Computational studies of GH29B

Glycans are important for human health and development, especially for early life growth. Human milk oligosaccharides (HMOs), for example, may benefit breast-fed infant in multiple ways; acting as prebiotics, antiadhesive antimicrobials, directly affect intestinal cells, modulating the immune system in multiple ways, and serving as essential nutrients for brain development and cognition. [1] HMOs are absent from bovine milk and are thus not present in most infant formula.

In the context of diseases, cancer cells often display differential expression levels of critical glycans [2] and various pathogens evade the immune system by utilizing glycans to avoid detection. Glycans are so essential to the immune system that they could be described as the workhorse of the immune system [2,3].

Enzyme catalysed transglycosylation is one way of producing HMOs from natural substrates. Engineering glycosidase hydrolases (GHs) to improve transglycosylation yields, is a promising avenue for high value/ low-cost HMO production. We are interested in utilizing computational chemistry methods to investigate the active site of GSs to study the balance between the two reactions these enzymes catalyze, hydrolysis and transglycosylation, and to be able to tailor the protein environment towards one or the other.