Any feedback?
Literature summary for 3.5.1.24 extracted from
- Effect of bile salt hydrolase inhibitors on a bile salt hydrolase from Lactobacillus acidophilus (2014), Pathogens, 3, 947-956.
Application
| Application | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence comparison, phylogenetic analysis and tree | Ligilactobacillus salivarius |
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| caffeic acid phenethyl ester | 71.8% inhibition of recombinant enzyme at 5 mM, 80% at 10 mM, 50% at 03125 mM | Lactobacillus acidophilus |  |
| caffeic acid phenethyl ester | - |
Ligilactobacillus salivarius | |
| CuCl2 | 97.2% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| CuCl2 | - |
Ligilactobacillus salivarius | |
| CuSO4 | 94.7% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| CuSO4 | - |
Ligilactobacillus salivarius | |
| demeclocycline | 99.6% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| demeclocycline | - |
Ligilactobacillus salivarius | |
| doxycycline | 98.3% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| doxycycline | - |
Ligilactobacillus salivarius | |
| epicatechin monogallate | 52.8% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| epicatechin monogallate | - |
Ligilactobacillus salivarius | |
| gossypetin | 96.1% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| gossypetin | - |
Ligilactobacillus salivarius | |
| KIO3 | 99.1% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| KIO3 | - |
Ligilactobacillus salivarius | |
| Lincomycin | 26.8% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| Lincomycin | - |
Ligilactobacillus salivarius | |
| menadione | 97.9% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| menadione | - |
Ligilactobacillus salivarius | |
| methacycline | 99.2% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| methacycline | - |
Ligilactobacillus salivarius | |
| 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 | |
| NaIO4 | 99.0% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| NaIO4 | - |
Ligilactobacillus salivarius | |
| oxytetracycline | 99.6% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| oxytetracycline | - |
Ligilactobacillus salivarius | |
| purpurogallin | 36.1% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| purpurogallin | - |
Ligilactobacillus salivarius | |
| riboflavin | 96.5% inhibition of recombinant enzyme at 0.5 mM, 50% at 0.016 mM | Lactobacillus acidophilus | |
| riboflavin c | - |
Ligilactobacillus salivarius | |
| roxarsone | 48.6% inhibition of recombinant enzyme at 2.5 mM | Lactobacillus acidophilus | |
| roxarsone | - |
Ligilactobacillus salivarius | |
| ZnCl2 | 38.4% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| ZnCl2 | - |
Ligilactobacillus salivarius | |
| ZnSO4 | 27.4% inhibition of recombinant enzyme at 5 mM | Lactobacillus acidophilus | |
| ZnSO4 | - |
Ligilactobacillus salivarius | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 32000 | - |
x * 32000, recombinant His-tagged enzyme, SDS-PAGE | Lactobacillus acidophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactobacillus acidophilus | A5HKP3 | isolated from swine | - |
| Lactobacillus acidophilus PF01 | A5HKP3 | isolated from swine | - |
| Ligilactobacillus salivarius | J7H3P9 | isolated from chicken | - |
| Ligilactobacillus salivarius NRRL B-30514 | J7H3P9 | isolated from chicken | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity | Lactobacillus acidophilus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| glycocholic acid + H2O | - |
Lactobacillus acidophilus | cholic acid + glycine | - |
? | |
| glycocholic acid + H2O | - |
Lactobacillus acidophilus PF01 | cholic acid + glycine | - |
? | |
| additional information | the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity | Ligilactobacillus salivarius | ? | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 32000, recombinant His-tagged enzyme, SDS-PAGE | Lactobacillus acidophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bile salt hydrolase | - |
Lactobacillus acidophilus |
| bile salt hydrolase | - |
Ligilactobacillus salivarius |
| BSH | - |
Lactobacillus acidophilus |
| BSH | - |
Ligilactobacillus salivarius |
| LaciP | - |
Lactobacillus acidophilus |
| LsalN1 | - |
Ligilactobacillus salivarius |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Lactobacillus acidophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Lactobacillus acidophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| additional information | structure modeling, overview | Lactobacillus acidophilus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
