bioRxivJClub
Mapping bacterial bile amidation across the bile salt hydrolase family
bioRxiv · · Preprint · Open access
Skrip, Prasad + 16 more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
Across 115 bacterial bile salt hydrolases (BSHs), distinct amine specificities were revealed, linking BSH sequence to transaminase function and defining which bacterial bile amidates (BBAs) can form.
- Why it matters: Enzyme activity and substrate specificity are hard to resolve in complex gut microbiomes, and it remains unclear which BSHs generate which BBAs that may matter for human health.
- What they did: The study tested transaminase activities of 115 BSHs and used molecular networking to map distinct amine preferences, then mined public metabolomics data to find enzymatically generated BBAs across human samples.
- The result: Enzymatically generated BBAs were detected across life-stage, tissue-, and disease-specific human samples, implying previously unrecognized catalytic diversity of BSHs relevant to human health.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.
- Open access