{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T15:05:03Z","timestamp":1789571103566,"version":"build-2803163510"},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T00:00:00Z","timestamp":1788739200000},"content-version":"vor","delay-in-days":15,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,23]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>O-glycopeptidases are proteolytic enzymes that obligately recognize the O-glycans appended to their substrates. Peptidase_M60 proteins comprise a superfamily of putative metal-dependent O-glycopeptidases that were initially described in host-associated bacteria but are now known to be distributed across bacteria occupying both host-associated and environmental niches. Although several members of this superfamily have been shown to possess O-glycopeptidase activity, the family is highly divergent at the amino acid sequence level, making it unclear whether this activity is conserved across all members. Here, we show that two peptidase_M60 enzymes, EfmM60 and EfcM60, from strains of Enterococcus faecium and Enterococcus faecalis, respectively, which are only distantly related at the primary sequence level to previously characterized O-glycopeptidases, exhibit both mucinase and O-glycopeptidase activity. Structural analysis of EfmM60 reveals distinct active-site features relative to previously characterized peptidase_M60 enzymes that provide a molecular basis for its ability to accommodate extended and branched O-glycans. Together, these findings highlight functional conservation within a highly divergent peptidase_M60 family and suggest that enterococcal O-glycopeptidases may contribute to ecological versatility by enabling access to O-glycosylated substrates across diverse biological contexts.<\/jats:p>","DOI":"10.1093\/glycob\/cwag076","type":"journal-article","created":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T11:21:23Z","timestamp":1788693683000},"source":"Crossref","is-referenced-by-count":0,"title":["Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus"],"prefix":"10.1093","volume":"36","author":[{"given":"Liam G","family":"Mihalynuk","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , PO Box 1700 STN CSC, Victoria, BC V8W 2Y2 ,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin","family":"Pluvinage","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , PO Box 1700 STN CSC, Victoria, BC V8W 2Y2 ,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivia","family":"Canil","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , PO Box 1700 STN CSC, Victoria, BC V8W 2Y2 ,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicole","family":"Thompson","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Alberta, Edmonton , CW 405, Biological Sciences Bldg, Alberta, T6G 2E9,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1539-1679","authenticated-orcid":false,"given":"Warren","family":"Wakarchuk","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Alberta , Edmonton, CW 405, Biological Sciences Bldg, Alberta, T6G 2E9,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6417-0592","authenticated-orcid":false,"given":"Alisdair B","family":"Boraston","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Microbiology, University of Victoria , PO Box 1700 STN CSC, Victoria, BC V8W 2Y2 ,","place":["Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,9,7]]},"reference":[{"issue":"5","key":"2026091610363784900_ref1","doi-asserted-by":"publisher","first-page":"374","DOI":"10.1016\/j.ijantimicag.2008.04.026","article-title":"Virulence and antimicrobial resistance in clinical enterococcus faecium","volume":"32","author":"Billstr\u00f6m","year":"2008","journal-title":"Int J Antimicrob Agents"},{"key":"2026091610363784900_ref2","first-page":"113","author":"Brockhausen","year":"2015"},{"key":"2026091610363784900_ref3","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/bs.mie.2026.03.007","article-title":"A dual-color FRET assay for detection and quantitative analysis of O-glycopeptidases","volume":"732","author":"Canil","year":"2026","journal-title":"Methods Enzymol"},{"key":"2026091610363784900_ref1c","first-page":"356","article-title":"Preliminary characterization of bacteriocins from Lactococcus lactis, Enterococcus faecium and Enterococcus mundtii strains isolated from turbot (Psetta maxima). 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