Information on EC 3.4.22.41 - cathepsin F

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The expected taxonomic range for this enzyme is: Bilateria

EC NUMBER
COMMENTARY
3.4.22.41
-
RECOMMENDED NAME
GeneOntology No.
cathepsin F
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L
show the reaction diagram
Cathepsin F is a lysosomal cysteine endopeptidase of family C1, papain family, most activite at pH 5.9. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Cathepsin F is expressed in most tissues of human, mouse and rat. Human gene locus: 11q13.1-13.3; endopeptidase
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
-
CAS REGISTRY NUMBER
COMMENTARY
65997-74-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
accession number AF071748, AF071749
Uniprot
Manually annotated by BRENDA team
accession number AF088886
Uniprot
Manually annotated by BRENDA team
accession number AF132894
-
-
Manually annotated by BRENDA team
accession numbers AJ007331, AJ131851
Uniprot
Manually annotated by BRENDA team
mexican women
-
-
Manually annotated by BRENDA team
production of cathepsin F is increased by stimulation of cells with angiotensin, level of lysosomal enzyme remains unaffected but more enzyme is secreted
-
-
Manually annotated by BRENDA team
C57BL/6J and 129 SVJ mice
-
-
Manually annotated by BRENDA team
olive flounder
UniProt
Manually annotated by BRENDA team
olive flounder
UniProt
Manually annotated by BRENDA team
Wistar rat
UniProt
Manually annotated by BRENDA team
italian large white pig
-
-
Manually annotated by BRENDA team
common abomasal nematode parasite of sheep
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
cathepsin F is implicated in the growth and reproduction regulation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Albumin + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
apoB-100 + H2O
?
show the reaction diagram
-
apoB-100 is part of LDL particles
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
low activity
-
-
?
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-leucine-L-arginine + 7-amino-4-methylcoumarin
show the reaction diagram
-
high catalytic activity with isozymes CF-4 and CF-11
-
?
benzyloxycarbonyl-L-leucyl-L-arginyl-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-leucyl-L-arginyl + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-phenylalanine-L-arginine + 7-amino-4-methylcoumarin
show the reaction diagram
-
high catalytic activity with isozymes CF-4 and CF-11
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
high activity
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
high activity
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
Collagen + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
Gelatin + H2O
?
show the reaction diagram
purified CtF is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
cathepsin F and cathepsin B can work in concert to hydrolyse hemoglobin at low pH
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
Ii-MHC class II complex + H2O
?
show the reaction diagram
-
-
-
-
?
immunoglobulin A + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
immunoglobulin G + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
immunoglobulin M + H2O
?
show the reaction diagram
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
N-acetyl-DEVD-7-amido-4-triflurormethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-triflurormethylcoumarin
show the reaction diagram
-
-
-
?
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
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-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
-
-
?
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-Val-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Val-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
highest activity
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
very low activity
-
-
?
LAMP 2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme likely plays a regulatory role in the processing in the invariant chain that is assoviated with the major histocompatibility complex class II
-
-
?
additional information
?
-
cathepsin F-1 is developmentally regulated
-
-
-
additional information
?
-
-
the enzyme is a cysteine protease
-
-
-
additional information
?
-
-
the enzyme plays a role in tumor-induced angiogenesis, cell migration, proliferation, apoptosis, and connective tissue degradation
-
-
-
additional information
?
-
-
the enzyme is a cysteine protease and modifies low density lipoprotein particles in vitro
-
-
-
additional information
?
-
-
involved in atherosclerotic inflammatory processes
-
-
-
additional information
?
-
-
cathepsin F degrades extracellular matrix proteins more effectively than capthespin B1 at physiological pH
-
-
-
additional information
?
-
the enzyme is not able to hydrolyze protein substrates such as azocasein, fibrinogen, and bovine serum albumin
-
-
-
additional information
?
-
-
the fully activated cathepsin F cleaves fluorogenic-NHMec substrates with the preference Val-Leu-Arg>Leu-Arg>Phe-Arg>Arg-Arg with little or no activity against Pro-Arg or Pro-Lys substrates
-
-
-
additional information
?
-
-
the isozymes CF-4, CF-6, and CF-11 do not hydrolyze benzyloxycarbonyl-L-arginine-L-arginine-7-amido-4-methylcoumarin and benzyloxycarbonyl-L-arginine-7-amido-4-methylcoumarin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Hemoglobin + H2O
?
show the reaction diagram
-
cathepsin F and cathepsin B can work in concert to hydrolyse hemoglobin at low pH
-
-
?
Ii-MHC class II complex + H2O
?
show the reaction diagram
-
-
-
-
?
LAMP 2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme likely plays a regulatory role in the processing in the invariant chain that is assoviated with the major histocompatibility complex class II
-
-
?
additional information
?
-
Q218Y2
cathepsin F-1 is developmentally regulated
-
-
-
additional information
?
-
-
the enzyme is a cysteine protease
-
-
-
additional information
?
-
-
the enzyme plays a role in tumor-induced angiogenesis, cell migration, proliferation, apoptosis, and connective tissue degradation
-
-
-
additional information
?
-
-
involved in atherosclerotic inflammatory processes
-
-
-
additional information
?
-
-
cathepsin F degrades extracellular matrix proteins more effectively than capthespin B1 at physiological pH
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
149.95% relative activity at 1 mM
K+
143.7% relative activity at 1 mM
Mg2+
133.38% relative activity at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
15.28% inhibition at 0.1 mM
antipain
complete inhibition at 0.1 mM
Aprotinin
36.94% inhibition at 0.1 mM
Chloroquine
-
-
chymostatin
35.42% inhibition at 0.1 mM
Co2+
6.85% residual activity at 5 mM
Cu2+
11.6% residual activity at 5 mM
cystatin B
-
-
-
E-64
56.3% inhibition at 0.1 mM
E-64
-
effective inhibition
EDTA
6.52% inhibition at 0.1 mM
EGTA
4.72% inhibition at 0.1 mM
Hg2+
0.81% residual activity at 5 mM
JPM565
-
radioactive-labeling by 125I, irrevrsible inhibitor of papin-type cathepsins, active site labeling
morpholine urea-Leu-homophenylalaninevinyl sulfone-phenyl
potent and irreversible inhibitor of cysteine proteases
-
morpholine urea-Leu-homophenylalaninevinyl sulfone-phenyl
-
-
-
NEM
44.59% inhibition at 0.1 mM
phenylmethylsufonyl fluoride
13.22% inhibition at 0.1 mM
SDS
complete inhibition at 0.05% (w/v)
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
i.e. E-64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
Z-VAD(OMe)-fluoromethylketone
-
-
-
Zn2+
5.94% residual activity at 1 mM
leupeptine
complete inhibition at 0.1 mM
-
additional information
downregulation of cathepsin F mRNA by E-64d; treatment with retinol/palmitic acid increases mRNA-level of cystatin B coupled with decrease in cathepsin F activity; treatment with retinol/palmitic acid increases mRNA-level of cystatin C coupled with decrease in cathepsin F activity
-
additional information
not inhibited by pepstatin A
-
additional information
-
the prodomain effectively inhibits the enzyme in which the ERFNAQ motif plays a critical role in the inhibition, but the GTFD motif is also required for complete inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Brij 35
273.6% relative activity at 0.01% (v/v)
chondroitin-4-sulfate
-
activates apoB-100/LDL degradation by cathepsin F
chondroitin-6-sulfate
-
activates apoB-100/LDL degradation by cathepsin F
dermatan sulfate
-
activates apoB-100/LDL degradation by cathepsin F
heparan sulfate
-
activates apoB-100/LDL degradation by cathepsin F
Triton X-100
310.29% relative activity at 0.01% (v/v)
Tween 20
282.7% relative activity at 0.01% (v/v)
human aortic proteoglycans
-
activates apoB-100/LDL degradation by cathepsin F
-
additional information
-
cathepsin F is secreted as an inactive zymogen that autocatalytically processes and activates to a mature enzyme at pH 4.5 (after 6 h incubation) via an intermolecular cleavage at the prosegment-mature domain junction, the active cathepsin B1 zymogen is capable of trans-activating cathepsin F by proteolytic removal of its prosegment at pH 5.5
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
pH 6.5, room temperature, mutant enzyme N97Q/N108Q/N170Q
0.017
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, wild-type enzyme
0.00287
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide
-
0.00023
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide
-
0.00044
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide
-
0.00124
N-benzyloxycarbonyl-L-Val-L-Arg-4-methylcoumarin 7-amide
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
Homo sapiens
-
pH 6.5, room temperature, mutant enzyme N97Q/N108Q/N170Q
2.9
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
Homo sapiens
-
pH 6.5, room temperature, wild-type enzyme
0.2
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide
Homo sapiens
Q9UBX1
-
1.3
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide
Homo sapiens
Q9UBX1
-
2.5
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide
Homo sapiens
Q9UBX1
-
1.3
N-benzyloxycarbonyl-L-Val-L-Arg-4-methylcoumarin 7-amide
Homo sapiens
Q9UBX1
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin
Clonorchis sinensis
-
isozyme CF-11, in 100 mM sodium phosphate (pH 5.5), at 37C
160415
7.6
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin
Clonorchis sinensis
-
isozyme CF-4, in 100 mM sodium phosphate (pH 6.5), at 37C
160415
6
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin
Clonorchis sinensis
-
isozyme CF-11, in 100 mM sodium phosphate (pH 5.5), at 37C
160414
8.2
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin
Clonorchis sinensis
-
isozyme CF-4, in 100 mM sodium phosphate (pH 6.5), at 37C
160414
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
assay method
additional information
adding E-64d (inhibitor) results in drastically inhibition of enzyme activity in cytosol and nucleus, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm, confirmed by cathepsin F siRNA treatment; higher activity in nucleus than in cytosol, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm, differentiation between cathepsin F and other cathepsins by using specific inhibitors and substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 6.8
-
5.5
substrate benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
5.5
-
pH optimum of isozyme CF-11
6
-
about
6.5
-
pH optimum of isozyme CF-4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
modest enzyme activity, substrates hemoglobin and gelatin
4.5 - 8
substrate benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
additional information
-
slightly acidic pH optimum, rapid inactivation at neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
distribution, overview
Manually annotated by BRENDA team
-
overexpression of cathepsin F
Manually annotated by BRENDA team
RT-PCR, immunohistochemistry
Manually annotated by BRENDA team
immunostaining using anti-PoCtF antibody was strongest on the epidermal mucus in the fin
Manually annotated by BRENDA team
immunohistochemistry
Manually annotated by BRENDA team
-
CFs are synthesized in the epithelial cells lining the parasite intestine and secreted into the intestinal lumen
Manually annotated by BRENDA team
-
monocyte-derived cell culture, enzyme is secreted
Manually annotated by BRENDA team
-
derived from cultured monocytes
Manually annotated by BRENDA team
-
cervical cancer cell lines, CTSF expression profile
Manually annotated by BRENDA team
additional information
not expressed in leukocytes, thymus
Manually annotated by BRENDA team
additional information
-
no CTSF expression in healthy cervical epithelium
Manually annotated by BRENDA team
additional information
temporal/developmental expression pattern
Manually annotated by BRENDA team
additional information
-
expression mainly in coronary atherosclerotic plaques
Manually annotated by BRENDA team
additional information
ubiquitous expression throughout the entirety of healthy tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secretion of the enzyme by macrophage cell culture
-
Manually annotated by BRENDA team
-
lysosomal enzyme can be secreted into the extracellular medium
-
Manually annotated by BRENDA team
immunofluorescence microscopy, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leucin-Arginin-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm; Western blot, immunofluorescence microscopy, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23590
mature enzyme, calculation from sequence of cDNA
137262
23810
predicted from amino acid sequence, 213 residues
700877
24000
-
fully matured enzymes CF-4 and CF-11, SDS-PAGE
709866
33860
302 amino acid protein composed of a 88 residue propeptide and a 214 residue mature enzyme
137262
41000
-
cathepsin F proenzyme in the yeast medium is present as two major protein bands migrating at 41000 Da and 47000 Da as a result of differential addition of N-linked glycans
708053
47000
-
cathepsin F proenzyme in the yeast medium is present as two major protein bands migrating at 41000 Da and 47000 Da as a result of differential addition of N-linked glycans
708053
50000
recombinant His-tag fusion protein, SDS-APGE
708220
additional information
cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins
137259
additional information
composed of a 88 residue propeptide and a 214 residue mature enzyme, no signal peptide
137262
additional information
-
long proregion of 270 amino acids
137263
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 41097, Tci-CF-1, amino acid sequence calculation
?
-
x * 31000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
?
x * 52880, calculated from amino acid sequence
?
-
x * 70000 + x * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
five potential glycosylation sites at positions 141p, 176p of the signal sequence and 97, 108, 170 of the mature enzyme
glycoprotein
four putative N-glycosylation site, one in the propeptide at Asn13, three in the mature region at Asn185, Asn196, Asn258 , no evidence of usage for in vivo glycosylation
glycoprotein
-
the enzyme contains three potential N-linked glycosylation sites in the mature region: N97 and N108 and N170
glycoprotein
-
-
additional information
recombinant expression results in zymogen which needs to be activated, recombinant Ov-CF-1 does not autocatalytically process and activate at pH 4.5, activation can be accomplished by Fasciola hepatica cathepsin L1
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, 1.7 A structure of the mature domain of cathepsin F associated with an irreversible vinyl sulfone inhibitor
-
hanging-drop vapour diffusion method, mutant cathepsin F, N97Q/N108Q/N170Q, complexed with an irreversible vinyl sulfone inhibitor
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
isozyme CF-4 is relatively stable at slight acidic and neutral pHs, but is comparatively unstable in acidic pHs, isozyme CF-11 is stable at acidic pHs, but is highly unstable in neutral and alkaline pH values
709866
4.5
-
best value for crude extracts
137265
5
4 h stable
137262
5
activity is greatly decreased at pH 5 (lysosomal pH) and below
708220
5.5
-
cathepsin F zymogen is inactive at pH 5.5
708053
7.2
half-life 2 min
137262
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, crude extract 2 years stable
-
4C, purified enzyme, 24 h, 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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Ni-NTA column chromatography, gel filtration
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glutathione-Sepharose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 (pREP4) cells
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expressed in Escherichia coli M15 [pREP4] cells
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chromosomal localization of the gene endocing cathepsin F at 11q13
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enhanced production and release of cathepsins in tumor cells leads to tumor cell growth, invasion and metastasis
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expressed in Escherichia coli HEK-293T cells
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expression of mature enzyme in Escherichia coli
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DNA and amino acid sequence determination and analysis
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PCR with primers specific for the Camellia sinensis cathepsin F gene, 5'- and 3'-RACE used to clone and identify a coding sequence of 981 bp (AY821800). The Ov-cf-1 gene is organized into 7 exons. Phylogenetic analysis confirms relationship of Ov-CF-1 with other cathepsin F proteases.
expressed in Escherichia coli DH5alphaMCR cells using the pGEX-4 T-1 expression vector system
cDNA cloned from primary HSCs using RACE-PCR
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the isozymes CF-4, CF-6, and CF-11 are expressed throughout various developmental stages of the parasite and the transcripts increased gradually in accordance with the maturation of the parasite
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CtF expressions increases significantly in gill at 3 h post-injection with lipopolysaccharide
the accumulation of cathepsin F mRNA in early stage of development increases with development
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N97Q/N108Q/N170Q
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KM-value for benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide is 2fold higher than that of the wild-type enzyme, the turnover number is 2fold lower
additional information
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generation of cat F-deficient mice by homologous recombination, the mutation leads to weight loss and death within 6 months, deficient neurons accumulate eosiniophilic granules causing neuronal ceroid lipofuscinosis beginning as early as 6 weeks of age, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for isozyme CF-4, the purified recombinant protein (10 mg) is slowly added to 1 l of 100 mM Tris-HCl (pH 8.0) containing 1 mM EDTA, 250 mM L-arginine, 5 mM reduced glutathione, and 1 mM oxidized glutathione and gently stirred at 4C for 20 h. Isozyme CF-11 is refolded in 100 mM Tris-HCl (pH 8.0) containing 1 mM EDTA, 250 mM L-arginine, 10 mM reduced glutathione, and 1 mM oxidized glutathione with the same method
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
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CTSF gene (encoding cathepsin F) is a suitable marker for screening pigs to improve cured weight and yield for country ham production
food industry
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CTSF gene is a suitable marker for screening pigs to improve meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness; CTSF gene is a suita marker for screening pigs to leimprove meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness
medicine
the enzyme is immunogenic and a possible target for development of vaccines for teladorsagiosis