The human genome doesn't contain the genes coding for xyloglucan degradation even though xyloglucans are an important component of most human diets. Recent studies have shown that a discrete genetic locus confers xyloglucan metabolism in selected human gut Bacteroidota. This findings reveals that the metabolism of even highly abundant components of dietary fiber maybe mediated by niche species.
The metabolism of xyloglucans is the result of the concerted action of several enzymes and membrane transporters. However, given the high diversity of composition of xyloglucans from different plant sources, there is a keystone enzyme, an endo-xyloglucanase called BoGH5A, that has the ability to cleave a range of xyloglucans to generate short xyloglucans ready for uptake. A detailed analysis of the structure and function of the enzyme has revealed the presence of a domain called the BACON domain whose primary function in BoGH5A may be to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain to attack the polysaccharide. A broad active-site cleft engendering binding plasticity is the key feature allowing BoGH5A which allows it to accommodate a wide range of natural XyGs.
The prevalence of XyGs in the human diet suggests that the mechanism by which bacteria degrade these complex polysaccharides is highly important to human energy acquisition. Moreover, the rarity of XyG metabolism highlights the significance of Bacteroides ovatus and other proficient XyG-degrading Bacteroidota as key members of the human gut microbial consortium.[5]