Reaction: 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
Comments: 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
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 65997-74-2
References:
1. Santamaría, I., Velasco, G., Pendás, A.M., Paz, A., and López-Otín, C. Molecular cloning and structural and functional chararcterization of cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274 (1999) 13800-13809. [PMID: 10318784]
2. Nägler, D.K. Sulea, T., and Ménard, 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 (1999) 313-318. [PMID: 10198209]
3. Wex, T., Levy, B., Wex, H. and Brömme, D. Human cathepsins F and W: A new subgroup of cathepsins. Biochem. Biophys. Res. Commun. 259 (1999) 401-407. [PMID: 10362521]
4. Wang, B., Shi, G.-P., Yao, P.M., Li, Z., Chapman, H.A. and Brömme, D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J. Biol. Chem. 273 (1998) 32000-32008. [PMID: 9822672]