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Information on EC 3.4.22.38 - cathepsin K
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3.4.22.38 cathepsin KSpecify your search results
Word Map
- 3.4.22.38
- resorption
- osteoporosis
-
osteoclastogenesis
- rankl
-
tartrate-resistant
- osteoblast
- collagen
- nfatc1
-
rankl-induced
-
multinucleated
- mmp-9
- c-fos
-
fracture
-
trabecular
- pi
- calcitonin
- osteocalcin
- osteoprotegerin
-
osteolytic
-
resorb
- m-csf
-
collagenolytic
- bisphosphonates
-
osteoclast-mediated
-
trap-positive
-
osteoclast-specific
- odanacatib
- oscar
-
antiresorptive
- tracp
- lacuna
-
ovariectomy-induced
-
rankl-mediated
-
dc-stamp
-
bone-resorbing
-
sclerostin
-
osteoclast-related
-
telopeptide
-
osteoclast-like
-
osteoclastogenic
-
denosumab
-
preosteoclasts
-
teriparatide
- pharmacology
-
anti-osteoclastogenic
- osteosclerosis
-
anti-osteoporotic
- atp6v0d2
- medicine
-
ranelate
- drug development
-
deoxypyridinoline
-
rankl-stimulated
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
cathepsin k, cathepsin-k, cat k, cath k, cat-k, cathepsin o2, oc-2 protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cat K
cath K
cathepsin K
Cathepsin O2
catK
CTSK
OC-2 protein
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rhCK
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additional information
Cat K
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cathepsin K
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Cathepsin O2
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catK
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additional information
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cathepsin K is a member of the papain family of cysteine proteases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg
endopeptidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
94716-09-3
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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
Abz-His-Pro-Gly-Gly-Pro-Gln-EDDnp + H2O
?
-
cathepsin k is unusual among the cysteine cathepsins since it can cleave substrates with Pro in the P2 position. A specific peptide substrate for cathepsin K is developed (kcat/Km: 426000/Msec) that is resistant to proteolysis by cathepsin B, L, S, F, H,V and the serine proteases (cathepsin G, chymotrypsin and leukocyte elastase)
-
-
?
Ac-Lys-His-Pro-Lys-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
Ac-Lys-His-Pro-Lys + 7-amino-3-carbamoylmethyl-4-methylcoumarin
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assay at pH 5.5, 37°C
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-
?
Acetyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Acetyl-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
31.29% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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-
?
Benzoyl-Arg 4-methylcoumarin 7-amide + H2O
Benzoyl-Arg + 7-amino-4-methylcoumarin
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?
Benzoyl-Phe-Val-Arg 4-methylcoumarin 7-amide + H2O
Benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
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?
Benzyloxycarbonyl-Arg-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
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-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
47.92% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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-
?
Benzyloxycarbonyl-Glu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Glu-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
89.78% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
Benzyloxycarbonyl-Gly-Pro-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
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?
Benzyloxycarbonyl-Leu-Arg 4-methoxy-2-naphthylamide + H2O
Benzyloxycarbonyl-Leu-Arg + 4-methoxy-2-naphthylamine
Benzyloxycarbonyl-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
Benzyloxycarbonyl-Leu-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Leu-Glu + 7-amino-4-methylcoumarin
23.91% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
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-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
Benzyloxycarbonyl-Phe-Pro-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Pro-Arg + 7-amino-4-methylcoumarin
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-
?
Benzyloxycarbonyl-Val-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Val-Arg + 7-amino-4-methylcoumarin
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?
Benzyloxycarbonyl-Val-Val-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
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?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
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?
carbobenzoxy-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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?
carbobenzoxy-Phe-Arg-7-amido-4-methylcoumarin + H2O
carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
?
carbobenzyloxy-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
carbobenzyloxy-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
carbobenzyloxy-Leu-Arg-4-methoxy-2-naphthylamide + H2O
carbobenzyloxy-Leu-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
carbobenzyloxy-Leu-Arg-4-methylcoumaryl-7-amide + H2O
carbobenzyloxy-Leu-Arg + 7-amino-4-methylcoumarin
carbobenzyloxy-Phe-Arg-4-methylcoumaryl-7-amide + H2O
carbobenzyloxy-Phe-Arg + 7-amino-4-methylcoumarin
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?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
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?
chemo-attractant stromal-derived factor-1alpha + H2O
?
the enzyme cleaves chemo-attractant stromal-derived factor-1alpha (SDF-1alpha) at 3 sites in the N-terminus, which is the region of SDF-1alpha that binds to its receptors
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-
?
Collagen type II + H2O
Fragments of collagen type II
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cleavage near the N-terminal region within the helical domain, Pro in P2- position
?
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Ala-Leu-Lys + 7-amino-4-methylcoumarin
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?
D-Phe-Phe-Arg 4-methylcoumarin 7-amide + H2O
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
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?
Lys-Gln-Lys-Leu-Arg-4-methylcoumarin-7-amide + H2O
Lys-Gln-Lys-Leu-Arg + 7-amino-4-methylcoumarin
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?
N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
24.13% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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?
N-succinyl-Ile-Ala-7-amido-4-methylcoumarin + H2O
N-succinyl-Ile-Ala + 7-amino-4-methylcoumarin
17.34% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
25.03% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
31.57% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
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?
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-alaninamide + H2O
?
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-
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?
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucyl-L-methioninamide + H2O
?
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?
N-[(1S)-2,2,2-trifluoro-1-[4'-(methylsulfonyl)biphenyl-4-yl]ethyl]-L-leucylglycinamide + H2O
?
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-
-
-
?
Osteonectin + H2O
Fragments of osteonectin
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the cleavage products are of MW 34000 and 14000. The 34000 Da protein represents the amino-terminus of osteonectin minus three amino acids Ala-Pro-Gln. Cleavage of the Arg-Val bond in the sequence Gln-Lys-Leu-Arg-Val-Lys-Ole-His of the 14000 Da fragment. The presence of Lsu-Arg at position P2-P1 is favorable
?
Succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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?
tert-Butyloxycarbonyl-Ala-Gly-Pro-Arg 4-methylcoumarin 7-amide + H2O
tert-Butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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-
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?
tert-Butyloxycarbonyl-Phe-Val-Arg 4-methylcoumarin 7-amide + H2O
tert-Butyloxycarbonyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
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-
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?
tert-Butyloxycarbonyl-Val-Leu-Lys 4-methylcoumarin 7-amide + H2O
tert-Butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
-
-
?
tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
Tosyl-Gly-Pro-Arg 4-methylcoumarin 7-amide + H2O
Tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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?
type II collagen + H2O
?
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cathepsin K cleaves the triple helix of type II collagen
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?
Z-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Pro-Arg + 7-amino-4-methylcoumarin
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?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
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?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
Benzyloxycarbonyl-Leu-Arg 4-methoxy-2-naphthylamide + H2O
Benzyloxycarbonyl-Leu-Arg + 4-methoxy-2-naphthylamine
-
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?
Benzyloxycarbonyl-Leu-Arg 4-methoxy-2-naphthylamide + H2O
Benzyloxycarbonyl-Leu-Arg + 4-methoxy-2-naphthylamine
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?
Benzyloxycarbonyl-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
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?
Benzyloxycarbonyl-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
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?
Benzyloxycarbonyl-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
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?
Benzyloxycarbonyl-Leu-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
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-
-
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?
Benzyloxycarbonyl-Leu-Leu-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
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-
-
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?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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-
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?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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-
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?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
?
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
71.17% activity compared to benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
-
-
?
carbobenzyloxy-Leu-Arg-4-methylcoumaryl-7-amide + H2O
carbobenzyloxy-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
carbobenzyloxy-Leu-Arg-4-methylcoumaryl-7-amide + H2O
carbobenzyloxy-Leu-Arg + 7-amino-4-methylcoumarin
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-
-
?
CBZ-Phe-Arg-4-methylcoumarin 7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
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-
-
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?
CBZ-Phe-Arg-4-methylcoumarin 7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
CBZ-Phe-Arg-4-methylcoumarin 7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
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?
Collagen + H2O
?
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cathepsin K cleaves within the telo as well as triple helical domains of collagens
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?
collagen I + H2O
?
-
Cat K can degrade several bone matrix proteins including type I collagen during osteoclastic bone resorption
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?
collagen I + H2O
?
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cathepsin K is responsible for the degradation of type I collagen in osteoclast-mediated bone resorption. Cathepsin K interaction with type I collagen is required for 1. the release of cryptic Arg-Gly-Asp motifs during the initial attachment of osteoclasts and 2. termination of resorption via the creation of autocrine signals originating from type I collagen degradation, overview
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-
?
collagen I + H2O
?
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cathepsin K is the only cathepsin that can degrade native type-I collagen in a triple-helix structure
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?
collagen I + H2O
?
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osteoclasts degrade bone matrix by demineralization followed by degradation of type I collagen through secretion of the cysteine protease, cathepsin K
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-
?
collagen I + H2O
?
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the lysosomal cysteine protease cathepsin K plays a key role in the degradation of the bone matrix, Cat K deficiency leads to an increase in bone mineral density
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-
?
collagen I + H2O
?
-
cathepsin K inhibition by cathepsin K inhibitor significantly increases the bone mineral density and the bone volume of the primary and secondary spongiosa, with a reduction of the urinary C-telopeptide of type I collagen that is increased by ovariectomized surgery compared to sham surgery, respectively, overview
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-
?
collagen I + H2O
?
-
cathepsin K is responsible for the degradation of type I collagen in osteoclast-mediated bone resorption. Cathepsin K interaction with type I collagen is required for 1. the release of cryptic Arg-Gly-Asp motifs during the initial attachment of osteoclasts and 2. termination of resorption via the creation of autocrine signals originating from type I collagen degradation, overview
-
-
?
collagen I + H2O
?
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cathepsin K regulates adipocyte differentiation, possible involvement of type I collagen degradation and regulation of collagen type I expression, molecular mechanism, overview
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-
?
collagen I + H2O
?
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CatK is a cysteine protease expressed predominantly in osteoclastsosteoclasts, that plays a prominent role in degrading type I collagen. Growing CatK null mice have osteopetrosis associated with a reduced ability to degrade bone matrix
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-
?
collagen I + H2O
?
-
inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice, overview
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-
?
collagen I + H2O
?
-
osteoclasts degrade bone matrix by demineralization followed by degradation of type I collagen through secretion of the cysteine protease, cathepsin K
-
-
?
collagen I + H2O
?
-
cathepsin K is responsible for the degradation of type I collagen in osteoclast-mediated bone resorption. Cathepsin K interaction with type I collagen is required for 1. the release of cryptic Arg-Gly-Asp motifs during the initial attachment of osteoclasts and 2. termination of resorption via the creation of autocrine signals originating from type I collagen degradation, overview
-
-
?
collagen I + H2O
?
-
inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice, overview
-
-
?
collagen I + H2O
?
-
cathepsin K is the only cathepsin that can degrade native type-I collagen in a triple-helix structure
-
-
?
collagen II + H2O
?
-
cathepsin K is a cysteine protease which can also cleave the triple helix of type II collagen
-
-
?
collagen II + H2O
?
-
cathepsin K is a cysteine protease of the papain family that cleaves triple-helical type II collagen, the major structural component of the extracellular matrix of articular cartilage
-
-
?
Collagen type I + H2O
Fragemnts of collagen type I
-
-
cleavage in telopeptide region
?