Divergent evolution for diverse substrate recognition by family 31 glycoside hydrolases.

Carbohydrates make up an important component of our diet, contributing a significant portion to our total caloric intake. The ability to harvest these molecules for energy is reliant on the activity of carbohydrate-active enzymes. Family 31 α-glucosidases are a group of glycoside hydrolases that has been shown to play a key role in the metabolic process of hydrolyzing dietary starch into monomers of glucose. The purpose of the research presented here is to explore evolutionary changes that occurred within this family of glycoside hydrolases, and to relate these divergences to observed structural differences in relation to predicted substrate preferences. Here we report specific single amino acid changes that are believed to have arisen through evolution, and are directly related to the ability of these enzymes to bind different starch-based glycans. Through phylogenetic analysis we observed a number of evolutionary adaptions that we believe resulted in duplicated genes that allow for the efficient utilization of dietary starch.