ArticleBiochemistry2023
Electrostatic Interactions Dictate Bile Salt Hydrolase Substrate Preference.
Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- A class of metallohydrolases expands bile salt hydrolase activity in the gut.bioRxiv : the preprint server for biology · 2026Article
- A previously unappreciated class of metal-dependent bile salt hydrolases from the human gut microbiome.bioRxiv : the preprint server for biology · 2026Article
- Chemical Proteomics Reveals Regulation of Bile Salt Hydrolases via Oxidative Post-translational Modifications.Journal of the American Chemical Society · 2026Article
- Chemical proteomics reveals regulation of bile salt hydrolases via oxidative post-translational modifications.bioRxiv : the preprint server for biology · 2025Article
- Chemoproteomic profiling of substrate specificity in gut microbiota-associated bile salt hydrolases.Cell chemical biology · 2025Article
- Metagenomic, metabolomic, and lipidomic shifts associated with fecal microbiota transplantation for recurrentmSphere · 2024Article
- Structural and functional analysis of a bile salt hydrolase from the bison microbiome.The Journal of biological chemistry · 2024Article
- Chemoproteomic profiling of substrate specificity in gut microbiota-associated bile salt hydrolases.bioRxiv : the preprint server for biology · 2024Article
- Bile acids impact the microbiota, host, andGut microbesReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The human intestines are colonized by trillions of microbes, comprising the gut microbiota, which produce diverse small molecule metabolites and modify host metabolites, such as bile acids, that regulate host physiology. Biosynthesized in the liver, bile acids are conjugated with glycine or taurine and secreted into the intestines, where gut microbial bile salt hydrolases (BSHs) deconjugate the amino acid to produce unconjugated bile acids that serve as precursors for secondary bile acid metabolites. Among these include a recently discovered class of microbially conjugated bile acids (MCBAs), wherein alternative amino acids are conjugated onto bile acids. To elucidate the metabolic potential of MCBAs, we performed detailed kinetic studies to investigate the preference of BSHs for host-conjugated bile acids and MCBAs. We identified a BSH that exhibits positive cooperativity uniquely for MCBAs containing an aromatic side chain. Further molecular modeling and phylogenetic analyses indicated that the BSH preference for aromatic MCBAs is due to a substrate-specific cation-π interaction and is predicted to be widespread among human gut microbial BSHs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.