Cathepsins are proteases , mainly intracellular. Most cathepsins are active inside lysosomes , destroying the molecules captured by the cell . According to the structure of the active site, cathepsins are divided into cysteine, serine and aspartate proteases. The most numerous cathepsins containing cysteine in their active site are: cathepsins B , C , H, F, L, K, O, S, V / L2 , X, W. Serine proteases include cathepsins A and G , aspartate proteases include D and E.
| Cathepsins | |
|---|---|
 Cathepsin K structure | |
| Identifiers | |
| Symbol | Cathepsin |
| Pfam | PF00112 |
| Interpro | IPR000668 |
| SMART | Pept_c1 |
| PROSITE | PDOC00126 |
| SCOP | 1aec |
| SUPERFAMILY | 1aec |
| Available protein structures | |
| Pfam | the structure |
| PDB | RCSB PDB ; PDBe ; PDBj |
| PDBsum | 3D model |
The optimum pH for the action of cathepsins is 3.8. The activity of cathepsins increases in tumor cells. Group B cathepsins are trypsin-like; groups D - act like pepsin , activate other cathepsins. Cathepsin of group G is most active in polymorphonuclear leukocytes , acts like chymotrypsin.
Links
- Human cathepsins - medbiol.ru