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A Novel Eliminase from a Marine Bacterium That Degrades Hyaluronan and Chondroitin Sulfate

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Title: A Novel Eliminase from a Marine Bacterium That Degrades Hyaluronan and Chondroitin Sulfate
Authors: Han, Wenjun Browse this author
Wang, Wenshuang Browse this author
Zhao, Mei Browse this author
Sugahara, Kazuyuki Browse this author →KAKEN DB
Li, Fuchuan Browse this author
Keywords: Chondroitin Sulfate
Marine Bacterium
Issue Date: 3-Oct-2014
Publisher: American Society for Biochemistry and Molecular Biology (ASBMB)
Journal Title: Journal of Biological Chemistry
Volume: 289
Issue: 40
Start Page: 27886
End Page: 27898
Publisher DOI: 10.1074/jbc.M114.590752
PMID: 25122756
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 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.
Rights: 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
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 菅原 一幸

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