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Literature summary for 3.4.22.41 extracted from

  • 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 (1999), J. Biol. Chem., 274, 13800-13809.
    View publication on PubMed
Search for more literature for 3.4.22.41

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane i.e. E-64 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UBX1 accession numbers AJ007331, AJ131851
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Source Tissue

Source Tissue Comment Organism Textmining
additional information not expressed in leukocytes, thymus Homo sapiens
-
prostate gland
-
 Homo sapiens
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skeletal muscle
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 Homo sapiens
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testis
-
 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
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 Homo sapiens N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
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