| Type: | Domain | Name: | Peptidase M16 domain |
| Description: | The M16 family of zinc peptidases comprises a pair of homologous domains that form two halves of a "clam-shell" surrounding the active site []. This entry represents this domain found in metallopeptidases and non-peptidase homologues belonging to MEROPS peptidase family M16 (clan ME), subfamilies M16A, M16B and M16C; they include:Insulinase, insulin-degrading enzyme ()Mitochondrial processing peptidase alpha subunit, (Alpha-MPP, )Pitrlysin, Protease III precursor ()Nardilysin, ()Ubiquinol-cytochrome C reductase complex core protein I,mitochondrial precursor ()Coenzyme PQQ synthesis protein F ()These proteins do not share many regions of sequence similarity; the most noticeable is in the N-terminal section. This region includes a conserved histidine followed, two residues later by a glutamate and another histidine. In pitrilysin, it has been shown [] that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity. The proteins classified as non-peptidase homologues either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity. | Short Name: | Pept_M16_dom |
