ArticleThe Journal of biological chemistry2013
Comparative characterization of two marine alginate lyases from Zobellia galactanivorans reveals distinct modes of action and exquisite adaptation to their natural substrate.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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93 citing papers in PubMed, 196 citations in OpenAlex.
- Biocatalytic ulvan degradation by Pseudoalteromonas marina: exploring a marine polysaccharide bioconversion system.Microbial cell factories · 2026Article
- Spatiotemporal regulation of alginate sub-structures at multiple scales revealed by monoclonal antibodies.Cell surface (Amsterdam, Netherlands) · 2025Article
- Diatom heterotrophy on brown algal polysaccharides emerged through horizontal gene transfer, gene duplication, and neofunctionalization.PLoS biology · 2025Article
- Insights into the mechanism of substrate specificity in a novel PL15_3 subfamily oligo-alginate lyase VBAly15A.Applied and environmental microbiology · 2025Article
- Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation.Nature communications · 2025Article
- A comparative study of the efficacy of alginate lyases in the presence of metal ions elevated in the cystic fibrosis lung milieu.Biochemistry and biophysics reports · 2024Article
- Degradation of NaturalMarine drugs · 2024Article
- Analysis of unsaturated alginate oligosaccharides using high-performance anion exchange chromatography coupled with mass spectrometry.Analytical and bioanalytical chemistry · 2024Article
- High-Level Extracellular Production of a Trisaccharide-Producing Alginate Lyase AlyC7 inMarine drugs · 2024Article
- Comparative molecular dynamics simulations provided insights into the mechanisms of cold-adaption of alginate lyases from the PL7 family.Extremophiles : life under extreme conditions · 2024Article
- A bifunctional endolytic alginate lyase with two different lyase catalytic domains fromFrontiers in microbiology · 2024Article
- Characterization and Mechanism Study of a Novel PL7 Family Exolytic Alginate Lyase from Marine Bacteria Vibrio sp. W13.Applied biochemistry and biotechnology · 2024Article
- Carbohydrates and carbohydrate degradation gene abundance and transcription in Atlantic waters of the Arctic.ISME communications · 2023Article
- Three alginate lyases provide a new gutApplied and environmental microbiology · 2023Article
- Genome Sequencing-Based Mining and Characterization of a Novel Alginate Lyase fromMarine drugs · 2023Article
- Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily.Frontiers in microbiology · 2023Article
- Characterization of Multiple Alginate Lyases in a Highly Efficient Alginate-DegradingApplied and environmental microbiology · 2022Article
- Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase fromApplied and environmental microbiology · 2022Article
- Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine BacteriumMarine drugs · 2022Article
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33 more citing papers are in PubMed but not listed here.
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8 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Cell walls of brown algae are complex supramolecular assemblies containing various original, sulfated, and carboxylated polysaccharides. Among these, the major marine polysaccharide component, alginate, represents an important biomass that is successfully turned over by the heterotrophic marine bacteria. In the marine flavobacterium Zobellia galactanivorans, the catabolism and uptake of alginate are encoded by operon structures that resemble the typical Bacteroidetes polysaccharide utilization locus. The genome of Z. galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes. This study reports on the detailed biochemical and structural characterization of two of these. We demonstrate here that AlyA1PL7 is an endolytic guluronate lyase, and AlyA5 cleaves unsaturated units, α-L-guluronate or β-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1(PL7), whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. Finally, in contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism suggesting an exquisite adaptation to their natural substrate in the context of brown algal cell walls.
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