ArticlePloS one2015
Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 21 citations in OpenAlex.
- Sequence-Based and Functional Analysis for the Discovery of N-Glycan Degrading Glycosidases From the Microbial Metagenome of the Infant Gut.MicrobiologyOpen · 2026Article
- The chitinolytic enzymes from the entomopathogenic fungusFrontiers in fungal biology · 2026Review
- Expansion of the diversity of dispersin scaffolds.Acta crystallographica. Section D, Structural biology · 2025Article
- Discovery of Lacto-N-Biosidases and a Novel N-Acetyllactosaminidase Activity in the CAZy Family GH20: Functional Diversity and Structural Insights.Chembiochem : a European journal of chemical biology · 2025Article
- Enzymatic Hydrolysis of Human Milk Oligosaccharides. The Molecular Mechanism ofACS catalysis · 2022Article
- The Role of ChitooligosaccharidolyticInternational journal of molecular sciences · 2022Article
- Activity of CcpA-Regulated GH18 Family Glycosyl Hydrolases That Contributes to Nutrient Acquisition and Fitness in Enterococcus faecalis.Infection and immunity · 2021Article
- Metabolism of Poly-β1,4-Journal of bacteriology · 2021Article
- Structural basis of chitin utilization by a GH20 β-N-acetylglucosaminidase from Vibrio campbellii strain ATCC BAA-1116.Acta crystallographica. Section D, Structural biology · 2021Article
- Transglycosylation Activity of EngineeredInternational journal of molecular sciences · 2021Article
- Article
- Identification and Characterization of a β-International journal of molecular sciences · 2020Article
- Genomic and transcriptomic landscapes and evolutionary dynamics of molluscan glycoside hydrolase families with implications for algae-feeding biology.Computational and structural biotechnology journal · 2020Article
- Proteomic Analysis Revealed the Fruiting-Body Protein Profile of Auricularia polytricha.Current microbiology · 2017Article
- A Second β-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans.The Journal of biological chemistry · 2015Article
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hexosaminidases are involved in important biological processes catalyzing the hydrolysis of N-acetyl-hexosaminyl residues in glycosaminoglycans and glycoconjugates. The GH20 enzymes present diverse domain organizations for which we propose two minimal model architectures: Model A containing at least a non-catalytic GH20b domain and the catalytic one (GH20) always accompanied with an extra α-helix (GH20b-GH20-α), and Model B with only the catalytic GH20 domain. The large Bifidobacterium bifidum lacto-N-biosidase was used as a model protein to evaluate the minimal functional unit due to its interest and structural complexity. By expressing different truncated forms of this enzyme, we show that Model A architectures cannot be reduced to Model B. In particular, there are two structural requirements general to GH20 enzymes with Model A architecture. First, the non-catalytic domain GH20b at the N-terminus of the catalytic GH20 domain is required for expression and seems to stabilize it. Second, the substrate-binding cavity at the GH20 domain always involves a remote element provided by a long loop from the catalytic domain itself or, when this loop is short, by an element from another domain of the multidomain structure or from the dimeric partner. Particularly, the lacto-N-biosidase requires GH20b and the lectin-like domain at the N- and C-termini of the catalytic GH20 domain to be fully soluble and functional. The lectin domain provides this remote element to the active site. We demonstrate restoration of activity of the inactive GH20b-GH20-α construct (model A architecture) by a complementation assay with the lectin-like domain. The engineering of minimal functional units of multidomain GH20 enzymes must consider these structural requirements.
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