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Literature summary for 3.5.1.24 extracted from

  • Xu, F.; Guo, F.; Hu, X.J.; Lin, J.
    Crystal structure of bile salt hydrolase from Lactobacillus salivarius (2016), Acta Crystallogr. Sect. F, 72, 376-381 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
nutrition BSH is a key mechanistic microbiome target for the development of non-antibiotic food additives to improve animal feed production and for the design of measures to control obesity in humans Ligilactobacillus salivarius

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His-tagged BSH in Escherichia coli strain BL21(DE3) Ligilactobacillus salivarius

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, sitting drop vapour diffusion method, mixing 200 nl of 16.0 mg/ml protein in 10 mM sodium acetate, pH 5.5, 400 mM NaCl, 1 mM DTT, 1 mM EDTA, and 10% glycerol with 200 nl of reservoir solution containing 20% PEG 3350, and 0.2 M potassium dihydrogen phosphate, pH 4.8, and equilibration against 0.15 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using the structure of Clostridium perfringens BSH as a starting model. Two BSH molecules are packed perfectly as a dimer in one asymmetric unit Ligilactobacillus salivarius

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Ligilactobacillus salivarius
-
-

Organism

Organism UniProt Comment Textmining
Ligilactobacillus salivarius J7GY78
-
-
Ligilactobacillus salivarius NRRL B-30514 J7GY78
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged BSH from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange and hydrophobic interaction chromatography, and gel filtration Ligilactobacillus salivarius

Source Tissue

Source Tissue Comment Organism Textmining

Subunits

Subunits Comment Organism
dimer
-
Ligilactobacillus salivarius

Synonyms

Synonyms Comment Organism
bile salt hydrolase
-
Ligilactobacillus salivarius
BSH
-
Ligilactobacillus salivarius
lsBSH
-
Ligilactobacillus salivarius

General Information

General Information Comment Organism
evolution bile salt hydrolase (BSH) is a member of the N-terminal nucleophile hydrolase superfamily. Structure comparisons Ligilactobacillus salivarius
additional information identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH Ligilactobacillus salivarius
physiological function bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycineconjugated or taurine-conjugated bile acids. BSH enzyme catalyzes the deconjugation of glycine-conjugated or taurine-conjugated bile acids, which is an essential gateway reaction in the metabolism of bile acids in the small intestine Ligilactobacillus salivarius