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Functional and structural characterization of a heparanase

Journal Article


Abstract


  • We report the structural and functional characterization of a novel heparanase (BpHep) from the invasive pathogenic bacterium Burkholderia pseudomallei (Bp), showing ∼24% sequence identity with human heparanase (hHep). Site-directed mutagenesis studies confirmed the active site resi-dues essential for activity, and we found that BpHep has specificity for heparan sulfate. Finally, we describe the first heparanase X-ray crystal structure, which provides new insight into both substrate recognition and inhibitor design.

Publication Date


  • 2015

Citation


  • Bohlmann, L., Tredwell, G. D., Yu, X., Chang, C. W., Haselhorst, T., Winger, M., . . . Von Itzstein, M. (2015). Functional and structural characterization of a heparanase. Nature Chemical Biology, 11(12), 955-957. doi:10.1038/nchembio.1956

Scopus Eid


  • 2-s2.0-84947775390

Start Page


  • 955

End Page


  • 957

Volume


  • 11

Issue


  • 12

Abstract


  • We report the structural and functional characterization of a novel heparanase (BpHep) from the invasive pathogenic bacterium Burkholderia pseudomallei (Bp), showing ∼24% sequence identity with human heparanase (hHep). Site-directed mutagenesis studies confirmed the active site resi-dues essential for activity, and we found that BpHep has specificity for heparan sulfate. Finally, we describe the first heparanase X-ray crystal structure, which provides new insight into both substrate recognition and inhibitor design.

Publication Date


  • 2015

Citation


  • Bohlmann, L., Tredwell, G. D., Yu, X., Chang, C. W., Haselhorst, T., Winger, M., . . . Von Itzstein, M. (2015). Functional and structural characterization of a heparanase. Nature Chemical Biology, 11(12), 955-957. doi:10.1038/nchembio.1956

Scopus Eid


  • 2-s2.0-84947775390

Start Page


  • 955

End Page


  • 957

Volume


  • 11

Issue


  • 12