ArticleFEBS letters2020
Enterococcus faecalis α1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification.
Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Biochemical characterization of the α-1,3-mannosidase AnGH92A from Aspergillus nidulans.Scientific reports · 2026Article
- Poking at probiotic mechanisms and microbial implications in cancer prevention and treatment.Gut · 2024Article
- Article
- Complete Genome Analysis ofMicroorganisms · 2023Article
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis.Acta crystallographica. Section D, Structural biology · 2023Article
- Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed inMolecules (Basel, Switzerland) · 2023Article
- PlantProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Analysis of fungal high-mannose structures using CAZymes.Glycobiology · 2022Article
- Unlocking the Hydrolytic Mechanism of GH92 α-1,2-Mannosidases: Computation Inspires the use of C-Glycosides as Michaelis Complex Mimics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Activity of CcpA-Regulated GH18 Family Glycosyl Hydrolases That Contributes to Nutrient Acquisition and Fitness in Enterococcus faecalis.Infection and immunity · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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