| Title |
Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family
|
|---|---|
| Published in |
Pflügers Archiv - European Journal of Physiology, January 2000
|
| DOI | 10.1007/s004240000112 |
| Pubmed ID | |
| Authors |
Jože Pungerčar, Gabriela Ivanovski |
| Abstract |
A cDNA encoding a novel human putative member of the papain family of cysteine peptidases has been cloned. The protease, named cathepsin P, is synthesized as a preproprotein. The presumed propeptide of 38 amino acids is followed by a 242-residue mature protein. The mature protease region is 30% identical to human papain-like cathepsins, with all the residues important for catalysis conserved. No similarity was observed in the propeptide region. On the contrary, the proenzyme shares 51-87% residues with some precursors of cysteine proteases from other species that have not yet been characterized. They all show a nearly completely conserved "CYTRED motif" in the propeptide region, not present in other members of the family, and could therefore constitute a distinct subfamily. |
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