Chem. Lett.
18
4642-4646
2008
Homo sapiens (P07711)
Manually annotated by BRENDA team
Irie, O.; Kosaka, T.; Kishida, M.; Sakaki, J.; Masuya, K.; Konishi, K.; Yokokawa, F.; Ehara, T.; Iwasaki, A.; Iwaki, Y.; Hitomi, Y.; Toyao, A.; Gunji, H.; Teno, N.; Iwasaki, G.; Hirao, H.; Kanazawa, T.; Tanabe, K.; Hiestand, P.C.; Malcangio, M.; Fox, A.J.; Bevan, S.J.; Yaqoob, M.; Culshaw, A.J.; Hart, T.W.; Hallet, A.
Overcoming hERG issues for brain-penetrating cathepsin S inhibitors: 2-cyanopyrimidines. Part 2
Bioorg. Med. Chem. Lett.
18
5280-5284
2008
Homo sapiens (P07711)
Manually annotated by BRENDA team
Ayesa, S.; Lindquist, C.; Agback, T.; Benkestock, K.; Classon, B.; Henderson, I.; Hewitt, E.; Jansson, K.; Kallin, A.; Sheppard, D.; Samuelsson, B.
Solid-phase parallel synthesis and SAR of 4-amidofuran-3-one inhibitors of cathepsin S: effect of sulfonamides P3 substituents on potency and selectivity
Bioorg. Med. Chem.
17
1307-1324
2009
Homo sapiens
Manually annotated by BRENDA team
Herszenyi, L.; Farinati, F.; Cardin, R.; Istvan, G.; Molnar, L.D.; Hritz, I.; De Paoli, M.; Plebani, M.; Tulassay, Z.
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer
BMC Cancer
8
194
2008
Homo sapiens
Manually annotated by BRENDA team
Fairhead, M.; Johnson, K.A.; Kowatz, T.; McMahon, S.A.; Carter, L.G.; Oke, M.; Liu, H.; Naismith, J.H.; van der Walle, C.F.
Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras
Chem. Commun. (Camb. )
15
1765-1767
2008
Homo sapiens (P07711)
Manually annotated by BRENDA team
Hook, V.; Funkelstein, L.; Toneff, T.; Mosier, C.; Hwang, S.R.
Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin
Endocrine
35
429-437
2009
Homo sapiens
Manually annotated by BRENDA team
dos Reis, F.C.; Smith, B.O.; Santos, C.C.; Costa, T.F.; Scharfstein, J.; Coombs, G.H.; Mottram, J.C.; Lima, A.P.
The role of conserved residues of chagasin in the inhibition of cysteine peptidases
FEBS Lett.
582
485-490
2008
Homo sapiens
Manually annotated by BRENDA team
Thomas, V.; Samanta, S.; Fikrig, E.
Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function
Infect. Immun.
76
4905-4912
2008
Homo sapiens
Manually annotated by BRENDA team
Sullivan, S.; Tosetto, M.; Kevans, D.; Coss, A.; Wang, L.; ODonoghue, D.; Hyland, J.; Sheahan, K.; Mulcahy, H.; OSullivan, J.
Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer
Int. J. Cancer
125
54-61
2009
Homo sapiens
Manually annotated by BRENDA team
Mihelic, M.; Dobersek, A.; Guncar, G.; Turk, D.
Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation
J. Biol. Chem.
283
14453-14460
2008
Homo sapiens, Homo sapiens (P07711), Mus musculus, Mus musculus (P06797)
Manually annotated by BRENDA team
Abboud-Jarrous, G.; Atzmon, R.; Peretz, T.; Palermo, C.; Gadea, B.B.; Joyce, J.A.; Vlodavsky, I.
Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
J. Biol. Chem.
283
18167-18176
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Cailhier, J.F.; Sirois, I.; Laplante, P.; Lepage, S.; Raymond, M.A.; Brassard, N.; Prat, A.; Iozzo, R.V.; Pshezhetsky, A.V.; Hebert, M.J.
Caspase-3 activation triggers extracellular cathepsin L release and endorepellin proteolysis
J. Biol. Chem.
283
27220-27229
2008
Homo sapiens
Manually annotated by BRENDA team
Beavers, M.P.; Myers, M.C.; Shah, P.P.; Purvis, J.E.; Diamond, S.L.; Cooperman, B.S.; Huryn, D.M.; Smith, A.B.
Molecular docking of cathepsin L inhibitors in the binding site of papain
J. Chem. Inf. Model.
48
1464-1472
2008
Homo sapiens (P07711)
Manually annotated by BRENDA team
Yadav, M.R.; Shinde, A.K.; Chouhan, B.S.; Giridhar, R.; Menard, R.
Peptidomimetic 2-cyanopyrrolidines as potent selective cathepsin L inhibitors
J. Enzyme Inhib. Med. Chem.
23
190-197
2008
Homo sapiens
Manually annotated by BRENDA team
Irie, O.; Kosaka, T.; Ehara, T.; Yokokawa, F.; Kanazawa, T.; Hirao, H.; Iwasaki, A.; Sakaki, J.; Teno, N.; Hitomi, Y.; Iwasaki, G.; Fukaya, H.; Nonomura, K.; Tanabe, K.; Koizumi, S.; Uchiyama, N.; Bevan, S.J.; Malcangio, M.; Gentry, C.; Fox, A.J.; Yaqoob, M.; Culshaw, A.J.; Allan Hallett, A.J.
Discovery of orally bioavailable cathepsin S inhibitors for the reversal of neuropathic pain
J. Med. Chem.
51
5502-5505
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Urbich, C.; Dernbach, E.; Roessig, L.; Zeiher, A.M.; Dimmeler, S.
High glucose reduces cathepsin L activity and impairs invasion of circulating progenitor cells
J. Mol. Cell. Cardiol.
45
429-436
2008
Homo sapiens
Manually annotated by BRENDA team
Tang, Q.; Cai, J.; Shen, D.; Bian, Z.; Yan, L.; Wang, Y.X.; Lan, J.; Zhuang, G.Q.; Ma, W.Z.; Wang, W.
Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3beta signaling
J. Mol. Med.
87
249-260
2009
Homo sapiens
Manually annotated by BRENDA team
Porotto, M.; Orefice, G.; Yokoyama, C.; Mungall, B.; Realubit, R.; Sganga, M.; Aljofan, M.; Whitt, M.; Glickman, F.; Moscona, A.
Simulating henipavirus multicycle replication in a screening assay leads to identification of a promising candidate for therapy
J. Virol.
83
5148-5155
2009
Homo sapiens
Manually annotated by BRENDA team
Zhu, S.; Wei, L.; Yamasaki, K.; Gallo, R.L.
Activation of cathepsin L by the cathelin-like domain of protegrin-3
Mol. Immunol.
45
2531-2536
2008
Homo sapiens
Manually annotated by BRENDA team
Shah, P.P.; Myers, M.C.; Beavers, M.P.; Purvis, J.E.; Jing, H.; Grieser, H.J.; Sharlow, E.R.; Napper, A.D.; Huryn, D.M.; Cooperman, B.S.; Smith, A.B.; Diamond, S.L.
Kinetic characterization and molecular docking of a novel, potent, and selective slow-binding inhibitor of human cathepsin L
Mol. Pharmacol.
74
34-41
2008
Homo sapiens
Manually annotated by BRENDA team
Haecker, H.G.; Grundmann, F.; Lohr, F.; Ottersbach, P.A.; Zhou, J.; Schnakenburg, G.; Guetschow, M.
2-Amino- and 2-alkylthio-4H-3,1-benzothiazin-4-ones: synthesis, interconversion and enzyme inhibitory activities
Molecules
14
378-402
2009
Homo sapiens
Manually annotated by BRENDA team
Park, Y.; Kong, J.Y.; Cho, H.
A furanquinone from Paulownia tomentosa stem for a new cathepsin K inhibitor
Phytother. Res.
23
1485-1488
2009
Homo sapiens
Manually annotated by BRENDA team
Hill, J.J.; Moreno, M.J.; Lam, J.C.; Haqqani, A.S.; Kelly, J.F.
Identification of secreted proteins regulated by cAMP in glioblastoma cells using glycopeptide capture and label-free quantification
Proteomics
9
535-549
2009
Homo sapiens
Manually annotated by BRENDA team
Sevenich, L.; Hagemann, S.; Stoeckle, C.; Tolosa, E.; Peters, C.; Reinheckel, T.
Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice
Biochimie
92
1674-1680
2010
Homo sapiens
Manually annotated by BRENDA team
Coppini, L.P.; Barros, N.M.; Oliveira, M.; Hirata, I.Y.; Alves, M.F.; Paschoalin, T.; Assis, D.M.; Juliano, M.A.; Puzer, L.; Broemme, D.; Carmona, A.K.
Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor
Biol. Chem.
391
561-570
2010
Homo sapiens
Manually annotated by BRENDA team
Huryn, D.M.; Smith, A.B.
The identification, characterization and optimization of small molecule probes of cysteine proteases: experiences of the Penn center for molecular discovery with cathepsin B and cathepsin L
Curr. Top. Med. Chem.
9
1206-1216
2009
Homo sapiens
Manually annotated by BRENDA team
See, V.; Free, P.; Cesbron, Y.; Nativo, P.; Shaheen, U.; Rigden, D.J.; Spiller, D.G.; Fernig, D.G.; White, M.R.; Prior, I.A.; Brust, M.; Lounis, B.; Levy, R.
Cathepsin L digestion of nanobioconjugates upon endocytosis
ACS Nano
3
2461-2468
2009
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Chu, F.; Chou, P.; Gallati, C.; Dier, U.; Mirkin, B.; Mousa, S.; Rebbaa, A.
Cathepsin L inhibition suppresses drug resistance in vitro and in vivo: A putative mechanism
Am. J. Physiol. Cell Physiol.
296
C65-C74
2009
Homo sapiens
Manually annotated by BRENDA team
Hsu, K.F.; Wu, C.L.; Huang, S.C.; Wu, C.M.; Hsiao, J.R.; Yo, Y.T.; Chen, Y.H.; Shiau, A.L.; Chou, C.Y.
Cathepsin L mediates resveratrol-induced autophagy and apoptotic cell death in cervical cancer cells
Autophagy
5
451-460
2009
Homo sapiens
Manually annotated by BRENDA team
Ueno, T.; Takahashi, K.
A cathepsin L-specific inhibitor preferentially inhibits degradation of autophagosomal LC3 and GABARAP in HeLa and Huh-7 cells
Autophagy
5
878-879
2009
Homo sapiens
Manually annotated by BRENDA team
Fortenberry, Y.M.; Brandal, S.; Bialas, R.C.; Church, F.C.
Protein C inhibitor regulates both cathepsin L activity and cell-mediated tumor cell migration
Biochim. Biophys. Acta
1800
580-590
2010
Homo sapiens
Manually annotated by BRENDA team
Schilling, K.; Krner, A.; Sehmisch, S.; Kreusch, A.; Kleint, R.; Benedix, Y.; Schlabrakowski, A.; Wiederanders, B.
Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases
Biol. Chem.
390
167-174
2009
Homo sapiens
Manually annotated by BRENDA team
Leto, G.; Sepporta, M.V.; Crescimanno, M.; Flandina, C.; Tumminello, F.M.
Cathepsin L in metastatic bone disease: therapeutic implications
Biol. Chem.
391
655-664
2010
Homo sapiens
Manually annotated by BRENDA team
Asaad, N.; Bethel, P.A.; Coulson, M.D.; Dawson, J.E.; Ford, S.J.; Gerhardt, S.; Grist, M.; Hamlin, G.A.; James, M.J.; Jones, E.V.; Karoutchi, G.I.; Kenny, P.W.; Morley, A.D.; Oldham, K.; Rankine, N.; Ryan, D.; Wells, S.L.; Wood, L.; Augustin, M.; Krapp, S.; Simader, H.; Steinbacher, S.
Dipeptidyl nitrile inhibitors of Cathepsin L
Bioorg. Med. Chem. Lett.
19
4280-4283
2009
Homo sapiens
Manually annotated by BRENDA team
Kishore Kumar, G.D.; Chavarria, G.E.; Charlton-Sevcik, A.K.; Arispe, W.M.; Macdonough, M.T.; Strecker, T.E.; Chen, S.E.; Siim, B.G.; Chaplin, D.J.; Trawick, M.L.; Pinney, K.G.
Design, synthesis, and biological evaluation of potent thiosemicarbazone based cathepsin L inhibitors
Bioorg. Med. Chem. Lett.
20
1415-1419
2010
Homo sapiens
Manually annotated by BRENDA team
Martinez, O.; Johnson, J.; Manicassamy, B.; Rong, L.; Olinger, G.G.; Hensley, L.E.; Basler, C.F.
Zaire Ebola virus entry into human dendritic cells is insensitive to cathepsin L inhibition
Cell. Microbiol.
12
148-157
2010
Homo sapiens
Manually annotated by BRENDA team
Biswas, N.; Rodriguez-Flores, J.L.; Courel, M.; Gayen, J.R.; Vaingankar, S.M.; Mahata, M.; Torpey, J.W.; Taupenot, L.; OConnor, D.T.; Mahata, S.K.
Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides
Endocrinology
150
3547-3557
2009
Homo sapiens
Manually annotated by BRENDA team
Klose, A.; Wilbrand-Hennes, A.; Brinckmann, J.; Hunzelmann, N.
Alternate trafficking of cathepsin L in dermal fibroblasts induced by UVA radiation
Exp. Dermatol.
19
e117-e123
2010
Homo sapiens
Manually annotated by BRENDA team
Xu, X.; Yuan, G.; Liu, W.; Zhang, Y.; Chen, W.
Expression of cathepsin L in nasopharyngeal carcinoma and its clinical significance
Exp. Oncol.
31
102-105
2009
Homo sapiens
Manually annotated by BRENDA team
Wartmann, T.; Mayerle, J.; Kaehne, T.; Sahin-Toth, M.; Ruthenbuerger, M.; Matthias, R.; Kruse, A.; Reinheckel, T.; Peters, C.; Weiss, F.U.; Sendler, M.; Lippert, H.; Schulz, H.U.; Aghdassi, A.; Dummer, A.; Teller, S.; Halangk, W.; Lerch, M.M.
Cathepsin L inactivates human trypsinogen, whereas cathepsin L-deletion reduces the severity of pancreatitis in mice
Gastroenterology
138
726-737
2010
Homo sapiens
Manually annotated by BRENDA team
Konjar, S.; Sutton, V.R.; Hoves, S.; Repnik, U.; Yagita, H.; Reinheckel, T.; Peters, C.; Turk, V.; Turk, B.; Trapani, J.A.; Kopitar-Jerala, N.
Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L
Immunology
131
257-267
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ceru, S.; Konjar, S.; Maher, K.; Repnik, U.; Krizaj, I.; Bencina, M.; Renko, M.; Nepveu, A.; Zerovnik, E.; Turk, B.; Kopitar-Jerala, N.
Stefin B interacts with histones and cathepsin L in the nucleus
J. Biol. Chem.
285
10078-10086
2010
Homo sapiens
Manually annotated by BRENDA team
Higgins, W.J.; Fox, D.M.; Kowalski, P.S.; Nielsen, J.E.; Worrall, D.M.
Heparin enhances serpin inhibition of the cysteine protease cathepsin L
J. Biol. Chem.
285
3722-3729
2010
Homo sapiens
Manually annotated by BRENDA team
Puchi, M.; Garcia-Huidobro, J.; Cordova, C.; Aguilar, R.; Dufey, E.; Imschenetzky, M.; Bustos, P.; Morin, V.
A new nuclear protease with cathepsin L properties is present in Hela and Caco-2 cells
J. Cell. Biochem.
111
1099-1106
2010
Homo sapiens
Manually annotated by BRENDA team
Shenoy, R.T.; Chowdhury, S.F.; Kumar, S.; Joseph, L.; Purisima, E.O.; Sivaraman, J.
A combined crystallographic and molecular dynamics study of cathepsin L retrobinding inhibitors
J. Med. Chem.
52
6335-6346
2009
Homo sapiens (P07711)
Manually annotated by BRENDA team
Gibbons, A.; McElvaney, N.; Taggart, C.; Cryan, S.
Delivery of rSLPI in a liposomal carrier for inhalation provides protection against cathepsin L degradation
J. Microencapsul.
26
513-522
2009
Homo sapiens
Manually annotated by BRENDA team
Hood, C.L.; Abraham, J.; Boyington, J.C.; Leung, K.; Kwong, P.D.; Nabel, G.J.
Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity
J. Virol.
84
2972-2982
2010
Homo sapiens
Manually annotated by BRENDA team
Lankelma, J.M.; Voorend, D.M.; Barwari, T.; Koetsveld, J.; Van der Spek, A.H.; De Porto, A.P.; Van Rooijen, G.; Van Noorden, C.J.
Cathepsin L, target in cancer treatment?
Life Sci.
86
225-233
2010
Homo sapiens
Manually annotated by BRENDA team
Urbanelli, L.; Trivelli, F.; Ercolani, L.; Sementino, E.; Magini, A.; Tancini, B.; Franceschini, R.; Emiliani, C.
Cathepsin L increased level upon Ras mutants expression: the role of p38 and p44/42 MAPK signaling pathways
Mol. Cell. Biochem.
343
49-57
2010
Homo sapiens
Manually annotated by BRENDA team
Shah, P.P.; Wang, T.; Kaletsky, R.L.; Myers, M.; Puvis, J.E.; Jing, H.; Huryn, D.M.; Greenbaum, D.C.; Smith, A.B.; Bates, P.; Diamond, S.L.
A small molecule oxocarbazate inhibitor of human cathepsin L blocks SARS and Ebola pseudotype virus infection into HEK 293T cells
Mol. Pharmacol.
78
319-324
2010
Homo sapiens
Manually annotated by BRENDA team
Sansanwal, P.; Shukla, A.A.; Das, T.K.; Chauhan, S.S.
Truncated human cathepsin L, encoded by a novel splice variant, exhibits altered subcellular localization and cytotoxicity
Protein Pept. Lett.
17
238-245
2010
Homo sapiens (Q9HBQ7), Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, M.; Tahara, Y.; Makino, T.; Shimizu, T.; Date, A.
Comparison of cathepsin L activity in cheek and forearm stratum corneum in young female adults
Skin Res. Technol.
15
370-375
2009
Homo sapiens
Manually annotated by BRENDA team
Yoshii, H.; Kamiyama, H.; Minematsu, K.; Goto, K.; Mizota, T.; Oishi, K.; Katunuma, N.; Yamamoto, N.; Kubo, Y.
Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells
Virology
394
227-234
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Diederich, S.; Dietzel, E.; Maisner, A.
Nipah virus fusion protein: influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin
Virus Res.
145
300-306
2009
Homo sapiens
Manually annotated by BRENDA team
Shenoy, R.T.; Sivaraman, J.
Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors
J. Struct. Biol.
173
14-19
2011
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Adams-Cioaba, M.A.; Krupa, J.C.; Xu, C.; Mort, J.S.; Min, J.
Structural basis for the recognition and cleavage of histone H3 by cathepsin L
Nat. Commun.
2
197
2011
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Legowska, M.; Wysocka, M.; Burster, T.; Pikula, M.; Rolka, K.; Lesner, A.
Ultrasensitive internally quenched substrates of human cathepsin L
Anal. Biochem.
466
30-37
2014
Homo sapiens
Manually annotated by BRENDA team
Torkar, A.; Lenarcic, B.; Lah, T.; Dive, V.; Devel, L.
Identification of new peptide amides as selective cathepsin L inhibitors: the first step towards selective irreversible inhibitors?
Bioorg. Med. Chem. Lett.
23
2968-2973
2013
Homo sapiens
Manually annotated by BRENDA team
Ramalho, S.D.; De Sousa, L.R.; Nebo, L.; Maganhi, S.H.; Caracelli, I.; Zukerman-Schpector, J.; Lima, M.I.; Alves, M.F.; Da Silva, M.F.; Fernandes, J.B.; Vieira, P.C.
Triterpenoids as novel natural inhibitors of human cathepsin L
Chem. Biodivers.
11
1354-1363
2014
Homo sapiens
Manually annotated by BRENDA team
Pietra, D.; Borghini, A.; Ricci, C.; Bianucci, A.M.
Enzyme kinetics studies on 29-kDa human liver cathepsin L
Chem. Biol. Drug Des.
84
648-658
2014
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Tamhane, T.; Lllukkumbura, R.; Lu, S.; Maelandsmo, G.M.; Haugen, M.H.; Brix, K.
Nuclear cathepsin L activity is required for cell cycle progression of colorectal carcinoma cells
Biochimie
122
208-218
2016
Homo sapiens (P07711)
Manually annotated by BRENDA team
Dana, D.; Garcia, J.; Bhuiyan, A.I.; Rathod, P.; Joo, L.; Novoa, D.A.; Paroly, S.; Fath, K.R.; Chang, E.J.; Pathak, S.K.
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L
Bioorg. Chem.
85
505-514
2019
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Parker, E.N.; Song, J.; Kishore Kumar, G.D.; Odutola, S.O.; Chavarria, G.E.; Charlton-Sevcik, A.K.; Strecker, T.E.; Barnes, A.L.; Sudhan, D.R.; Wittenborn, T.R.; Siemann, D.W.; Horsman, M.R.; Chaplin, D.J.; Trawick, M.L.; Pinney, K.G.
Synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L
Bioorg. Med. Chem.
23
6974-6992
2015
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Jefferson, T.; McShan, D.; Warfield, J.; Ogungbe, I.V.
Screening and identification of inhibitors of Trypanosoma brucei cathepsin L with antitrypanosomal activity
Chem. Biol. Drug Des.
87
154-158
2016
Homo sapiens (P07711), Homo sapiens, Trypanosoma brucei brucei (Q95PM0), Trypanosoma brucei rhodesiense (Q95PM0), Trypanosoma brucei brucei 427 (Q95PM0)
Manually annotated by BRENDA team
Pranjol, M.Z.I.; Gutowski, N.J.; Hannemann, M.; Whatmore, J.L.
Cathepsin L induces proangiogenic changes in human omental microvascular endothelial cells via activation of the ERK1/2 pathway
Curr. Cancer Drug Targets
19
231-242
2019
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Korenc, M.; Lenarcic, B.; Novinec, M.
Human cathepsin L, a papain-like collagenase without proline specificity
FEBS J.
282
4328-4340
2015
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Sosnowski, P.; Turk, D.
Caught in the act the crystal structure of cleaved cathepsin L bound to the active site of cathepsin L
FEBS Lett.
590
1253-1261
2016
Homo sapiens (P07711)
Manually annotated by BRENDA team
Cao, Y.; Liu, X.; Li, Y.; Lu, Y.; Zhong, H.; Jiang, W.; Chen, A.F.; Billiar, T.R.; Yuan, H.; Cai, J.
Cathepsin L activity correlates with proteinuria in chronic kidney disease in humans
Int. Urol. Nephrol.
49
1409-1417
2017
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team
Hashimoto, Y.; Kondo, C.; Katunuma, N.
An active 32-kDa cathepsin L is secreted directly from HT 1080 fibrosarcoma cells and not via lysosomal exocytosis
PLoS ONE
10
e0145067
2015
Homo sapiens (P07711), Homo sapiens
Manually annotated by BRENDA team