1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR014782 | Domain | Peptidase M1, membrane alanine aminopeptidase, N-terminal |
1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR001930 | Family | Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase |
| Type: | Family | Name: | Peptidase M1, alanyl aminopeptidase |
| 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 [].The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, , after the Escherichia colienzyme, suggesting a similar activity profile (see for a description of catalytic activity).This family of zinc metallopeptidases belong to MEROPS peptidase family M1 (aminopeptidase N, clan MA); the majority are identified as alanyl aminopeptidases (proteobacteria) that are closely related to E. coli PepN and presumed to have a similar (not identical) function. Nearly all are found in proteobacteria, but members are found also in cyanobacteria, plants, and apicomplexan parasites [, ]. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividansPepN () and from the membrane bound aminopeptidase N family in animals. | Short Name: | Peptidase_M1_pepN |
| DB identifier | Type | Name |
|---|---|---|
| IPR014782 | Domain | Peptidase M1, membrane alanine aminopeptidase, N-terminal |
| DB identifier | Type | Name |
|---|---|---|
| IPR001930 | Family | Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase |
