| Type: | Family | Name: | Peptidase C11, Clostripain Clostridium species |
| Description: | Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad or triad []. Clostripain is a cysteine protease characterised from Clostridium histolyticum, and also known from Clostridium perfringens. It is a heterodimer processed from a single precursor polypeptide, using a specific Arg-|-Xaa cleavage. The older term alpha-clostripain refers to the most active, most reduced form, rather than to the product of one of several different genes. This group of cysteine peptidases belong to the MEROPS peptidase family C11 (clostripain family, clan CD). | Short Name: | Pept_C11_CLOspp |
