ArticleThe Journal of biological chemistry2011
Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 79 citations in OpenAlex.
- Late Stage Mannan Metabolism in Cellvibrio japonicus Requires the Combined Action of a Mannosyl-Glucose Phosphorylase and a Mannobiose Epimerase.Molecular microbiology · 2026Article
- Genomic and phenotypic characterisation of Leeuwenhoekiella obamensis sp. nov., a novel marine bacterium isolated from the surface water of a Japanese fishing port.Antonie van Leeuwenhoek · 2025Article
- MAN2B1 in immune system-related diseases, neurodegenerative disorders and cancers: functions beyond α-mannosidosis.Expert reviews in molecular medicine · 2024Review
- Effects of Cold Plasma Pretreatment on the Synthesis of Polysaccharide from Pleurotus ostreatus.Applied biochemistry and biotechnology · 2024Article
- Mechanism of high-mannose N-glycan breakdown and metabolism by Bifidobacterium longum.Nature chemical biology · 2023Article
- Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides.Communications biology · 2023Article
- Combining the In Silico and In Vitro Assays to IdentifyPharmaceuticals (Basel, Switzerland) · 2023Article
- A Rapid Protocol for Preparing 8-Aminopyrene-1,3,6-Trisulfonate-Labeled Glycans for Capillary Electrophoresis-Based Enzyme Assays.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Separation and Visualization of Glycans by Fluorophore-Assisted Carbohydrate Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. Hel_I_6 consumes alpha-mannan from fungi.The ISME journal · 2022Article
- Mechanistic insights into consumption of the food additive xanthan gum by the human gut microbiota.Nature microbiology · 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
- Microbial iron and carbon metabolism as revealed by taxonomy-specific functional diversity in the Southern Ocean.The ISME journal · 2021Article
- MonteCarbo: A software to generate and dock multifunctionalized ring molecules.Journal of computational chemistry · 2021Article
- Quantifying fluorescent glycan uptake to elucidate strain-level variability in foraging behaviors of rumen bacteria.Microbiome · 2021Article
- Structure and function ofThe Journal of biological chemistry · 2020Article
- Host-glycan metabolism is regulated by a species-conserved two-component system in Streptococcus pneumoniae.PLoS pathogens · 2020Article
- Two complementary α-fucosidases fromThe Journal of biological chemistry · 2019Article
- Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The modification of N-glycans by α-mannosidases is a process that is relevant to a large number of biologically important processes, including infection by microbial pathogens and colonization by microbial symbionts. At present, the described mannosidases specific for α1,6-mannose linkages are very limited in number. Through structural and functional analysis of two sequence-related enzymes, one from Streptococcus pneumoniae (SpGH125) and one from Clostridium perfringens (CpGH125), a new glycoside hydrolase family, GH125, is identified and characterized. Analysis of SpGH125 and CpGH125 reveal them to have exo-α1,6-mannosidase activity consistent with specificity for N-linked glycans having their α1,3-mannose branches removed. The x-ray crystal structures of SpGH125 and CpGH125 obtained in apo-, inhibitor-bound, and substrate-bound forms provide both mechanistic and molecular insight into how these proteins, which adopt an (α/α)(6)-fold, recognize and hydrolyze the α1,6-mannosidic bond by an inverting, metal-independent catalytic mechanism. A phylogenetic analysis of GH125 proteins reveals this to be a relatively large and widespread family found frequently in bacterial pathogens, bacterial human gut symbionts, and a variety of fungi. Based on these studies we predict this family of enzymes will primarily comprise such exo-α1,6-mannosidases.
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Registered trials
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