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Literature summary extracted from

  • Rani, R.P.; Anandharaj, M.; Ravindran, A.D.
    Characterization of bile salt hydrolase from Lactobacillus gasseri FR4 and demonstration of its substrate specificity and inhibitory mechanism using molecular docking analysis (2017), Front. Microbiol., 8, 1004 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.24 acetone slight activation Lactobacillus gasseri
3.5.1.24 butanol
-
 Lactobacillus gasseri
3.5.1.24 DTT slight activation at 10 mM Lactobacillus gasseri
3.5.1.24 Isopropanol
-
 Lactobacillus gasseri
3.5.1.24 Triton X-100
-
 Lactobacillus gasseri
3.5.1.24 Tween 80
-
 Lactobacillus gasseri

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.24 gene bsh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Eschericchia coli strain DH5alpha Lactobacillus gasseri

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.24 ampicillin almost complete inhibition Lactobacillus gasseri
3.5.1.24 ascorbic acid moderate inhibition Lactobacillus gasseri
3.5.1.24 CaCl2 slight inhibition Lactobacillus gasseri
3.5.1.24 CuCl2 strong inhibition Lactobacillus gasseri
3.5.1.24 CuSO4 strong inhibition Lactobacillus gasseri
3.5.1.24 doxycycline hydrochloride almost complete inhibition Lactobacillus gasseri
3.5.1.24 erythromycin moderate inhibition Lactobacillus gasseri
3.5.1.24 ethanol slight inhibition Lactobacillus gasseri
3.5.1.24 KIO3 strong inhibition Lactobacillus gasseri
3.5.1.24 Lincomycin slight inhibition Lactobacillus gasseri
3.5.1.24 methanol slight inhibition Lactobacillus gasseri
3.5.1.24 MgCl2
-
 Lactobacillus gasseri
3.5.1.24 MgSO4
-
 Lactobacillus gasseri
3.5.1.24 MnCl2
-
 Lactobacillus gasseri
3.5.1.24 MnSO4
-
 Lactobacillus gasseri
3.5.1.24 additional information chloroform, 2-mercaptoethanol and EDTA show poor effects on the enzyme activity. Proteinase K almost completely abolishes the enzyme activity, strong inhibition by pepsin. The enzyme is not affected by alpha-amylase and catalase, and only slightly by lysozyme Lactobacillus gasseri
3.5.1.24 NaHIO3 strong inhibition Lactobacillus gasseri
3.5.1.24 neomycin strong inhibition Lactobacillus gasseri
3.5.1.24 oxytetracycline almost complete inhibition Lactobacillus gasseri
3.5.1.24 Penicillin V almost complete inhibition Lactobacillus gasseri
3.5.1.24 riboflavin almost complete inhibition Lactobacillus gasseri
3.5.1.24 SDS almost complete inhibition Lactobacillus gasseri
3.5.1.24 ZnCl2
-
 Lactobacillus gasseri
3.5.1.24 ZnSO4
-
 Lactobacillus gasseri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.24 glycocholate + H2O Lactobacillus gasseri
-
 cholate + glycine
-
 ?
3.5.1.24 glycocholate + H2O Lactobacillus gasseri FR4
-
 cholate + glycine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.24 Lactobacillus gasseri B9V405
-
-
3.5.1.24 Lactobacillus gasseri FR4 B9V405
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.24 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Lactobacillus gasseri

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 glycocholate + H2O
-
 Lactobacillus gasseri cholate + glycine
-
 ?
3.5.1.24 glycocholate + H2O
-
 Lactobacillus gasseri FR4 cholate + glycine
-
 ?
3.5.1.24 additional information purified recombinant LgBSH exhibits substrate specificity toward glyco-conjugated bile salts (GCA and GDCA) compared to tauro-conjugated bile salts. Substrate specificity of LgBSH, overview Lactobacillus gasseri ?
-
 ?
3.5.1.24 additional information purified recombinant LgBSH exhibits substrate specificity toward glyco-conjugated bile salts (GCA and GDCA) compared to tauro-conjugated bile salts. Substrate specificity of LgBSH, overview Lactobacillus gasseri FR4 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.24 ? x * 37000, recombinant enzyme, SDS-PAGE Lactobacillus gasseri

Synonyms

EC Number Synonyms Comment Organism
3.5.1.24 bile salt hydrolase
-
 Lactobacillus gasseri
3.5.1.24 BSH
-
 Lactobacillus gasseri
3.5.1.24 LgBSH
-
 Lactobacillus gasseri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.24 52
-
 recombinant enzyme Lactobacillus gasseri

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.24 20 70 activity range, profile overview Lactobacillus gasseri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.24 5.5
-
 recombinant enzyme Lactobacillus gasseri

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.24 3 8 activity range, profile overview Lactobacillus gasseri

General Information

EC Number General Information Comment Organism
3.5.1.24 additional information enzyme structure homology model of LgBSH using the structure of Enterococcus faecalis BSH (PDB ID 4WL3) as a template. Residues involved in catalysis are identified based on the superimposed structure, including Cys1, Arg16, Asp19, Asn79, Asn171, and Arg224. Molecular docking analysis of ligands Lactobacillus gasseri