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Title
  • en A Novel Eliminase from a Marine Bacterium That Degrades Hyaluronan and Chondroitin Sulfate
Creator
    • en Han, Wenjun
    • en Wang, Wenshuang
    • en Zhao, Mei
    • en Li, Fuchuan
Accessrights open access
Rights
  • en This research was originally published in Journal of Biological Chemistry. Wenjun Han, Wenshuang Wang, Mei Zhao, Kazuyuki Sugahara and Fuchuan Li. A Novel Eliminase from a Marine Bacterium That Degrades Hyaluronan and Chondroitin Sulfate. Journal of Biological Chemistry. 2014; Vol:289(40) p.27886-27898 © the American Society for Biochemistry and Molecular Biology
Subject
  • Other en Chondroitin Sulfate
  • Other en Glycosaminoglycan
  • Other en Hyaluronan
  • Other en Hyaluronidase
  • Other en Proteoglycan
  • Other en Chondroitinase
  • Other en Eliminase
  • Other en Lyase
  • Other en Marine Bacterium
  • NDC 460
Description
  • Abstract en 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 Δ4,5HexUAα1-3GalNAc(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.
Publisher en American Society for Biochemistry and Molecular Biology (ASBMB)
Date
    Issued2014-10-03
Language
  • eng
Resource Type journal article
Version Type VoR
Identifier HDL http://hdl.handle.net/2115/62912
Relation
  • isIdenticalTo DOI https://doi.org/10.1074/jbc.M114.590752
  • PMID 25122756
Journal
    • PISSN 0021-9258
    • EISSN 1083-351X
      • en Journal of Biological Chemistry
      • Volume Number289 Issue Number40 Page Start27886 Page End27898
File
Oaidate 2023-08-19