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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role. Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].Proteins in this entry are metalloendopeptidases belong to the MEROPS peptidase family M10 (subfamily M10B, clan MA). They include serralysin, epralysin, mirabilysin, aeruginolysin and other related peptidases. The peptidase unit is found at the N terminus while in this entry it is found at the C terminus and forms a corkscrew. It is thought to be important for secretion of the protein through the bacterial cell wall. Proteins in this entry contain a calcium ion binding domain. | Name | Peptidase M10B |
| Short Name | Pept_M10B | Type | Family |
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