Katepsin F
Izgled
Katepsin F | |||||||||
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Dimer katepsina F (čovjek) | |||||||||
Identifikatori | |||||||||
EC broj | 3.4.22.41 | ||||||||
CAS broj | 65997-74-2 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Katepsin F (EC 3.4.22.41, Cathepsin F) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Ovaj rekombinantni enzim razlaže sintetičke supstrate sa Phe i Leu (u većoj meri nego Val) u P2, sa visokom specifičnošću slično katepsinu L
Katepsin F je lizozomalna cisteinska endopeptidaza iz familije C1 (papainske familije)
- ↑ Santamaría, I., Velasco, G., Pendás, A.M., Paz, A. and López-Otín, C. (1999). „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: 13800-13809. PMID 10318784.
- ↑ Nägler, D.K. Sulea, T. and Ménard, R. (1999). „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. PMID 10198209.
- ↑ Wex, T., Levy, B., Wex, H. and Brömme, D. (1999). „Human cathepsins F and W: A new subgroup of cathepsins”. Biochem. Biophys. Res. Commun. 259: 401-407. PMID 10362521.
- ↑ Wang, B., Shi, G.-P., Yao, P.M., Li, Z., Chapman, H.A. and Brömme, D. (1998). „Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization”. J. Biol. Chem. 273: 32000-32008. PMID 9822672.
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- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
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