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Literature summary extracted from

  • Lin, J.; Negga, R.; Zeng, X.; Smith, K.
    Effect of bile salt hydrolase inhibitors on a bile salt hydrolase from Lactobacillus acidophilus (2014), Pathogens, 3, 947-956.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.24 drug development the broad substrate specificity nature of Lactobacillus salivarius enzyme may make it an ideal candidate for screening desired BSH inhibitors targeting various BSH enzymes Ligilactobacillus salivarius
3.5.1.24 food industry inhibitors are a promising alternatives to antibiotic growth promoters for enhanced animal growth performance and food safety, required since antibiotic growth promoter usage is linked to the emergence of antibiotic resistant bacteria. Enzyme BSH inhibitors are promising feed additives to replace antibiotic growth promoters for enhanced host lipid metabolism and growth performance Lactobacillus acidophilus
3.5.1.24 food industry inhibitors are a promising alternatives to antibiotic growth promoters for enhanced animal growth performance and food safety, required since antibiotic growth promoter usage is linked to the emergence of antibiotic resistant bacteria. Enzyme BSH inhibitors are promising feed additives to replace antibiotic growth promoters for enhanced host lipid metabolism and growth performance Ligilactobacillus salivarius

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.24 DNA and amino acid sequence comparison, phylogenetic analysis and tree Ligilactobacillus salivarius
3.5.1.24 DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Lactobacillus acidophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.24 caffeic acid phenethyl ester 71.8% inhibition of recombinant enzyme at 5 mM, 80% at 10 mM, 50% at 03125 mM Lactobacillus acidophilus
3.5.1.24 caffeic acid phenethyl ester
-
 Ligilactobacillus salivarius
3.5.1.24 CuCl2 97.2% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 CuCl2
-
 Ligilactobacillus salivarius
3.5.1.24 CuSO4 94.7% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 CuSO4
-
 Ligilactobacillus salivarius
3.5.1.24 demeclocycline 99.6% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 demeclocycline
-
 Ligilactobacillus salivarius
3.5.1.24 doxycycline 98.3% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 doxycycline
-
 Ligilactobacillus salivarius
3.5.1.24 epicatechin monogallate 52.8% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 epicatechin monogallate
-
 Ligilactobacillus salivarius
3.5.1.24 gossypetin 96.1% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 gossypetin
-
 Ligilactobacillus salivarius
3.5.1.24 KIO3 99.1% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 KIO3
-
 Ligilactobacillus salivarius
3.5.1.24 Lincomycin 26.8% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 Lincomycin
-
 Ligilactobacillus salivarius
3.5.1.24 menadione 97.9% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 menadione
-
 Ligilactobacillus salivarius
3.5.1.24 methacycline 99.2% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 methacycline
-
 Ligilactobacillus salivarius
3.5.1.24 additional information the broad substrate specificity nature of Lactobacillus salivarius enzyme may make it an ideal candidate for screening desired BSH inhibitors targeting various BSH enzymes Ligilactobacillus salivarius
3.5.1.24 NaIO4 99.0% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 NaIO4
-
 Ligilactobacillus salivarius
3.5.1.24 oxytetracycline 99.6% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 oxytetracycline
-
 Ligilactobacillus salivarius
3.5.1.24 purpurogallin 36.1% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 purpurogallin
-
 Ligilactobacillus salivarius
3.5.1.24 riboflavin 96.5% inhibition of recombinant enzyme at 0.5 mM, 50% at 0.016 mM Lactobacillus acidophilus
3.5.1.24 riboflavin c
-
 Ligilactobacillus salivarius
3.5.1.24 roxarsone 48.6% inhibition of recombinant enzyme at 2.5 mM Lactobacillus acidophilus
3.5.1.24 roxarsone
-
 Ligilactobacillus salivarius
3.5.1.24 ZnCl2 38.4% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 ZnCl2
-
 Ligilactobacillus salivarius
3.5.1.24 ZnSO4 27.4% inhibition of recombinant enzyme at 5 mM Lactobacillus acidophilus
3.5.1.24 ZnSO4
-
 Ligilactobacillus salivarius

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.24 32000
-
 x * 32000, recombinant His-tagged enzyme, SDS-PAGE Lactobacillus acidophilus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.24 Lactobacillus acidophilus A5HKP3 isolated from swine
-
3.5.1.24 Lactobacillus acidophilus PF01 A5HKP3 isolated from swine
-
3.5.1.24 Ligilactobacillus salivarius J7H3P9 isolated from chicken
-
3.5.1.24 Ligilactobacillus salivarius NRRL B-30514 J7H3P9 isolated from chicken
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.24 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity Lactobacillus acidophilus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.24 glycocholic acid + H2O
-
 Lactobacillus acidophilus cholic acid + glycine
-
 ?
3.5.1.24 glycocholic acid + H2O
-
 Lactobacillus acidophilus PF01 cholic acid + glycine
-
 ?
3.5.1.24 additional information the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity Ligilactobacillus salivarius ?
-
 ?
3.5.1.24 additional information the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity Ligilactobacillus salivarius NRRL B-30514 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.24 ? x * 32000, recombinant His-tagged enzyme, SDS-PAGE Lactobacillus acidophilus

Synonyms

EC Number Synonyms Comment Organism
3.5.1.24 bile salt hydrolase
-
 Lactobacillus acidophilus
3.5.1.24 bile salt hydrolase
-
 Ligilactobacillus salivarius
3.5.1.24 BSH
-
 Lactobacillus acidophilus
3.5.1.24 BSH
-
 Ligilactobacillus salivarius
3.5.1.24 LaciP
-
 Lactobacillus acidophilus
3.5.1.24 LsalN1
-
 Ligilactobacillus salivarius

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.24 37
-
 assay at Lactobacillus acidophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.24 6
-
 assay at Lactobacillus acidophilus

General Information

EC Number General Information Comment Organism
3.5.1.24 evolution comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme Lactobacillus acidophilus
3.5.1.24 evolution comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme Ligilactobacillus salivarius
3.5.1.24 additional information structure modeling, overview Lactobacillus acidophilus