HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.4.22.15 - cathepsin L
for references in articles please use BRENDA:EC3.4.22.15Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.22.15 cathepsin LSpecify your search results
Word Map
- 3.4.22.15
- cathepsins
- lysosomal
- proteinases
- papain
- cystatins
- metastasis
- fasciola
- collagen
- peptidase
- tmprss2
-
b-like
- fluke
- cruzain
-
surimi
-
metacercariae
-
trematode
- proforms
- medicine
-
procathepsin
- pharmacology
- legumain
-
ii-associated
-
elastinolytic
- kininogens
-
helminth
- endolysins
- microplus
-
asparaginyl
- coronavirus
-
excretory-secretory
-
fasciolosis
-
sars-cov
- pepstatin
- azocasein
- gigantica
-
fluorogenic
-
papain-like
- prodomains
-
collagenolytic
- drug development
- heparanase
-
proregions
- hepatica
- endosomal
- trypanosoma
-
stefins
- calpains
- osteoclast
- proenzyme
-
excysted
- propeptide
- diagnostics
- leupeptin
- endopeptidases
The enzyme appears in 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
AgCatL, Aldrichina grahami cysteine proteinase, cat L, Cat L-A, Cath L, cath-L, cathepsin L, cathepsin L isoform CRA-b, cathepsin L-A, cathepsin L-A1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aldrichina grahami cysteine proteinase
-
-
-
-
cat L
Cath L
cathepsin L
cathepsin L isoform CRA-b
splice variant encoding a truncated form of cathepsin L
cathepsin L-like protein
cathepsin L1
cathepsin-L
CathL
CatL
CPL
cpl-1
CtL
CTSL
Cwp84
major excreted protein
-
-
-
-
MEP
-
-
-
-
PDP
-
-
-
-
progesterone-dependent protein
-
-
-
-
SMCL1
-
-
-
-
cathepsin L
-
-
CatL
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
60616-82-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
3-carboxypropionyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
48 kDa intermediate of cathepsin D + H2O
34 kDa mature cathepsin D + ?
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ala-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Gln-3-nitrotyrosineamide
-
-
-
-
?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ser-3-nitrotyrosineamide
-
-
-
-
?
acetyl-AGPRNAA-N-methyl amide + H2O
acetyl-AGPR + NAA-N-methyl amide
docking study
-
-
?
actomyosin + H2O
?
-
endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
benzoyl-Phe-Ala-Arg-4-methoxy-2-naphtylamide + H2O
benzoyl-Phe-Ala-Arg + 4-methoxy-2-naphthylamine
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
28.61% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-citrulline-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-L-citrulline 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu + 7-amino-4-methylcoumarin
76.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
cathepsin L specific synthetic substrate
-
-
?
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Lys-Gln-Lys-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
preferred substrate
-
-
?
benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Phe-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin + H2O
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
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 + ?
-
-
-
-
?
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
the substrate is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment, respectively. The cleavage site is between amino acid residues 214 and 261
-
-
?
dynamin + H2O
?
CatL is highly reactive toward recombinant dynamin at pH 5.0 and 6.0
-
-
?
FabA antibody + H2O
?
model protein, determination of fragments compared to the recombinant murine enzyme
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
28.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
L-arginine 7-amido-4-methylcoumarin + H2O
?
-
very poor substrate
-
-
?
L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
L-Val-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Val-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Tyr-7-amido-4-methylcoumarin + H2O
Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-Phe-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Phe-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-2-(4-methoxynaphthylamide) + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-carbobenzoxy-L-arginine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
7% of the activity with N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin
-
-
?
N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
precursor form 77IL-8 of interleukin-8 + H2O
precursor form 72IL-8 of interleukin-8 + ?
-
cleavage between Arg5 and Ser6
-
?
pro-neuropeptide Y + H2O
neuropeptide Y + ?
cathepsin L cleaves pro-neuropeptide Y (1-70) to generate neuropeptide Y-Gly (1-38) and the COOH-terminal peptide fragment (39-70)
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
secretory leukocyte protease inhibitor + H2O
?
-
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
?
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')
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Val-Pro-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
1% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
thyroglobulin type-1 domain + H2O
?
-
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
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
trypsinogen + H2O
trypsin + ?
-
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)
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg-Ile
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe + H2O
?
-
cleavage sites: Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe-NH2 + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Z-Val-Val-Arg-AMC + H2O
Z-Val-Val-Arg + 7-amino-4-methylcoumarin
a cathepsin L-specific substrate
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
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
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
no activity
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
7% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
no activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
9% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
88.77% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
preferred substrate
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
most efficient substrate
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Collagen + H2O
?
-
selective cleavage of terminal peptides leads to conversion of beta- and higher components mainly to alpha-chains
-
-
?
Collagen + H2O
?
-
conversion of cross-linked beta-chain dimers into uncross-linked alpha-chain monomers
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Elastin + H2O
?
-
the enzyme shows distinctive preferences in degrading elastins from bovine neck ligament, aorta, and lung
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
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
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate
-
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
Gelatin + H2O
?
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
histone H3 + H2O
?
-
during embryonic stem cell differentiation, histone H3 is proteolytically cleaved at its N-terminus. H3 cleavage may be regulated by covalent modifications present on the histone tail itself
-
-
?
Insulin B-chain + H2O
?
-
preferential cleavage at: Glu13-Ala14, Leu17-Val18, and Tyr26-Thr27
-
-
?
Insulin B-chain + H2O
?
-
main cleavage sites: Glu13-Ala14 and Tyr26-Thr27, minor cleavage sites: Val2-Asn3, Asn3-Gln4, Cys7-Glu8, Tyr16-Leu17, Leu17-Val18
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL5
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
Nipah virus fusion protein + H2O
?
-
cathepsin L specifically converts Nipah virus fusion protein to a mature and fusogenic form
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
proheparanase + H2O
active form of heparanase + ?
-
removal of the linker peptide and conversion of proheparanase into its active 8 + 50-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
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL1G
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
type 1 collagen + H2O
?
-
isoform Catl1G completely digests collagen type 1
-
-
?
type 1 collagen + H2O
?
-
efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Met-Arg-Arg
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
-
-
?
additional information
?
-
no activity with benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin. The recombinant CsCPL-m can degrade bovine serum albumin and gelatin, but can not degrade human hemoglobin and human immunoglobulin G
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin. The recombinant CsCPL-m can degrade bovine serum albumin and gelatin, but can not degrade human hemoglobin and human immunoglobulin G
-
-
?
additional information
?
-
proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
-
-
?
additional information
?
-
-
proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
-
-
?
additional information
?
-
proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
-
-
?
additional information
?
-
owing to its low specificity, cathepsin L is able to cleave a diversity of proteins, it cleaves a variety of recombinant proteins including monoclonal antibodies, antibody fragments, bispecific antibodies, and fusion proteins. Cathepsin L is a low specificity protease. CHO cathepsin L seems to have preferential cleavage sites on mAbs of different subclass as similar fragment profiles exist for three tested mAbs. IgG1 does not interact with cathepsin L
-
-
?
additional information
?
-
-
owing to its low specificity, cathepsin L is able to cleave a diversity of proteins, it cleaves a variety of recombinant proteins including monoclonal antibodies, antibody fragments, bispecific antibodies, and fusion proteins. Cathepsin L is a low specificity protease. CHO cathepsin L seems to have preferential cleavage sites on mAbs of different subclass as similar fragment profiles exist for three tested mAbs. IgG1 does not interact with cathepsin L
-
-
?
additional information
?
-
-
enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
-
?
additional information
?
-
-
3% with benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin and 1% with both L-Arg-7-amido-4-methylcoumarin and Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin. No activity with Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin and succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the cathepsin B and H specific synthetic substrates benzyloxycarbonyl-L-Ala-L-Ala-7-amido-4-trifluoromethylcoumarin and L-Arg-7-amido-4-methylcoumarin do not show any hydrolysis with the partially purified enzyme
-
-
?
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2, isoform CatL1G is unable to digest albumin or hemoglobin, efficiently at either pH 5.5 or 7.0
-
-
?
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2
-
-
?
additional information
?
-
analysis of substrate specificity of FhCL3, strong preference of the cathepsin for Pro and Gly residues at P2 and P3 sites, respectively, of substrates. Residues residues, Q19, G23, G25, W26, G67, W69, Y143, T161, H162 and W184, of FhCL3 largely contribute to the substrate binding. W69, Y143 and T161 have the largest per-residue free energy contributions to the complex formation, interaction analysis, overview
-
-
?
additional information
?
-
-
analysis of substrate specificity of FhCL3, strong preference of the cathepsin for Pro and Gly residues at P2 and P3 sites, respectively, of substrates. Residues residues, Q19, G23, G25, W26, G67, W69, Y143, T161, H162 and W184, of FhCL3 largely contribute to the substrate binding. W69, Y143 and T161 have the largest per-residue free energy contributions to the complex formation, interaction analysis, overview
-
-
?
additional information
?
-
the enzyme performs autocleavage of its proform
-
-
?
additional information
?
-
the enzyme performs autocleavage of its proform
-
-
?
additional information
?
-
-
the enzyme performs autocleavage of its proform
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-Phe-Ala-4-methylcoumarin 7-amide and with benzyloxycarbonyl-Phe-Met-4-methylcoumarin 7-amide
-
-
?
additional information
?
-
-
the enzyme is involved in tissue destruction in arthritis
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in the degradation of the invariant chain during maturation of major histocompatibility complex class II molecules and antigen processing
-
-
?
additional information
?
-
-
differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
-
-
?
additional information
?
-
-
CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
-
-
?
additional information
?
-
-
cathepsin L has a pro-survival function within the cell which may be due, at least in part, to its ability to deplete the cells from the proapoptotic molecule caspase-3. The existence of a proteolytic hierarchy between pro-survival and pro-death proteases suggests that changes in cellular proteolytic profiles are likely to have significant consequences not only on its survival but also on the type of death it may undergo in response to a specific stress
-
-
?
additional information
?
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
-
-
?
additional information
?
-
-
contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins in HeLa and Huh-7 cells are nearly equal. Cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers
-
-
?
additional information
?
-
-
pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine , Ortho-aminobenzoic acid-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, and ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
-
?
additional information
?
-
human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
-
-
?
additional information
?
-
-
human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
-
-
?
additional information
?
-
the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
-
-
?
additional information
?
-
-
the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
-
-
?
additional information
?
-
the enzyme performs autocatalytic cleavage
-
-
?
additional information
?
-
no activity towards benzyloxycarbonyl-Gly-Gly-L-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
p4165aa, a 65 amino acid segment of the p41 splice variant of major histocompatibility complex class II-associated invariant chain, stabilizes cathepsin L in the extracellular environment and induces a local decrease in the concentration of matrix-degrading enzymes during inflammation. Through its interaction with cathepsin L, complex class II-associated invariant chain Ii may control the migratory response of antigen-presenting cells and/or the recruitment of effectors of the inflammatory response
-
?
additional information
?
-
upon interferon-gamma activation of peritoneal macrophages, enzymatic activityof cathepsin L is specifically inhibited, such that cathepsin S mediates Ii degradation and regulates MHC class II maturation
-
?
additional information
?
-
-
cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides
-
-
?
additional information
?
-
-
cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
-
-
?
additional information
?
-
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
additional information
?
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
additional information
?
-
-
the enzyme has a preference for hydrophobic amino acids in P2 and P3 residues
-
-
?
additional information
?
-
-
the enzyme removes the Ca-sensitivity of ATPase activity of myofibrils
-
-
?
additional information
?
-
-
involved in extracellular food digestion
-
-
?
additional information
?
-
the recombinant enzyme is inefficient in hydrolyzing azocasein, fibrinogen, and bovine serum albumin
-
-
?
additional information
?
-
-
the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
-
-
?
additional information
?
-
-
plays a crucial role in the pathogenesis of adjuvant arthritis
-
-
?
additional information
?
-
-
basement membrane of larval brains contains two substrate proteins
-
?
additional information
?
-
-
the enzyme is suggested to play a crucial role in the degradation of the basement membranes
-
?
additional information
?
-
no activity with human immunoglobulin
-
-
?
additional information
?
-
-
enzyme has a role in the progress of the cell cycle during the cleavage divisions of embryonic development. Inhibition of the protease abolishes the chromatin decondensation after mitosis
-
-
?
additional information
?
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
?
additional information
?
-
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
?
additional information
?
-
-
leucine is preferred over phenylalanine in position P2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
actomyosin + H2O
?
-
endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
the substrate is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment, respectively. The cleavage site is between amino acid residues 214 and 261
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
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
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
secretory leukocyte protease inhibitor + H2O
?
-
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
-
-
?
trypsinogen + H2O
trypsin + ?
-
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
-
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
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
-
?
Gelatin + H2O
?
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
histone H3 + H2O
?
-
during embryonic stem cell differentiation, histone H3 is proteolytically cleaved at its N-terminus. H3 cleavage may be regulated by covalent modifications present on the histone tail itself
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
removal of the linker peptide and conversion of proheparanase into its active 8 + 50-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
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
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
-
-
?
type 1 collagen + H2O
?
-
isoform Catl1G completely digests collagen type 1
-
-
?
type 1 collagen + H2O
?
-
efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
-
-
?
additional information
?
-
-
enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
-
-
?
additional information
?
-
-
enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
-
?
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2, isoform CatL1G is unable to digest albumin or hemoglobin, efficiently at either pH 5.5 or 7.0
-
-
?
additional information
?
-
-
isoform CatL1G can cleave substrates with proline residues at P2
-
-
?
additional information
?
-
-
the enzyme is involved in tissue destruction in arthritis
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in the degradation of the invariant chain during maturation of major histocompatibility complex class II molecules and antigen processing
-
-
?
additional information
?
-
-
differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
-
-
?
additional information
?
-
-
CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
-
-
?
additional information
?
-
-
cathepsin L has a pro-survival function within the cell which may be due, at least in part, to its ability to deplete the cells from the proapoptotic molecule caspase-3. The existence of a proteolytic hierarchy between pro-survival and pro-death proteases suggests that changes in cellular proteolytic profiles are likely to have significant consequences not only on its survival but also on the type of death it may undergo in response to a specific stress
-
-
?
additional information
?
-
catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
-
-
?
additional information
?
-
-
contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins in HeLa and Huh-7 cells are nearly equal. Cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers
-
-
?
additional information
?
-
-
pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
-
-
?
additional information
?
-
-
p4165aa, a 65 amino acid segment of the p41 splice variant of major histocompatibility complex class II-associated invariant chain, stabilizes cathepsin L in the extracellular environment and induces a local decrease in the concentration of matrix-degrading enzymes during inflammation. Through its interaction with cathepsin L, complex class II-associated invariant chain Ii may control the migratory response of antigen-presenting cells and/or the recruitment of effectors of the inflammatory response
-
?
additional information
?
-
upon interferon-gamma activation of peritoneal macrophages, enzymatic activityof cathepsin L is specifically inhibited, such that cathepsin S mediates Ii degradation and regulates MHC class II maturation
-
?
additional information
?
-
-
cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides
-
-
?
additional information
?
-
-
cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
-
-
?
additional information
?
-
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
additional information
?
-
cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
-
-
?
additional information
?
-
-
involved in extracellular food digestion
-
-
?
additional information
?
-
-
the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
-
-
?
additional information
?
-
-
plays a crucial role in the pathogenesis of adjuvant arthritis
-
-
?
additional information
?
-
-
the enzyme is suggested to play a crucial role in the degradation of the basement membranes
-
?
additional information
?
-
-
enzyme has a role in the progress of the cell cycle during the cleavage divisions of embryonic development. Inhibition of the protease abolishes the chromatin decondensation after mitosis
-
-
?
additional information
?
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
?
additional information
?
-
-
granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
(2E)-1,3-diphenylprop-2-en-1-one
33% inhibition of FhCL1; 4% inhibition of FhCL3
(2E)-1-(2-hydroxyphenyl)-3-(3-nitrophenyl)prop-2-en-1-one
26% inhibition of FhCL1; 37% inhibition of FhCL3
(2E)-1-(2-hydroxyphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one
3% inhibition of FhCL3; 48% inhibition of FhCL1
(2E)-1-(2-hydroxyphenyl)-3-(4-phenoxyphenyl)prop-2-en-1-one
16% inhibition of FhCL3; 8% inhibition of FhCL1
(2E)-1-(2-hydroxyphenyl)-3-(pyridin-2-yl)prop-2-en-1-one
20% inhibition of FhCL19; 54% inhibition of FhCL1
(2E)-1-(2-hydroxyphenyl)-3-(thiophen-2-yl)prop-2-en-1-one
52% inhibition of FhCL1; 9% inhibition of FhCL3
(2E)-1-(2-hydroxyphenyl)-3-phenylprop-2-en-1-one
16% inhibition of FhCL2
(2E)-1-(2-hydroxyphenyl)-3-[4-(methylsulfanyl)phenyl]prop-2-en-1-one
19% inhibition of FhCL3
(2E)-1-(7-hydroxynaphthalen-1-yl)-3-(naphthalen-1-yl)prop-2-en-1-one
a slow-reversible inhibitor that interacts with the Cys-His catalytic dyad and key S2 and S3 pocket residues, causing 65% inhibition of FhCL3, enzyme binding structure by molecular docking, overview. Analysis of fasciolicide activity of C34 on vitro cultu; a slow-reversible inhibitor that interacts with the Cys-His catalytic dyad and key S2 and S3 pocket residues, causing 75% inhibition of FhCL1, enzyme binding structure by molecular docking, overview. Analysis of fasciolicide activity of C34 on vitro cultu
(2E)-1-(7-hydroxynaphthalen-1-yl)-3-(naphthalen-2-yl)prop-2-en-1-one
44% inhibition of FhCL3; 67% inhibition of FhCL1
(2E)-1-(8-hydroxynaphthalen-2-yl)-3-(naphthalen-2-yl)prop-2-en-1-one
29% inhibition of FhCL3; 65% inhibition of FhCL1
(2E)-1-(naphthalen-2-yl)-3-phenylprop-2-en-1-one
13% inhibition of FhCL3; 65% inhibition of FhCL1
(2E)-1-phenyl-3-(pyridin-2-yl)prop-2-en-1-one
4% inhibition of FhCL3; 8% inhibition of FhCL1
(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-[(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-(trifluoromethyl)phenyl]methylidene]hydrazinecarbothioamide
-
-
(2E)-2-[(3-bromophenyl)[4-(trifluoromethyl)phenyl]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)-3-(1,3-benzodioxol-5-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
11% inhibition of FhCL1; 19% inhibition of FhCL3
(2E)-3-(2-bromophenyl)-1-(2-hydroxyphenyl)prop-2-en-1-one
29% inhibition of FhCL1; 33% inhibition of FhCL3
(2E)-3-(3,4-dimethoxyphenyl)-1-phenylprop-2-en-1-one
2% inhibition of FhCL3; 35% inhibition of FhCL1
(2E)-3-(4-aminophenyl)-1-phenylprop-2-en-1-one
2% inhibition of FhCL3; 4% inhibition of FhCL1
(2E)-3-(4-bromophenyl)-1-(2-hydroxyphenyl)prop-2-en-1-one
12% inhibition of FhCL3; 19% inhibition of FhCL1
(2E)-3-(4-bromophenyl)-1-phenylprop-2-en-1-one
12% inhibition of FhCL3; 52% inhibition of FhCL1
(2E)-3-(4-chlorophenyl)-1-(2-hydroxyphenyl)prop-2-en-1-one
23% inhibition of FhCL3; 63% inhibition of FhCL1
(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-one
25% inhibition of FhCL1; 6% inhibition of FhCL43
(2E)-3-(4-methoxyphenyl)-1-phenylprop-2-en-1-one
48% inhibition of FhCL1; 4% inhibition of FhCL3
(2E)-3-(furan-2-yl)-1-(2-hydroxyphenyl)prop-2-en-1-one
4% inhibition of FhCL3; 57% inhibition of FhCL1
(2E)-3-(naphthalen-1-yl)-1-phenylprop-2-en-1-one
17% inhibition of FhCL1; 27% inhibition of FhCL3
(2E)-3-[4-(dimethylamino)phenyl]-1-(2-hydroxyphenyl)prop-2-en-1-one
20% inhibition of FhCL3; 34% inhibition of FhCL1
(2E)-3-[4-(methylsulfanyl)phenyl]-1-phenylprop-2-en-1-one
26% inhibition of FhCL3; 8% inhibition of FhCL1
(2E)-N'-(2-[(naphthalen-1-ylmethyl)sulfanyl]acetyl)-3-phenylprop-2-enehydrazide
-
(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-[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]
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
0.1 mM
(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-[(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-[[3,5-bis(trifluoromethyl)phenyl](4-methylphenyl)methylidene]hydrazinecarbothioamide
-
-
(3-bromo-3'-hydroxybenzophenone) thiosemicarbazone
a slowly reversible inhibitor of cathepsin L
(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
(E)N-[(S)1-[(S)2-cyano-1-pyrrolidinecarbonyl]-3-methylbutyl]-2,3-diphenylacrylamide
-
selective towards cathepsin L over cathepsin B
(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucine(3-methylbutyl)-amide
-
0.01 mg/ml
(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
-
CA-074Me, more than 99% inhibition at 0.1 mM
(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-bis(2-fluorobenzoyl)-5-bromobenzene thiosemicarbazone
molecular docking in the active site
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- (L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane
-
i.e. E-64, 0.1 mM, complete loss of activity
1-hydroxy-6-[(1E)-3-oxo-3-phenylprop-1-en-1-yl]-2,1,3-benzoxadiazol-1-ium
21% inhibition of FhCL1; 26% inhibition of FhCL3
1-N-[3,5-bis (trifluoromethyl) phenyl]-2-N-(1-ethynylcyclohexyl) benzene-1,2-dicarboxamide
-
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
1-[(1E)-3-phenylprop-1-en-1-yl]naphthalene
38% inhibition of FhCL1; 39% inhibition of FhCL3
2,3,7,8-tetrachlorodibenzodioxin
-
treatment of cells results in resistance to apoptosis, increased expression of the tumor marker cathepsin L, and a high degree of invasiveness
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-(4-bromophenyl)-4H-chromen-4-one
19% inhibition of FhCL3; 21% inhibition of FhCL1
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-(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-([4-benzyl-5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl)-1-(1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one
-
2-cyano-4-(2-hydroxyethoxy)-N-methyl-6-[(spiro[3.5]non-7-ylmethyl)amino]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-hydroxy-4-[(1E)-3-(2-hydroxyphenyl)-3-oxoprop-1-en-1-yl]-1,2,5-oxadiazol-2-ium
14% inhibition of FhCL3; 48% inhibition of FhCL1
2-phenyl-4H-chromen-4-one
5% inhibition of FhCL1; 8% inhibition of FhCL3
2-[(1E)-3-phenylprop-1-en-1-yl]naphthalene
38% inhibition of FhCL3; 62% inhibition of FhCL1
2-[(2E)-3-(naphthalen-1-yl)prop-2-en-1-yl]phenol
32% inhibition of FhCL3; 42% inhibition of FhCL1
2-[(2E)-3-(naphthalen-2-yl)prop-2-en-1-yl]phenol
41% inhibition of FhCL3; 61% inhibition of FhCL1
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-chloro-N-[(2S)-3-(3-chlorophenyl)-1-[(cyanomethyl)amino]-1-oxopropan-2-yl]benzamide
-
pH and temperature not specified in the publication
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-(2,5-dimethyl-1H-pyrrol-1-yl)-N'-(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)benzohydrazide
-
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-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