ArticleBiotechnology letters2021
Characterization of substrate specificity and inhibitory mechanism of bile salt hydrolase from Lactobacillus reuteri CRL 1098 using molecular docking analysis.
Article in Biotechnology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Drug Advances in NAFLD: Individual and Combination Treatment Strategies of Natural Products and Small-Synthetic-Molecule Drugs.Biomolecules · 2025Review
- Molecular Insight into the Response of Lactic Acid Bacteria to Bile Acids.Biotech (Basel (Switzerland)) · 2024Article
- Insight into the High-Efficiency Benzo(a)pyrene Degradation Ability ofInternational journal of molecular sciences · 2023Article
- Article
- Farnesoid X Receptor, Bile Acid Metabolism, and Gut Microbiota.Metabolites · 2022Review
- Functional analysis of four bile salt hydrolase and penicillin acylase family members in Lactobacillus plantarum WCFS1.Applied and environmental microbiology · 2008Article
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Authors and funding
3 authors.
Funding
Abstract
objectivesTo elucidate the molecular mechanisms involved in the substrate interaction of the bile salt hydrolase of Lactobacillus reuteri CRL 1098 (LrBSH) with bile acids (BAs) and to evaluate potential enzyme inhibitors based on computer and in vitro modeling assays.
resultsAsp19, Asn79, and Asn171 participated in the LrBSH interaction with all BAs tested while Leu56 and Glu 222 played an important role in the interaction with glyco- and tauro-conjugated BAs, respectively. A great percentage of hydrophobic and polar interactions were responsible for the binding of LrBSH with glyco- and tauro-conjugated BAs, respectively. Remarkably, the four binding pocket loops participated in the substrate binding site of LrBSH unlike most of the reported BSHs. Inhibition assays showed that ascorbic acid, citric acid, penicillin G, and ciprofloxacin decreased LrBSH activity by 47.1%, 40.14%, 28.8%, and 9%, respectively. Docking analysis revealed that tetracycline and caffeic acid phenethyl ester had the low binding energy (-7.32 and -7.19 kcal/mol, respectively) and resembled the interaction pattern of GDCA (-6.88 kcal/mol) while penicillin (-6.25 kcal/mol) and ascorbic acid (-5.98 kcal/mol) interacted at a longer distance.
conclusionThis study helps to delve into the molecular mechanisms involved in the recognition of substrates and potential inhibitors of LrBSH.
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