| Entry |
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| Name |
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| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
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| Reaction(IUBMB) |
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
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| Comment |
Cathepsin F is a lysosomal cysteine endopeptidase of family C1 (papain family), most active 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
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| History |
EC 3.4.22.41 created 2000
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| Orthology |
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| Genes |
» show all
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| Reference |
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| Authors |
Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C. |
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| Title |
Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Nagler DK, Sulea T, Menard R. |
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| Title |
Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Wex T, Levy B, Wex H, Bromme D. |
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| Title |
Human cathepsins F and W: A new subgroup of cathepsins. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Wang B, Shi GP, Yao PM, Li Z, Chapman HA, Bromme D. |
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| Title |
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 3.4.22.41 |
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