Publications by authors named "Xing Yu Mou"
Pseudomonas aeruginosa, a versatile bacterium, has dual significance because of its beneficial roles in environmental soil processes and its detrimental effects as a nosocomial pathogen that causes clinical infections. Understanding adaptability to environmental stress is essential. This investigation delves into the complex interplay of two-component system (TCS), specifically ParRS and CprRS, as P.
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- 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.
Structural analysis of the sulfatase AmAS from Akkermansia muciniphila.
Acta Crystallogr D Struct Biol
December 2021
Article Synopsis
- 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.
Structural and biochemical analysis of 1-Cys peroxiredoxin ScPrx1 from Saccharomyces cerevisiae mitochondria.
Biochim Biophys Acta Gen Subj
December 2020
Article Synopsis
- ScPrx1 is a yeast mitochondrial enzyme that protects cells from oxidative stress by utilizing reducing agents like ScTrx3 and glutathione, but its substrate recognition mechanism still needs further investigation.
- The study determined the structure and oligomeric state of ScPrx1, revealing it exists as a homodimer with specific mutations enhancing or reducing its catalytic activity.
- The findings suggest that changes in the C-terminal segment and certain loop regions of ScPrx1 are crucial for its catalytic function and its ability to use various reductants.