Enterococcus faecalis α1–2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification

Yanhong Li, Riyao Li, Hai Yu, Xue Sheng, Jing Wang, Andrew J. Fisher, Xi Chen

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


While multiple α 1–2-mannosidases are necessary for glycoprotein N-glycan maturation in vertebrates, a single bacterial α1–2-mannosidase can be sufficient to cleave all α1–2-linked mannose residues in host glycoprotein N-glycans. We report here the characterization and crystal structure of a new α1–2-mannosidase (EfMan-I) from Enterococcus faecalis, a Gram-positive opportunistic human pathogen. EfMan-I catalyzes the cleavage of α1–2-mannose from not only oligomannoses but also high-mannose-type N-glycans on glycoproteins. Its 2.15 Å resolution crystal structure reveals a two-domain enzyme fold similar to other CAZy GH92 mannosidases. An unexpected potassium ion was observed bridging two domains near the active site. These findings support EfMan-I as an effective catalyst for in vitro N-glycan modification of glycoproteins with high-mannose-type N-glycans.

Original languageEnglish (US)
JournalFEBS Letters
StateAccepted/In press - Jan 1 2019


  • alpha-mannosidase
  • crystal structure
  • glycoprotein modification
  • mannosidase
  • N-glycan enzymatic modification

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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