Scientists from DTU Biosustain and DTU Bioengineering have finally been able to explain the long mysterious mechanism at work with the enzyme N-acetylgalactosaminidase (GH109). This enzyme can convert abundant “beta sugars” into “alpha sugars” that have some therapeutic properties. The new research on its chemistry has provided an array of possible applications and is published in the journal, ACS Catalysis.
David Teze, interim Group Leader of Enzyme Engineering at The Novo Nordisk Foundation Center for Biosustainability (DTU Biosustain) and first-author of this publication notes, “We are very excited to have discovered how this human symbiont uses so far unknown chemistry to feed on human sugars. Now that we understand the chemistry behind this mode of action, we can change the enzyme to make valuable sugars.”
GH109 is found in human gut bacteria and is responsible for breaking down the sugars in the mucus found in the gut. By degrading these sugars, GH109 makes them “alpha-GalNAc” which feeds GH109 itself. It is possible that GH109 could be utilized to add alpha-GalNAc to other compounds. Alpha-GalNAc is part of a common cancer antigen called the Thomsen-Friedenreich antigen (Galβ1-3GalNAcα1). Thus, alpha-GalNAc sugars could be used to create cancer vaccines.
Teze continues, “Alpha-GalNAc containing sugars could be protective against cancer, but it is hard to synthesize enough of them for vaccines. But now, we may be able to optimize an enzyme to produce them biotechnologically.”