| Type: | Family | Name: | Peptidase M28E, aminopeptidase AP1 |
| Description: | Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half 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 [].This family are metallopeptidases belonging to MEROPS peptidase family M28, subfamily M28E (aminopeptidase Ap1, clan MH). Representative members are aminopeptidase Ap1 from Vibrio proteolyticus(Vibrio proteolyticus(Aeromonas proteolytica)) [] and aminopeptidase apAC from Aeromonas punctata(Aeromona caviae) []. | Short Name: | Pept_M28E_Ap1 |
