Biochemical analysis reveals conserved mucinase and O-glycopeptidase activity in divergent enterococci, suggesting structural adaptations that broaden ecological versatility.
Key Points
To determine whether highly divergent peptidase_M60 superfamily proteins in Enterococcus faecium and Enterococcus faecalis conserve mucinase and O-glycopeptidase functions.
Assayed recombinant peptidase_M60 enzymes (EfmM60 from E. faecium and EfcM60 from E. faecalis) for mucinase and O-glycopeptidase activities against glycosylated substrates.
Performed structural characterization of the EfmM60 active site to assess glycan-binding architecture relative to known peptidase_M60 family members.
Both EfmM60 and EfcM60 demonstrate functional mucinase and O-glycopeptidase cleavage despite substantial primary sequence divergence from established homologs.
Structural analysis of EfmM60 identified distinctive active-site features that accommodate extended and branched O-glycan configurations.