Structural insights into heparanase activity using a fluorogenic heparan sulfate disaccharide

Liang Wu, Norbert Wimmer, Gideon J. Davies*, Vito Ferro

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


A synthetic heparan sulfate disaccharide has been assessed as a fluorogenic heparanase substrate, enabling enzyme turnover and inhibition kinetics measurements despite slow turnover. Crystal structures with human heparanase also provide the first ever observation of a substrate in an activated 1S3 conformation, highlighting previously unknown interactions involved in enzymatic processing. Our data provide insights into the heparanase catalytic mechanism, and will inform the design of improved heparanase substrates and inhibitors.

Original languageEnglish
Pages (from-to)13780-13783
Number of pages4
JournalChemical Communications
Issue number89
Early online date10 Oct 2020
Publication statusPublished - 18 Nov 2020

Cite this