| Primary Identifier | IPR034115 | Type | Domain |
| Short Name | M35_peptidyl-Lys |
| description | This entry includes the family M35 Zn2+-metallopeptidase extracellular domain from proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20; MEROPS identifier M35.004), including some well-characterized domains in Armillaria mellea [], Aeromonas salmonicida subsp. achromogenes (AsaP1) [, ]and Grifola frondosa (GfMEP) [, , ]. These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase (MEROPS identifier M35.003) has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response []. AsaP1 is synthesized as an inactive precursor, the structure of which shows that the propeptide inhibits activity by inserting a lysine into the S1' pocket of active site [].Peptidase family M35 contains metalloendopeptidases known as Asp-zincins, in which a single catalytic zinc ion is ligated by two histidines in an HExxH motif and an aspartic acid in a GTXDXXYG or similar motif C-terminal to the HExxH motif. The glutamic acid in the HExxH motif is a catalytic residue []. |
