ArticleScientific reports2019
The complex structure of bile salt hydrolase from Lactobacillus salivarius reveals the structural basis of substrate specificity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Using meta-analysis to understand the impacts of dietary protein and fat content on the composition of fecal microbiota of domestic dogs (Canis lupus familiaris): A pilot study.MicrobiologyOpen · 2024Pooled it
- Probiotic and safety characterization of Lactiplantibacillus plantarum ZZM01 isolated from mink.AMB Express · 2026Article
- A Novel Broad pH-Adaptive Bile Salt Hydrolase from Nomascus concolor Fecal Microbial Metagenome Facilitates the Cholesterol-Lowering Ability of Escherichia coli Nissle 1917.Probiotics and antimicrobial proteins · 2026Article
- Chemical Proteomics Reveals Regulation of Bile Salt Hydrolases via Oxidative Post-translational Modifications.Journal of the American Chemical Society · 2026Article
- Genome-wide association analysis reveals specialization to hosts and niches in multiple species of the Lactobacillaceae.The ISME journal · 2026Article
- Chemical proteomics reveals regulation of bile salt hydrolases via oxidative post-translational modifications.bioRxiv : the preprint server for biology · 2025Article
- Gut microbiota in regulatory T cell generation and function: mechanisms and health implications.Gut microbes · 2025Review
- Novel Probiotic Candidates in Artisanal Feta-Type Kefalonian Cheese: Unveiling a Still-Undisclosed Biodiversity.Probiotics and antimicrobial proteins · 2025Article
- Intermittent fasting and metabolic dysfunction-associated steatotic liver disease: the potential role of the gut-liver axis.Cell & bioscience · 2025Review
- Bile salt hydrolase: a key player in gut microbiota and its implications for metabolic dysfunction-associated steatotic liver disease.Microbiome research reports · 2025Review
- Interplay among IL1R1, gut microbiota, and bile acids in metabolic dysfunction-associated steatotic liver disease: a comprehensive review.Journal of gastroenterology and hepatology · 2025Review
- In Vitro Evaluation of Probiotic Activities and Anti-Obesity Effects ofFoods (Basel, Switzerland) · 2024Article
- Interplay between Bile Acids and Intestinal Microbiota: Regulatory Mechanisms and Therapeutic Potential for Infections.Pathogens (Basel, Switzerland) · 2024Review
- Article
- Bile salt hydrolases shape the bile acid landscape and restrict Clostridioides difficile growth in the murine gut.Nature microbiology · 2023Article
- Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation.NPJ biofilms and microbiomes · 2022Article
- Influence of high-fat diet on host animal health via bile acid metabolism and benefits of oral-fed Streptococcus thermophilus MN-ZLW-002.Experimental animals · 2022Article
- Ring Trial on Quantitative Assessment of Bile Acids Reveals a Method- and Analyte-Specific Accuracy and Reproducibility.Metabolites · 2022Article
- Identifying a Novel Bile Salt Hydrolase from the Keystone Gut BacteriumMicroorganisms · 2021Article
- Functional and Phylogenetic Diversity of BSH and PVA Enzymes.Microorganisms · 2021Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gut bacterial bile salt hydrolase (BSH) plays a critical role in host lipid metabolism and energy harvest. Therefore, BSH is a promising microbiome target to develop new therapies to regulate obesity in humans and novel non-antibiotic growth promoters for food animals. We previously reported the 1.90 Å apo crystal structure of BSH from Lactobacillus salivarius (lsBSH). In this study, we soaked the lsBSH crystal with glycocholic acid (GCA), a substrate, and obtained a 2.10 Å structure containing complex of lsBSH bound to GCA and cholic acid (CA), a product. The substrate/product sits in the water-exposed cavity molded by Loops 2 and 3. While the glycine moiety of GCA is exposed into a highly polar pocket, the sterane core of GCA is stabilized by aromatic and hydrophobic interactions. Comparison of product binding with BSH from Clostridium perfringenes reveals a distinct orientation of the sterane core in the binding site. The stability of the substrate-lsBSH complex and the putative catalytic mechanism were explored with molecular dynamics simulations. Site-directed mutagenesis of lsBSH demonstrated that Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Together, this study provides structural insights into BSH-substrate interaction, the mechanism of catalysis and substrate specificity, which facilitate rational design of BSH inhibitors.
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