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Discovery of exolytic heparinases and their catalytic mechanism and potential application

Author

Listed:
  • Qingdong Zhang

    (Shandong University)

  • Hai-Yan Cao

    (Shandong University
    Ocean University of China
    Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingdao))

  • Lin Wei

    (Shandong University)

  • Danrong Lu

    (Shandong University)

  • Min Du

    (Shandong University)

  • Min Yuan

    (Shandong University)

  • Deling Shi

    (Shandong University)

  • Xiangxue Chen

    (Tiandong Pharma)

  • Peng Wang

    (Ocean University of China
    Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingdao))

  • Xiu-Lan Chen

    (Shandong University
    Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingdao))

  • Lianli Chi

    (Shandong University)

  • Yu-Zhong Zhang

    (Ocean University of China
    Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingdao))

  • Fuchuan Li

    (Shandong University)

Abstract

Heparinases (Hepases) are critical tools for the studies of highly heterogeneous heparin (HP)/heparan sulfate (HS). However, exolytic heparinases urgently needed for the sequencing of HP/HS chains remain undiscovered. Herein, a type of exolytic heparinases (exoHepases) is identified from the genomes of different bacteria. These exoHepases share almost no homology with known Hepases and prefer to digest HP rather than HS chains by sequentially releasing unsaturated disaccharides from their reducing ends. The structural study of an exoHepase (BIexoHep) shows that an N-terminal conserved DUF4962 superfamily domain is essential to the enzyme activities of these exoHepases, which is involved in the formation of a unique L-shaped catalytic cavity controlling the sequential digestion of substrates through electrostatic interactions. Further, several HP octasaccharides have been preliminarily sequenced by using BIexoHep. Overall, this study fills the research gap of exoHepases and provides urgently needed tools for the structural and functional studies of HP/HS chains.

Suggested Citation

  • Qingdong Zhang & Hai-Yan Cao & Lin Wei & Danrong Lu & Min Du & Min Yuan & Deling Shi & Xiangxue Chen & Peng Wang & Xiu-Lan Chen & Lianli Chi & Yu-Zhong Zhang & Fuchuan Li, 2021. "Discovery of exolytic heparinases and their catalytic mechanism and potential application," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21441-8
    DOI: 10.1038/s41467-021-21441-8
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