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Information on EC 3.4.22.43 - cathepsin V and Organism(s) Homo sapiens and UniProt Accession P07711

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.43 cathepsin V
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P07711 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
cathepsin v, ctsl2, stratum corneum thiol protease, cathepsin v/l2, cathepsin-v, cathepsin l2/v, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cathepsin L2
cathepsin L2/V
-
-
cathepsin like 2
-
cathepsin U
cathepsin V/L2
-
-
cathepsin-V
-
CatV
-
-
CTSL2
CV/L2
-
-
stratum corneum thiol protease
-
-
additional information
-
the enzyme belongs to the C1A peptidase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
223670-00-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
best substrate
-
-
?
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + SIKQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
best substrate
-
-
?
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KLRSXKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + SXKQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
X is varied with diverse amino acids, highest activity with Ile, kinetics, detailed overview
-
-
?
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KLRXSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + XSKQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
X is varied with diverse amino acids, highest activity with Val, kinetics, detailed overview
-
-
?
2-aminobenzoyl-KLXSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLX + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
X is varied with diverse amino acids, highest activity with Arg, kinetics, detailed overview
-
-
?
2-aminobenzoyl-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-KPPVV + LLPDQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-KPVS + TEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-KXRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
X is varied with diverse amino acids, highest activity with Leu, kinetics, detailed overview
-
-
?
2-aminobenzoyl-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-LF + EKQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKKQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
selective substrate for cathepsin V when compared with cathepsins B, L, and S
-
-
?
2-aminobenzoyl-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKKVY + LQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine + H2O
2-aminobenzoyl-VLF + EKQ-N-[2,4-dinitrophenyl]ethylenediamine
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-XLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
X is varied with diverse amino acids, highest activity with Ala, kinetics, detailed overview
-
-
?
Albumin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Boc-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gly-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
kininogen fragments + H2O
?
show the reaction diagram
-
kininogenase activity with high and low molecular weight kininogens
Lys-bradykinin is the major product
-
?
MHC class II-associated invariant chain + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
very low activity
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
very low activity
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
neuropeptide Y + H2O
?
show the reaction diagram
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
proenkephalin + H2O
(Met)enkephalin + ?
show the reaction diagram
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
cleavage of telopeptide region
-
-
?
Z-Arg-Arg-4-methoxy-2-nitroanilide + H2O
Z-Arg-Arg + 4-methoxy-2-nitroaniline
show the reaction diagram
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Leu-Arg-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-4-methylcoumarin-7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
neuropeptide Y + H2O
?
show the reaction diagram
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
proenkephalin + H2O
(Met)enkephalin + ?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
stimulates at 0.3 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
-
odanacatib
-
(1R)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1R)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1S)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
(1S)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
-
less than 10% residual activity at 0.001 mM
1,3,5-trihydroxy-2,8-bis(3-methylbut-2-enyl)-10-methyl-9-acridone
-
-
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
-
-
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
-
-
2-[butyl(dichloro)-l4-tellanyl]benzyl methyl ether
-
about 10% residual activity at 0.001 mM
2-[dibromo(butyl)-l4-tellanyl]benzyl methyl ether
-
less than 10% residual activity at 0.001 mM
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
-
-
4-methylpiperazine-1-carboxylic acid [1-[(3-benzenesulfonyl-1-phenethylallyl)carbamoyl]-2-phenylethyl]amide
-
i.e. APC-3316
4-morpholincarbonyl-Leu-homophenylalaninevinyl sulfone-phenyl
-
5-hydroxynoracronycine
-
-
calpeptin
cathepsin V propeptide
CatV PP, tight-binding inhibitor
-
chondroitin 4-sulfate
-
specific inhibition of elastolytic activity, formation of specific complexes with the enzyme, no inhibition of the activity with Z-Phe-Arg-4-methyl-7-coumaryl amide
chymostatin
-
citibrasine
-
-
citrusinine-I
-
-
citrusinine-II
-
-
clitocypin
-
-
cystatin
-
cystatin C
endogenous inhibitor of cathepsin V analyzed, expression of cystatin C increased in stenotic valves, cystatin C protein particularly found in areas with infiltrates of inflammatory cells
-
cystatin M/E
-
cystatins
-
-
-
fragment p41 of major histocompatibility complex class II-associated invariant chain
-
inhibitory to human cathepsin V, cathepsin L, cathepsin K, cathepsin F with Ki values in the low nanomolar range. Ki values are sufficiently low to ensure complex formation at physiological concentrations. Regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation
-
glycocitrine-I
-
-
glycocitrine-IV
-
-
iodoacetic acid
-
leupeptin
macrocypin-1
-
-
morpholineurea-leucyl-homophenylalanine-vinylsulfone phenyl
-
-
morpholineurea-naphthyl-homophenylalanine-vinylsulfone naphthyl
-
-
-
N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
peptidl vinyl sulfones
-
-
-
pyranofoline
-
-
saquinavir
SQV, the HIV protease inhibitor Inhibits the interaction between cathepsin V and the TLR4-MyD88 receptor complex, also blocks disulfide HMGB1-induced TLR4 activation
serpin
cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA
-
STO33438
334, a mammalian protease inhibitor, inhibits cathepsin V, also blocks disulfide HMGB1-induced TLR4 activation
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
VBY-825
-
reversible cathepsin inhibitor with high potency against cathepsins V
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the recombinant proenzyme is autocatalytically activated in vitro by incubation at pH 4.0 and 30°C
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0017
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.002
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0008
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0006
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0012
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0006
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.0044
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
0.0024
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
0.0041 - 0.0048
Z-Phe-Arg-4-methyl-7-coumaryl amide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.3
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.6
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.7
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.5
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
1.3
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
0.9
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37°C
156
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
19
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
3.4 - 3.7
Z-Phe-Arg-4-methyl-7-coumaryl amide
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
496
2-aminobenzoyl-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
903
2-aminobenzoyl-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
4528
2-aminobenzoyl-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
3055
2-aminobenzoyl-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
6833
2-aminobenzoyl-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, pH 5.5
4277
2-aminobenzoyl-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37°C, in 0.1 M sodium acetate buffer, pH 5.5
35000
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
7900
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
1,3,5-trihydroxy-2,8-bis(3-methylbut-2-enyl)-10-methyl-9-acridone
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0005
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0044
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0017
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0102
cathepsin V propeptide
varying concentrations tested
-
0.0002
citibrasine
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.001
citrusinine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0042
citrusinine-II
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.00000008
clitocypin
pH and temperature not specified in the publication
-
0.00000047
cystatin M/E
-
pH and temperature not specified in the publication
-
0.0000000072
fragment p41 of major histocompatibility complex class II-associated invariant chain
-
pH 6.0, 25°C
-
0.01
glycocitrine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0011
glycocitrine-IV
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.00000069
macrocypin-1
pH and temperature not specified in the publication
-
0.00000034
mutant N64A cystatin M/E
-
pH 5.5, 22°C
-
0.00000025
VBY-825
-
apparent value, in 50 mM MES pH 6.5, 2.5 mM DTT, 2.5 mM EDTA, 100 mM NaCl, 0.01% (w/v) bovine serum albumin, and 10% (v/v) DMSO, at 25°C
0.00000047
wild-type cystatin M/E
-
pH 5.5, 22°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.000016
N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.00091
N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.046
N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.0006
odanacatib
Homo sapiens
50 mM MES pH 5.5, 25 mM EDTA and 2.5 mM DTT. 0.05% Tween 20 (v/v), 37°C
0.0039
1,3,5-trihydroxy-2,8-bis(3-methylbut-2-enyl)-10-methyl-9-acridone
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0025
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0052
2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0028
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.048
5-hydroxynoracronycine
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0012
citibrasine
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0022
citrusinine-I
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.01
citrusinine-II
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.025
glycocitrine-I
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.0022
glycocitrine-IV
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
0.044
pyranofoline
Homo sapiens
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
-
-
5.5 - 6.5
-
assay at
6.5
plasminogen digestion assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
cathepsin V is active at pH 4.0 and 6.0
4 - 7.2
less than 50% of maximal activity above and below
additional information
-
bell-shaped pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression in aorta valve, control valves and stenotic valves analyzed
Manually annotated by BRENDA team
cathepsin V localized to endothelial cells in areas rich of neovascularization
Manually annotated by BRENDA team
-
ZR-75-1, Hs-578T, MDA-MB435
Manually annotated by BRENDA team
from healthy subjects and Besnier-Boeck-Schaumann (BBS) disease patients, the latter show decreased cathepsin V concentrations, while contents of endostatin, an inhibitor of lung epithelial cells, are increased
Manually annotated by BRENDA team
recombinant human cathepsin V for inhibition studies, N-terminal propeptide domains as inhibitors of cathepsin V
Manually annotated by BRENDA team
-
thymic and corneal
Manually annotated by BRENDA team
-
in the human thymic cortex, CTSV is the predominately expressed protease
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
cathepsin V is located on the outside of the nucleus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATL1_HUMAN
333
0
37564
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23000
-
x * 23000, nonglycosylated form, SDS-PAGE
23999
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
24000
31000
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
35000
35500
-
proprotein, SDS-PAGE
37000
37330
preproprotein, containing a 17 amino acid signal peptide, a 96 amino acid propeptide and a 221 amino acid mature region, calculation from sequence of cDNA
39000
-
glycosylated enzyme form, SDS-PAGE
41000
-
glycosylated enzyme form, SDS-PAGE
52000
-
recombinant GST-tagged enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 23999, amino acid sequence calculation of the mature enzyme, 2 * 31000, recombinant mature enzyme from insect cells and Pichia pastoris, 2 * 38000-45000, recombinant proenzyme from Pichi pastoris
additional information
-
three-dimensional two-domain structure analysis at 1.6 A resolution, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cathepsin V in complex with clitocypin, vapor diffusion method, using 0.4 M Li2SO4, 12% (w/v) polyethylene glycol 800, 20% (v/v) glycerol
molecular modeling of complex with fragment p41 of major histocompatibility complex class II-associated invariant chain
-
space group P6422, crystal structure at 1.6 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5.5
-
very stable
668763
6.5
2 h, residual acitviy
137269
7
1 h, residual acitviy
137269
additional information
-
rapid loss of activity at neutral pH
668763
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
pH 5.5, loss of 60% activity within 20 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, pre-activated before use
gel filtration, recombinant human cathepsin V
Ni-NTA column chromatography
recombinant enzyme from Pichia pastoris to homogeneity, activated mature native enzyme by hyrophobic interaction chromatography, recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography
-
recombinant enzyme from Pichia pastoris, further purified by gel filtration after activation by pepsin treatment
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cathepsin V with mutated glycosylation site is expressed in Pichia pastoris
-
expressed in Escherichia coli
expressed in Pichia pastoris
expressed in thymus of transgenic Mus musculus
-
expression in Escherichia coli
-
expression in Pichia pastoris
from cDNA libraries, the gene maps to chromosome 9q21, DNA and amino acid sequence determination and analysis, genomic organization, expression in insect cells using the baculovirus system, in Pichia pastoris, and as GST-tagged enzyme with low activity in Escherichia coli
-
gene CTSV, real-time PCR enzyme expression analysis
human cathepsins V expressed in Pichia pastoris
recombinant human cathepsin V produced using the Pichia pastoris expression system
recombinant procathepsin V is expressed in soluble form in the cytoplasm of Escherichia coli Rosetta-gami B (DE3) pLysS cells
transgenic expression in cathepsin L-deficient mice, phylogenetic tree
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CTSL2 transcript levels are strongly elevated in endometrial cancer, particularly in G3 tumors
E2F1 activates cathepsin like 2 gene promoter activity
L-homocysteine induces cathepsin V expression, L-homocysteine promoted cathepsin V expression in HUVECs. Methylation of the promoter region of cathepsin V is decreased following L-Hcy stimulation
siRNA-cathepsin V inhibits the up-regulation of cathepsin V-induced by L-homocysteine
there is decreased expression of cathepsin V in lesional atopic dermatitis and psoriasis epidermis at the mRNA level as well as the protein level
-
tissue necrosis factor alpha increases cathepsin V expression and activity by 2fold. Tissue necrosis factor alpha and co-culturing with THP-1 monocytes stimulates a 460% increase in cathepsin V active enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
the enzyme is a potential marker for certain colon tumors and breast cancer
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brmme, D.; Li, Z.; Barnes, M.; Mehler, E.
Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
Biochemistry
38
2377-2385
1999
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Adachi, W.; Kawamoto, S.; Ohno, I.; Nishida, K.; Kinoshita, S.; Matsubara, K.; Okubo, K.
Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium
Invest. Ophthalmol. Vis. Sci.
39
1789-1796
1998
Homo sapiens
Manually annotated by BRENDA team
Santamaria, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; Lopez-Otin, C.
Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
Cancer Res.
58
1624-1630
1998
Homo sapiens
Manually annotated by BRENDA team
Somoza, J.R.; Zhan, H.; Bowman, K.K.; Yu, L.; Mortara, K.D.; Palmer, J.T.; Clark, J.M.; McGrath, M.E.
Crystal structure of human cathepsin V
Biochemistry
39
12543-12551
2000
Homo sapiens
Manually annotated by BRENDA team
Puzer, L.; Cotrin, S.S.; Alves, M.F.; Egborge, T.; Araujo, M.S.; Juliano, M.A.; Juliano, L.; Broemme, D.; Carmona, A.K.
Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L
Arch. Biochem. Biophys.
430
274-283
2004
Homo sapiens
Manually annotated by BRENDA team
Hagemann, S.; Guenther, T.; Dennemaerker, J.; Lohmueller, T.; Broemme, D.; Schuele, R.; Peters, C.; Reinheckel, T.
The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles
Eur. J. Cell Biol.
83
775-780
2004
Homo sapiens
Manually annotated by BRENDA team
Broemme, D.
Cathepsin V
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2nd Ed.
1107-1109
2004
Homo sapiens
-
Manually annotated by BRENDA team
Kenney, M.C.; Chwa, M.; Atilano, S.R.; Tran, A.; Carballo, M.; Saghizadeh, M.; Vasiliou, V.; Adachi, W.; Brown, D.J.
Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder
Invest. Ophthalmol. Vis. Sci.
46
823-832
2005
Homo sapiens
Manually annotated by BRENDA team
Yasuda, Y.; Li, Z.; Greenbaum, D.; Bogyo, M.; Weber, E.; Broemme, D.
Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
J. Biol. Chem.
279
36761-36770
2004
Homo sapiens
Manually annotated by BRENDA team
Cheng, T.; Hitomi, K.; van Vlijmen-Willems, I.M.; de Jongh, G.J.; Yamamoto, K.; Nishi, K.; Watts, C.; Reinheckel, T.; Schalkwijk, J.; Zeeuwen, P.L.
Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification
J. Biol. Chem.
281
15893-15899
2006
Homo sapiens
Manually annotated by BRENDA team
Zeeuwen, P.L.; Ishida-Yamamoto, A.; van Vlijmen-Willems, I.M.; Cheng, T.; Bergers, M.; Iizuka, H.; Schalkwijk, J.
Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation
J. Invest. Dermatol.
127
120-128
2006
Homo sapiens
Manually annotated by BRENDA team
Helske, S.; Syvaeranta, S.; Lindstedt, K.A.; Lappalainen, J.; Oeoerni, K.; Maeyraenpaeae, M.I.; Lommi, J.; Turto, H.; Werkkala, K.; Kupari, M.; Kovanen, P.T.
Increased Expression of Elastolytic Cathepsins S, K, and V and Their Inhibitor Cystatin C in Stenotic Aortic Valves
Arterioscler. Thromb. Vasc. Biol.
26
1791-1798
2006
Homo sapiens (O60911)
Manually annotated by BRENDA team
Burden, R.E.; Snoddy, P.; Jefferies, C.A.; Walker, B.; Scott, C.J.
Inhibition of cathepsin L-like proteases by cathepsin V propeptide
Biol. Chem.
388
541-545
2007
Homo sapiens (O60911)
Manually annotated by BRENDA team
Puzer, L.; Barros, N.M.; Paschoalin, T.; Hirata, I.Y.; Tanaka, A.S.; Oliveira, M.C.; Broemme, D.; Carmona, A.K.
Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
Biol. Chem.
389
195-200
2008
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Ong, P.C.; McGowan, S.; Pearce, M.C.; Irving, J.A.; Kan, W.T.; Grigoryev, S.A.; Turk, B.; Silverman, G.A.; Brix, K.; Bottomley, S.P.; Whisstock, J.C.; Pike, R.N.
DNA accelerates the inhibition of human cathepsin V by serpins
J. Biol. Chem.
282
36980-36986
2007
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Mihelic, M.; Dobersek, A.; Guncar, G.; Turk, D.
Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation
J. Biol. Chem.
283
14453-14460
2008
Homo sapiens
Manually annotated by BRENDA team
Elie, B.T.; Gocheva, V.; Shree, T.; Dalrymple, S.A.; Holsinger, L.J.; Joyce, J.A.
Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model
Biochimie
92
1618-1624
2010
Homo sapiens
Manually annotated by BRENDA team
Sevenich, L.; Hagemann, S.; Stoeckle, C.; Tolosa, E.; Peters, C.; Reinheckel, T.
Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice
Biochimie
92
1674-1680
2010
Homo sapiens
Manually annotated by BRENDA team
Coppini, L.P.; Barros, N.M.; Oliveira, M.; Hirata, I.Y.; Alves, M.F.; Paschoalin, T.; Assis, D.M.; Juliano, M.A.; Puzer, L.; Broemme, D.; Carmona, A.K.
Plasminogen hydrolysis by cathepsin S and identification of derived peptides as selective substrate for cathepsin V and cathepsin L inhibitor
Biol. Chem.
391
561-570
2010
Homo sapiens
Manually annotated by BRENDA team
Cheng, T.; Tjabringa, G.S.; van Vlijmen-Willems, I.M.; Hitomi, K.; van Erp, P.E.; Schalkwijk, J.; Zeeuwen, P.L.
The cystatin M/E-controlled pathway of skin barrier formation: expression of its key components in psoriasis and atopic dermatitis
Br. J. Dermatol.
161
253-264
2009
Homo sapiens
Manually annotated by BRENDA team
Renko, M.; Sabotic, J.; Mihelic, M.; Brzin, J.; Kos, J.; Turk, D.
Versatile loops in mycocypins inhibit three protease families
J. Biol. Chem.
285
308-316
2010
Homo sapiens (O60911)
Manually annotated by BRENDA team
Zeeuwen, P.L.; Cheng, T.; Schalkwijk, J.
The biology of cystatin M/E and its cognate target proteases
J. Invest. Dermatol.
129
1327-1338
2009
Homo sapiens
Manually annotated by BRENDA team
Wilder, C.L.; Park, K.Y.; Keegan, P.M.; Platt, M.O.
Manipulating substrate and pH in zymography protocols selectively distinguishes cathepsins K, L, S, and V activity in cells and tissues
Arch. Biochem. Biophys.
516
52-57
2011
Homo sapiens
Manually annotated by BRENDA team
Severino, R.P.; Guido, R.V.; Marques, E.F.; Broemme, D.; da Silva, M.F.; Fernandes, J.B.; Andricopulo, A.D.; Vieira, P.C.
Acridone alkaloids as potent inhibitors of cathepsin V
Bioorg. Med. Chem.
19
1477-1481
2011
Homo sapiens
Manually annotated by BRENDA team
Piovan, L.; Alves, M.F.; Juliano, L.; Broemme, D.; Cunha, R.L.; Andrade, L.H.
Structure-activity relationships of hypervalent organochalcogenanes as inhibitors of cysteine cathepsins V and S
Bioorg. Med. Chem.
19
2009-2014
2011
Homo sapiens
Manually annotated by BRENDA team
Skrzypczak, M.; Springwald, A.; Lattrich, C.; Haering, J.; Schueler, S.; Ortmann, O.; Treeck, O.
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes
Cancer Invest.
30
398-403
2012
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Funkelstein, L.; Lu, W.D.; Koch, B.; Mosier, C.; Toneff, T.; Taupenot, L.; O'Connor, D.T.; Reinheckel, T.; Peters, C.; Hook, V.
Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters
J. Biol. Chem.
287
15232-15241
2012
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Keegan, P.M.; Wilder, C.L.; Platt, M.O.
Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte-endothelial cell signaling and JNK activation
Mol. Cell. Biochem.
367
65-72
2012
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Wong, C.H.; Wu, Z.; Yu, Q.
CTSL2 is a pro-apoptotic target of E2F1 and a modulator of histone deacetylase inhibitor and DNA damage-induced apoptosis
Oncogene
33
1249-1257
2014
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Novinec, M.; Pavsic, M.; Lenarcic, B.
A simple and efficient protocol for the production of recombinant cathepsin V and other cysteine cathepsins in soluble form in Escherichia coli
Protein Expr. Purif.
82
1-5
2012
Homo sapiens (O60911)
Manually annotated by BRENDA team
Naumnik, W.; Ossolinska, M.; Plonska, I.; Chyczewska, E.; Niklinski, J.
Endostatin and cathepsin-V in bronchoalveolar lavage fluid of patients with pulmonary sarcoidosis
Adv. Exp. Med. Biol.
833
55-61
2015
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Homma, T.; Kageyama, S.; Nishikawa, A.; Nagata, K.
Melanosome degradation in epidermal keratinocytes related to lysosomal protease cathepsin V
Biochem. Biophys. Res. Commun.
500
339-343
2018
Homo sapiens (O60911)
Manually annotated by BRENDA team
Leng, Y.P.; Ma, Y.S.; Li, X.G.; Chen, R.F.; Zeng, P.Y.; Li, X.H.; Qiu, C.F.; Li, Y.P.; Zhang, Z.; Chen, A.F.
L-Homocysteine-induced cathepsin V mediates the vascular endothelial inflammation in hyperhomocysteinaemia
Br. J. Pharmacol.
175
1157-1172
2018
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Huang, K.; Gao, L.; Yang, M.; Wang, J.; Wang, Z.; Wang, L.; Wang, G.; Li, H.
Exogenous cathepsin V protein protects human cardiomyocytes HCM from angiotensin II-induced hypertrophy
Int. J. Biochem. Cell Biol.
89
6-15
2017
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team
Mons, E.; Jansen, I.D.C.; Loboda, J.; van Doodewaerd, B.R.; Hermans, J.; Verdoes, M.; van Boeckel, C.A.A.; van Veelen, P.A.; Turk, B.; Turk, D.; Ovaa, H.
The Alkyne moiety as a latent electrophile in irreversible covalent small molecule inhibitors of cathepsin K
J. Am. Chem. Soc.
141
3507-3514
2019
Homo sapiens (P07711)
Manually annotated by BRENDA team
Pribis, J.P.; Al-Abed, Y.; Yang, H.; Gero, D.; Xu, H.; Montenegro, M.F.; Bauer, E.M.; Kim, S.; Chavan, S.S.; Cai, C.; Li, T.; Szoleczky, P.; Szabo, C.; Tracey, K.J.; Billiar, T.R.
The HIV protease inhibitor saquinavir inhibits HMGB1-driven inflammation by targeting the interaction of cathepsin V with TLR4/MyD88
Mol. Med.
21
749-757
2015
Homo sapiens (O60911), Homo sapiens
Manually annotated by BRENDA team