|Family type peptidase||M73.001 - camelysin (Bacillus cereus), MEROPS Accession MER0031615 (peptidase unit: 28-197)|
|Content of family||Peptidase family M73 contains metallo-endopeptidases.|
Identifier created: MEROPS 6.7 (29 June 2004)|
Peptidase family M73 includes a cell-surface endopeptidase from Bacillus cereus known as camelysin (M73.001).
|Active site||Active site residues and metal ligands have not been determined. Completely conserved potential metal ligands are Asp31, Asp63, Asn73, Asp101, Gln173 and Gln177, though not all members of the family are known to be active peptidases. No histidine is conserved in the family. The only other family of metallopeptidases in which none of the metal ligands are histidine is family M63. The metal content has been determined as one zinc ion per molecule (Grass et al., 2004).|
|Activities and specificities||Camelysin has been shown to cleave proteins such as caseins, actin and collagen type I. Specificity has been determined to be cleavage of bonds with an aliphatic or hydrophilic residue in P1" (Fricke et al., 2001).|
|Inhibitors||Camelysin is inhibited by the chelating agents EDTA and 1,10-phenanthroline at millimolar concentrations. Inhibition was also seen with 10 mM diethylpyrocarbonate, which modifies histidine residues (Fricke et al., 2001), even though a histidine residue is not conserved in the family.|
|Molecular structure||No tertiary structure has been determined for any member of the family. Camelysin is predicted to have an N-terminal signal peptide, and is strongly bound to the cell surface (Grass et al., 2004).|