ArticleThe Journal of biological chemistry2014
A novel eliminase from a marine bacterium that degrades hyaluronan and chondroitin sulfate.
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 29 papers.
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Who cites it
29 citing papers in PubMed, 66 citations in OpenAlex.
- Cloning and Characterization of a PL6 Alginate Lyase Aly94 from the Marine Bacteria.Molecular biotechnology · 2026Article
- Environmental gradients and habitat specificity structure benthic microbial assemblages in a temperate seagrass ecosystem.bioRxiv : the preprint server for biology · 2026Article
- Characterization of a NaWorld journal of microbiology & biotechnology · 2025Article
- Pharmaceutical applications of halophilic enzymes.Heliyon · 2025Review
- A novelFrontiers in microbiology · 2025Article
- A comprehensive review on microbial hyaluronan-degrading enzymes: from virulence factors to biotechnological tools.Bioresources and bioprocessing · 2024Review
- Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1.Microorganisms · 2024Article
- Efficient Expression and Characterization of an Endo-Type Lyase HCLase_M28 and Its Gradual Scale-Up Fermentation for the Preparation of Chondroitin Sulfate Oligosaccharides.Applied biochemistry and biotechnology · 2024Article
- Cloning and Biochemical Characterization of a Hyaluronate Lyase fromJournal of microbiology and biotechnology · 2023Article
- Hungatella hathewayi, an Efficient Glycosaminoglycan-DegradingApplied and environmental microbiology · 2022Article
- Biochemical and Molecular Characteristics of a Novel Hyaluronic Acid Lyase fromFoods (Basel, Switzerland) · 2022Article
- Characterization of a Thermostable and Surfactant-Tolerant Chondroitinase B from a Marine BacteriumInternational journal of molecular sciences · 2022Article
- Identification and Biochemical Characterization of a Surfactant-Tolerant Chondroitinase VhChlABC fromMarine drugs · 2021Article
- Discovery of exolytic heparinases and their catalytic mechanism and potential application.Nature communications · 2021Article
- Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine BacteriumFrontiers in microbiology · 2021Article
- A Technical System for the Large-Scale Application of Metabolites FromFrontiers in bioengineering and biotechnology · 2021Article
- Characterization of a Hyaluronic Acid Utilization Locus and Identification of Two Hyaluronate Lyases in a Marine BacteriumFrontiers in microbiology · 2021Article
- Assembling custom side chains on proteoglycans to interrogate their function in living cells.Nature communications · 2020Article
- Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes.Frontiers in cell and developmental biology · 2020Review
- Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lyases cleave glycosaminoglycans (GAGs) in an eliminative mechanism and are important tools for the structural analysis and oligosaccharide preparation of GAGs. Various GAG lyases have been identified from terrestrial but not marine organisms even though marine animals are rich in GAGs with unique structures and functions. Herein we isolated a novel GAG lyase for the first time from the marine bacterium Vibrio sp. FC509 and then recombinantly expressed and characterized it. It showed strong lyase activity toward hyaluronan (HA) and chondroitin sulfate (CS) and was designated as HA and CS lyase (HCLase). It exhibited the highest activities to both substrates at pH 8.0 and 0.5 m NaCl at 30 °C. Its activity toward HA was less sensitive to pH than its CS lyase activity. As with most other marine enzymes, HCLase is a halophilic enzyme and very stable at temperatures from 0 to 40 °C for up to 24 h, but its activity is independent of divalent metal ions. The specific activity of HCLase against HA and CS reached a markedly high level of hundreds of thousands units/mg of protein under optimum conditions. The HCLase-resistant tetrasaccharide Δ(4,5)HexUAα1-3GalNAc(6-O-sulfate)β1-4GlcUA(2-O-sulfate)β1-3GalNAc(6-O-sulfate) was isolated from CS-D, the structure of which indicated that HCLase could not cleave the galactosaminidic linkage bound to 2-O-sulfated d-glucuronic acid (GlcUA) in CS chains. Site-directed mutagenesis indicated that HCLase may work via a catalytic mechanism in which Tyr-His acts as the Brønsted base and acid. Thus, the identification of HCLase provides a useful tool for HA- and CS-related research and applications.
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