β--acetylhexosaminidases from the GH20 family are crucial enzymes for modifying oligosaccharides, with significant roles in biology and biotechnology.
The study focused on Am2136, a specific β--acetylhexosaminidase from an anaerobic gut bacterium, demonstrating its ability to cleave mucin glycans and highlighting its generalist nature by hydrolyzing β-linkages of various substrates.
The research also uncovered that the enzyme's activity is enhanced by nucleotides, suggesting a novel regulatory mechanism linked to structural interactions between enzyme domains, which could facilitate the development of targeted glycan-modifying catalysts.
Akkermansia muciniphila is a significant gut bacterium that helps modulate immune responses and provides nutrients for intestinal health.
Research focused on the structure of its sulfatase enzyme, AmAS, revealing key areas that are critical for its function and substrate binding.
Understanding the structural differences in these sulfatases could clarify their roles in breaking down complex sugars and their interactions within the human gut.