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Structural insights into heparanase activity using a fluorogenic heparan sulfate disaccharide

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Publication details

JournalChemical Communications
DateAccepted/In press - 9 Oct 2020
DateE-pub ahead of print - 10 Oct 2020
DatePublished (current) - 18 Nov 2020
Issue number89
Number of pages4
Pages (from-to)13780-13783
Early online date10/10/20
Original languageEnglish


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.

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