ArticleThe Journal of biological chemistry2014
The β-glucanase ZgLamA from Zobellia galactanivorans evolved a bent active site adapted for efficient degradation of algal laminarin.
Article in The Journal of biological chemistry, 2014. 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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31 citing papers in PubMed, 85 citations in OpenAlex.
- Functions of the cell wall polysaccharide schizophyllan during vegetative growth ofCell surface (Amsterdam, Netherlands) · 2026Article
- A novel acidic laminarinase derived from Jermuk hot spring metagenome.Applied microbiology and biotechnology · 2025Article
- Genes for laminarin degradation are dispersed in the genomes of particle-associatedFrontiers in microbiology · 2024Article
- Structural basis of EHEP-mediated offense against phlorotannin-induced defense from brown algae to protecteLife · 2023Article
- Consuming fresh macroalgae induces specific catabolic pathways, stress reactions and Type IX secretion in marine flavobacterial pioneer degraders.The ISME journal · 2022Article
- Connecting Algal Polysaccharide Degradation to Formaldehyde Detoxification.Chembiochem : a European journal of chemical biology · 2022Article
- From Cancer Therapy to Winemaking: The Molecular Structure and Applications of β-Glucans and β-1, 3-Glucanases.International journal of molecular sciences · 2022Review
- Identification and structural analysis of a thermophilic β-1,3-glucanase from compost.Bioresources and bioprocessing · 2021Article
- North Sea spring bloom-associated Gammaproteobacteria fill diverse heterotrophic niches.Environmental microbiome · 2021Article
- Analysis and application of a suite of recombinant endo-β(1,3)-D-glucanases for studying fungal cell walls.Microbial cell factories · 2021Article
- Genome-Wide Analysis of PL7 Alginate Lyases in the GenusMolecules (Basel, Switzerland) · 2021Article
- CAZymes inFrontiers in microbiology · 2021Article
- Molecular Basis for Substrate Recognition and Catalysis by a Marine Bacterial Laminarinase.Applied and environmental microbiology · 2020Article
- If you eat it, or secrete it, they will grow: the expanding list of nutrients utilized by human gut bacteria.Journal of bacteriology · 2020Review
- Article
- Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown.Nature communications · 2020Article
- Laminarin is a major molecule in the marine carbon cycle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The agar-specific hydrolaseThe Journal of biological chemistry · 2019Article
- Adaptations ofFrontiers in microbiology · 2019Article
- Biphasic cellular adaptations and ecological implications of Alteromonas macleodii degrading a mixture of algal polysaccharides.The ISME journal · 2019Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminarinase is commonly used to describe β-1,3-glucanases widespread throughout Archaea, bacteria, and several eukaryotic lineages. Some β-1,3-glucanases have already been structurally and biochemically characterized, but very few from organisms that are in contact with genuine laminarin, the storage polysaccharide of brown algae. Here we report the heterologous expression and subsequent biochemical and structural characterization of ZgLamAGH16 from Zobellia galactanivorans, the first GH16 laminarinase from a marine bacterium associated with seaweeds. ZgLamAGH16 contains a unique additional loop, compared with other GH16 laminarinases, which is composed of 17 amino acids and gives a bent shape to the active site cleft of the enzyme. This particular topology is perfectly adapted to the U-shaped conformation of laminarin chains in solution and thus explains the predominant specificity of ZgLamAGH16 for this substrate. The three-dimensional structure of the enzyme and two enzyme-substrate complexes, one with laminaritetraose and the other with a trisaccharide of 1,3-1,4-β-d-glucan, have been determined at 1.5, 1.35, and 1.13 Å resolution, respectively. The structural comparison of substrate recognition pattern between these complexes allows the proposition that ZgLamAGH16 likely diverged from an ancestral broad specificity GH16 β-glucanase and evolved toward a bent active site topology adapted to efficient degradation of algal laminarin.
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