| Type: | Family | Name: | Peptidase M3B, oligoendopeptidase F |
| 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 group of metallopeptidases belong to MEROPS peptidase family M3 (clan MA(E)), the type example being oligoendopeptidase F from Lactococcus lactis. The enzyme hydrolyses peptides of 7 and 17 amino acids with fairly broad specificity. Differences in substrate specificity should be expected in other species. The gene is duplicated in L. lactis on the plasmid that bears it. A shortened second copy is found in Bacillus subtilis. | Short Name: | Peptidase_M3B |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Pum1578s0001.1.p | A0A1X6NM09 | PAC:38009677 | Porphyra umbilicalis |
719
 |
| Pum1578s0001.2.p | A0A1X6NLC2 | PAC:38009678 | Porphyra umbilicalis |
697
|
