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Information on EC 3.4.22.41 - cathepsin F and Organism(s) Homo sapiens
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3.4.22.41 cathepsin FSpecify your search results
Word Map
- 3.4.22.41
- cathepsins
- diagnostics
- westermani
- viroid
- paragonimus
-
f-like
- food industry
- metalloproteinase-10
-
cystatin-like
- viverrini
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cathepsin f, cf-11, ov-cf-1, pwcp2, pwcp5, cat f, tci-cf-1, pwcp1, pwcp3, pwcp4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CATSF
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
65997-74-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-Val-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
the enzyme plays a role in tumor-induced angiogenesis, cell migration, proliferation, apoptosis, and connective tissue degradation
-
-
?
additional information
?
-
-
involved in atherosclerotic inflammatory processes
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
morpholine urea-Leu-homophenylalaninevinyl sulfone-phenyl
potent and irreversible inhibitor of cysteine proteases
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
human aortic proteoglycans
-
activates apoB-100/LDL degradation by cathepsin F
-
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, mutant enzyme N97Q/N108Q/N170Q
2.9
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
slightly acidic pH optimum, rapid inactivation at neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
production of cathepsin F is increased by stimulation of cells with angiotensin, level of lysosomal enzyme remains unaffected but more enzyme is secreted
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
lysosomal enzyme can be secreted into the extracellular medium
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATF_HUMAN
484
0
53366
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33860
302 amino acid protein composed of a 88 residue propeptide and a 214 residue mature enzyme
additional information
additional information
composed of a 88 residue propeptide and a 214 residue mature enzyme, no signal peptide
additional information
-
composed of a 88 residue propeptide and a 214 residue mature enzyme, no signal peptide
additional information
cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins
additional information
-
cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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
five potential glycosylation sites at positions 141p, 176p of the signal sequence and 97, 108, 170 of the mature enzyme
glycoprotein
-
the enzyme contains three potential N-linked glycosylation sites in the mature region: N97 and N108 and N170
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N97Q/N108Q/N170Q
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enhanced production and release of cathepsins in tumor cells leads to tumor cell growth, invasion and metastasis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Santamaria, I.; Velasco, G.; Pendas, A.M.; Paz, A.; Lopez-Otin, C.
Molecular cloning and structural and functional characterization of cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
J. Biol. Chem.
274
13800-13809
1999
Homo sapiens (Q9UBX1), Homo sapiens
Ngler, D.K.; Sulea, T.; Menard, R.
Full length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
Biochem. Biophys. Res. Commun.
257
313-318
1999
Homo sapiens (Q9UBX1), Homo sapiens
Wex, T.; Levy, B.; Wex, H.; Brmme, D.
Human cathepsins F and W: A new subgroup of cathepsins
Biochem. Biophys. Res. Commun.
259
401-407
1999
Homo sapiens
Wang, B.; Shi, G.P.; Yao, P.M.; Li, Z.; Chapman, H.A.; Brmme, D.
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
J. Biol. Chem.
273
32000-32008
1998
Homo sapiens (Q9UBX1), Homo sapiens
Wex, T.; Wex, H.; Brmme, D.
The human cathepsin F gene - a fusion product between an ancestral cathepsin and cystatin gene
Biol. chem.
380
1439-1442
1999
Homo sapiens
Dingle, J.T.; Blow, A.M.J.; Barrett, A.J.; Martin, P.E.N.
Proteoglycan-degrading enzymes. A radiochemical assay method and the detection of a new enzyme, cathepsin F
Biochem. J.
167
775-785
1977
Homo sapiens, Oryctolagus cuniculus
Ho, J.D.; Meltser, Y.; Buggy, J.J.; Palmer, J.T.; Elrod, K.C.; Chan, H.; Mortara, K.D.; Somoza, J.R.
Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitor
Acta Crystallogr. Sect. D
58
2187-2190
2002
Homo sapiens
Somoza, J.R.; Palmer, J.T.; Ho, J.D.
The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators
J. Mol. Biol.
322
559-568
2002
Homo sapiens
Vazquez-Ortiz, G.; Pina-Sanchez, P.; Vazquez, K.; Duenas, A.; Taja, L.; Mendoza, P.; Garcia, J.A.; Salcedo, M.
Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer
BMC Cancer
5
68
2005
Homo sapiens
Oeoerni, K.; Sneck, M.; Broemme, D.; Pentikaeinen, M.O.; Lindstedt, K.A.; Maeyraenpaeae, M.; Aitio, H.; Kovanen, P.T.
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro
J. Biol. Chem.
279
34776-34784
2004
Homo sapiens
Kaakinen, R.; Lindstedt, K.A.; Sneck, M.; Kovanen, P.T.; Ooerni, K.
Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect
Atherosclerosis
192
323-327
2007
Homo sapiens
Kuester, D.; Lippert, H.; Roessner, A.; Krueger, S.
The cathepsin family and their role in colorectal cancer
Pathol. Res. Pract.
204
491-500
2008
Homo sapiens
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