ArticleThe Journal of biological chemistry2014
Structure of a PL17 family alginate lyase demonstrates functional similarities among exotype depolymerases.
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 50 papers.
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50 citing papers in PubMed, 99 citations in OpenAlex.
- Genomic and Phenotypic Analysis of Antarctic Marine Cryobacterium sp. PAMC25264.Current microbiology · 2026Article
- Structural and functional insights into Uly1040, an ulvan lyase from polysaccharide lyase family 40.Applied and environmental microbiology · 2026Article
- Article
- Characterization of a novel alginate lyase Alg0392 with organic solvent-tolerance from Alteromonas sp. A1-6.Applied microbiology and biotechnology · 2025Article
- Insights into the mechanism of substrate specificity in a novel PL15_3 subfamily oligo-alginate lyase VBAly15A.Applied and environmental microbiology · 2025Article
- Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovery of a novel marine Bacteroidetes with a rich repertoire of carbohydrate-active enzymes.Computational and structural biotechnology journal · 2024Article
- Alginate oligosaccharide assimilation by gut microorganisms and the potential role in gut inflammation alleviation.Applied and environmental microbiology · 2024Article
- Metagenomic insights into the dynamic degradation of brown algal polysaccharides by kelp-associated microbiota.Applied and environmental 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
- Three alginate lyases provide a new gutApplied and environmental microbiology · 2023Article
- Structure-Activity Relationships of Low Molecular Weight Alginate Oligosaccharide Therapy againstBiomolecules · 2023Article
- A novel alginate lyase and its domain functions for the preparation of unsaturated monosaccharides.Applied microbiology and biotechnology · 2023Article
- Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine BacteriumMarine drugs · 2022Article
- Alginate Lyases from Marine Bacteria: An Enzyme Ocean for Sustainable Future.Molecules (Basel, Switzerland) · 2022Review
- Degradation of Alginate by a Newly Isolated Marine BacteriumMarine drugs · 2022Article
- Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine BacteriumMarine drugs · 2022Article
- Evolving strategies for marine enzyme engineering: recent advances on the molecular modification of alginate lyase.Marine life science & technology · 2022Review
- Structure-function analysis of a new PL17 oligoalginate lyase from the marine bacterium Zobellia galactanivorans DsijT.Glycobiology · 2021Article
- Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases.Marine drugs · 2021Review
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Brown macroalgae represent an ideal source for complex polysaccharides that can be utilized as precursors for cellulosic biofuels. The lack of recalcitrant lignin components in macroalgae polysaccharide reserves provides a facile route for depolymerization of constituent polysaccharides into simple monosaccharides. The most abundant sugars in macroalgae are alginate, mannitol, and glucan, and although several classes of enzymes that can catabolize the latter two have been characterized, studies of alginate-depolymerizing enzymes have lagged. Here, we present several crystal structures of Alg17c from marine bacterium Saccharophagus degradans along with structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization. This represents the first structural and biochemical characterization of a family 17 polysaccharide lyase enzyme. Despite the lack of appreciable sequence conservation, the structure and β-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases. This work illuminates the evolutionary relationships among enzymes within this unexplored class of polysaccharide lyases and reinforces the notion of a structure-based hierarchy in the classification of these enzymes.
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