Information on EC 3.4.22.43 - cathepsin V

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The expected taxonomic range for this enzyme is: Homo sapiens

EC NUMBER
COMMENTARY
3.4.22.43
-
RECOMMENDED NAME
GeneOntology No.
cathepsin V
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec)
show the reaction diagram
Cathepsin V is a human lysosomal cysteine endopeptidase of family C1, papain family that is maximally active at pH 5.7 and unstable at neutral pH. Compound E-64, leupeptin and chicken cystatin are inhibitors. Human cathepsin V shows expression restricted to thymus, testis, corneal epithelium and some colon and breast carcinomas. Human gene locus: 9q22.2; endopeptidase
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cathepsin L2
-
-
-
-
cathepsin L2
-
-
cathepsin L2/V
-
-
cathepsin U
-
-
-
-
cathepsin U
-
-
cathepsin V/L2
-
-
CatV
-
-
CTSL2
-
-
stratum corneum thiol protease
-
-
CV/L2
-
-
additional information
-
the enzyme belongs to the C1A peptidase family
CAS REGISTRY NUMBER
COMMENTARY
223670-00-6
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
expression of CTSV rescues the reduced frequency of CD4+ T cells in cysteine protease cathepsin L-deficient mice with H-2b haplotype
physiological function
-
CTSV is involved in the breakdown of corneodesmosomal proteins
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-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-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-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amido-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
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
elastin degradation activity leading to loss of elasticity in atherosclerosis, the enzyme exhibits high elastolytic cysteine protease activity
-
-
?
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
-
?
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
-, O60911
-
-
?
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
-
-
-
?
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
-
Cbz-Phe-Arg-AMC, 25 microM used for protease inhibition assay, inhibitory conditions of cathepsin V propeptide analyzed
-
-
-
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
-
mechanisms of interaction between serpins, human cathepsin V and DNA analyzed, kinetic constants for substrate cleavage in the presence and absence of cofactors determined, final concentrations of cathepsin V and ds65mer DNA at 0.1 and 10 nM, final substrate concentrations ranging from 5 to 200 microM in cathepsin V buffer
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
capability of recombinant human cathepsin V to hydrolyze plasminogen analyzed, physiological role for cathepsin V related to the control of neovascularization in cornea suggested, 4.5 microM human plasminogen and 30 nM of recombinant human cathepsins V used for plasminogen digestion assay, three major products of 60, 50 and 40 kDa obtained, SDS-PAGE
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
cathepsin V hydrolyzes plasminogen at Phe94-Glu95, Ser358-Thr359, and Val468-Leu469 generating angiostatin-related fragments
-
-
?
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-Leu-Arg-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-4-methyl-7-coumaryl amide + H2O
Z-Phe-Arg + 4-methyl-7-coumaryl amine
show the reaction diagram
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + 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
-
role of cathepsis V and the endogenous inhibitor cystatin C in adverse extracellular matrix remodeling of stenotic aortic valves analyzed
-
-
?
MHC class II-associated invariant chain + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the corneal enzyme stays within cells and is not secreted, suggesting that components of the corneal epithelium are likely substrates
-
-
-
additional information
?
-
-
the predominant expression in thymus suggests a role in the immune system, the expression in testes suggests a role in fertilization processes, the expression in cancer cells together with its absence in normal cells suggests a role in tumor processes
-
-
-
additional information
?
-
-
the enzyme and inhibitor cystatin M/E are involved in regulation of epidermal differentiation
-
-
-
additional information
?
-
-
the enzyme can stimulate H2O2 production, enzyme expression is increased in keratoconus corneas compared to healthy ones, oxidative stress might be involved in the disorder
-
-
-
additional information
?
-
-
substrate and cleavage site specificity of activated recombinant enzyme, comparison to cathepsin L, overview
-
-
-
additional information
?
-
-
the enzyme prefers hydrophobic residues in its S2-binding pocket, the substrate specificity is similar to cathepsin L, no cleavage of the triple-helical region of native collagen
-
-
-
additional information
?
-
-
the human transglutaminase zymogen is no substrate for the enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
elastin degradation activity leading to loss of elasticity in atherosclerosis
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
capability of recombinant human cathepsin V to hydrolyze plasminogen analyzed, physiological role for cathepsin V related to the control of neovascularization in cornea suggested
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
cathepsin V hydrolyzes plasminogen at Phe94-Glu95, Ser358-Thr359, and Val468-Leu469 generating angiostatin-related fragments
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the corneal enzyme stays within cells and is not secreted, suggesting that components of the corneal epithelium are likely substrates
-
-
-
additional information
?
-
-
the predominant expression in thymus suggests a role in the immune system, the expression in testes suggests a role in fertilization processes, the expression in cancer cells together with its absence in normal cells suggests a role in tumor processes
-
-
-
additional information
?
-
-
the enzyme and inhibitor cystatin M/E are involved in regulation of epidermal differentiation
-
-
-
additional information
?
-
-
the enzyme can stimulate H2O2 production, enzyme expression is increased in keratoconus corneas compared to healthy ones, oxidative stress might be involved in the disorder
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
NaCl
-
stimulates at 0.3 M
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
-
-
-
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
-
cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA
-
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
-
cystatin M/E wild-type and mutant N64A show high affinity for cathepsin V, but not cystatin M/E mutant W135A
-
cystatin M/E
-
regulatory role, two distinct binding sites for cysteine proteases of the C1 peptidase family, the endogenous inhibitor is co-localized with the enzyme in lamellar granules and corneodesmosomes
-
cystatin M/E
-
the antiprotease activity of cystatin M/E inhibits the activity of cathepsin V
-
cystatin M/E
-
high-affinity inhibitor of cathepsin V, directly controls the activity of cathepsin V
-
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
-
-
macrocypin-1
-
-
-
morpholineurea-leucyl-homophenylalanine-vinylsulfone phenyl
-
-
morpholineurea-naphthyl-homophenylalanine-vinylsulfone naphthyl
-
-
-
peptidl vinyl sulfones
-
-
-
pyranofoline
-
-
-
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
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
-
VBY-825
-
reversible cathepsin inhibitor with high potency against cathepsins V
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.0017
-
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.002
-
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.0008
-
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.0006
-
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.0012
-
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.0041
-
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25C, in presence of 0.3 M NaCl
0.0048
-
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25C
0.0006
-
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
presence of ds65-mer DNA causes a nonsignificant decrease in the Km value for the interaction between cathepsin V and the substrate, values from about 33.1 microM to 27.5 microM measured
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4
-
2-aminobenzoyl-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
1.3
-
2-aminobenzoyl-EE-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
0.6
-
2-aminobenzoyl-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
1.7
-
2-aminobenzoyl-KK-epsilon-amino-caproic acid-ELKLQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
1.5
-
2-aminobenzoyl-KLRSIKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
1.3
-
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
3.4
-
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25C
3.7
-
Z-Phe-Arg-4-methyl-7-coumaryl amide
-
recombinant enzyme, pH 5.5, 25C, in presence of 0.3 M NaCl
0.9
-
2-aminobenzoyl-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
recombinant enzyme, pH 5.5, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
presence of DNA reduces the turnover rate up to 50% indicating that the binding of DNA changes the active site of cathepsin V such that the enzyme interacts with peptide substrates differently
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
496
-
2-aminobenzoyl-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, in 0.1 M sodium acetate buffer, pH 5.5
302860
903
-
2-aminobenzoyl-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, in 0.1 M sodium acetate buffer, pH 5.5
302859
4528
-
2-aminobenzoyl-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, in 0.1 M sodium acetate buffer, pH 5.5
302861
3055
-
2-aminobenzoyl-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, in 0.1 M sodium acetate buffer, pH 5.5
302863
6833
-
2-aminobenzoyl-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, pH 5.5
302858
4277
-
2-aminobenzoyl-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine
-
at 37C, in 0.1 M sodium acetate buffer, pH 5.5
302862
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 27C
-
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 27C
-
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 27C
-
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 27C
-
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 27C
-
0.001
-
citrusinine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0042
-
citrusinine-II
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
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, 25C
-
0.01
-
glycocitrine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0011
-
glycocitrine-IV
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.00000069
-
macrocypin-1
-
pH and temperature not specified in the publication
-
0.00000034
-
mutant N64A cystatin M/E
-
pH 5.5, 22C
-
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 25C
0.00000047
-
wild-type cystatin M/E
-
pH 5.5, 22C
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0039
-
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 27C
-
0.0025
-
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 27C
-
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
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0028
-
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 27C
-
0.048
-
5-hydroxynoracronycine
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0012
-
citibrasine
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0022
-
citrusinine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.01
-
citrusinine-II
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.025
-
glycocitrine-I
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.0022
-
glycocitrine-IV
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
0.044
-
pyranofoline
-
in 100 mM sodium acetate buffer (pH 5.5) containing 5 mM EDTA and 5 mM dithioerythritol, at 27C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity in aortic valves quantified by fluorometric microassay, increased mRNA expression and high activity of cathepsin V in stenotic valves observed, association of cathepsin V and the inhibitor cystatin C with calcific aortic valve disease determined, participation in adverse extracellular matrix remodelling of stenotic aortic valves suggested; expression of cathepsin V studied by RT-PCR and immunohistochemistry, cathepsin activity quantified by fluorometric microassay, intense association of cathepsin V with neovessels of the stenotic aortic valves reveals a role in neovascularization of the valves
additional information
-
-
inhibition properties of cathepsin V propeptide by fluorimetric assay determined, purification and expression of cathepsin V propeptide described, recombinant cathepsin V used for inhibition studies
additional information
-
-
plasminogen digestion by cathepsin V determined by SDS-PAGE and by subsequent plasmin activity tests, sequences EKKVYL, TEQLAP and LLPNVE obtained by N-terminal sequencing compatible with cleavage sites at plasminogen F94-E95, S358-T359 and V468-L469 peptide bonds, in vitro angiogenesis Matrigel assay described, angiogenesis inhibition activity caused by plasminogen processing by cathepsin V determined
additional information
-
-
interaction between cathepsin V with the model serpins MENT and SCCA-1 and with cystatin A analyzed, association rate constant (ka) for cathepsin V interaction in the presence and absence of cofactors determined, stoichiometry of inhibition (SI) in the absence and presence of cofactors determined, kinetic parameters of MENT and cystatin A in the presence of various DNA constructs ranging between 18mers and 65mers measured, binding of serpins and cathepsin V to DNA indicated by gel mobility shift analysis, electrostatic potential of human cathepsins V and effect of dsDNA on cathepsin V fluorescence indicated
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6
-
-
5.5
6.5
-
assay at
5.5
-
-
assay at
5.5
-
-
protease inhibition assay at
5.7
-
-
-
6.5
-
-
plasminogen digestion assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
25
-
-
assay at
37
-
-
assay at
37
-
-
plasminogen digestion assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
recombinant human cathepsin V for inhibition studies, N-terminal propeptide domains as inhibitors of cathepsin V
Manually annotated by BRENDA team
-
epithelium
Manually annotated by BRENDA team
-
normal and keratoconus corneas, the latter show a 1.5fold increased cathepsin V expression level, expression pattern, overview
Manually annotated by BRENDA team
-
thymic and corneal
Manually annotated by BRENDA team
-
localization of the enzyme in the root sheets of the hair follicle
Manually annotated by BRENDA team
-
in the root sheath of the hair follicles
Manually annotated by BRENDA team
-
plasminogen processing by cathepsin V, angiogenesis inhibition activity determined in
Manually annotated by BRENDA team
-
in extracellular space associated to corneodesmosomes, co-localization of the enzyme and inhibitor cystatin M/E
Manually annotated by BRENDA team
-
co-localization of the enzyme and inhibitor cystatin M/E, which are separately transported within lamellar granules
Manually annotated by BRENDA team
-
in the human thymic cortex, CTSV is the predominately expressed protease
Manually annotated by BRENDA team
-
epithelium
Manually annotated by BRENDA team
-
in plaque areas of diseased blood vessels, cathepsin expression levels during differentiation, overview
Manually annotated by BRENDA team
additional information
-
selective, tissue-specific expression
Manually annotated by BRENDA team
additional information
-
no expression in colon, lung, trachea, ureter, testis, heart, muscle, aorta, spleen, and mammary gland
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the corneal enzyme stays within cells and is not secreted
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24000
-
-
mature protein, SDS-PAGE
35500
-
-
proprotein, SDS-PAGE
37000
-
-
preproprotein, SDS-PAGE
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 23000, nonglycosylated form, SDS-PAGE; x * 35000, glycoprotein, SDS-PAGE
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 ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
recombinant enzyme is partially and heterogenously glycosylated
glycoprotein
-
three potential N-lycosylation sites
glycoprotein
-
N-glycosylation of extracellular proenzyme and mature enzyme
glycoprotein
-
-
proteolytic modification
-
autoactivation of the inactive extracellular zymogen at pH 4.0 and 37C to the active mature protein
proteolytic modification
-
the recombinant enzyme is activated by pepsin treatment and further purified by gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
5.5
-
very stable
5.5
-
-
2 h stable
5.5
-
-
37C, loss of 60% activity within 20 min
6.5
-
-
2 h, residual acitviy
7
-
-
1 h, residual acitviy
additional information
-
-
rapid loss of activity at neutral pH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
pH 5.5, loss of 60% activity within 20 min
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration, pre-activated before use
-
gel filtration, recombinant human cathepsin V
-
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 ACCESSION NO.
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
-
human cathepsins V expressed in Pichia pastoris
-
recombinant human cathepsin V produced using the Pichia pastoris expression system
-
transgenic expression in cathepsin L-deficient mice, phylogenetic tree
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
there is decreased expression of cathepsin V in lesional atopic dermatitis and psoriasis epidermis at the mRNA level as well as the protein level
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
the enzyme can complement cathepsin L-deficient mice by expression of cathepsin V in epidermis and hair follicles, the mutant mice suffer from a complex skin phenotype consisting of hair loss and epidermal hyperplasia with hyperproliferation of basal epidermal keratinocytes, acanthosis, and hyperkeratosis, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
the enzyme is a potential marker for certain colon tumors and breast cancer
medicine
-
studies on the role of cathepsin V and cystatin C in the pathophysiology aortic stenosis