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Information on EC 3.5.1.24 - choloylglycine hydrolase and Organism(s) Lactiplantibacillus plantarum and UniProt Accession Q06115
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3.5.1.24 choloylglycine hydrolaseIUBMB Comments
Also acts on the 3alpha,12alpha-dihydroxy-derivative, and on choloyl-taurine.
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Word Map
- 3.5.1.24
- lactobacillus
- cholesterol
-
deconjugation
- plantarum
- microbiota
-
cholesterol-lowering
- bifidobacterium
-
taurodeoxycholic
-
cholic
-
taurocholic
-
glycocholic
- drug development
-
glycodeoxycholic
-
farnesoid
-
co-aggregation
- pentosaceus
- rhamnosus
-
glycine-conjugated
- pentosus
- pediococcus
- acylase
- fermentum
-
auto-aggregation
-
taurine-conjugated
-
rogosa
- medicine
- food industry
- taurochenodeoxycholic
-
oxgall
- nutrition
The taxonomic range for the selected organisms is: Lactiplantibacillus plantarum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bile salt hydrolase, cholylglycine hydrolase, choloylglycine hydrolase, conjugated bile salt hydrolase, conjugated bile acid hydrolase, bsh a, efbsh, lgbsh, lsbsh, bile-salt-hydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bile salt hydrolase
BSH
BSH1
BSH2
BSH3
BSH4
CBAH
-
-
-
-
Conjugated bile acid hydrolase
-
-
-
-
glycocholase
-
-
-
-
bile salt hydrolase
-
-
-
-
bile salt hydrolase
-
-
BSH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine amidohydrolase
Also acts on the 3alpha,12alpha-dihydroxy-derivative, and on choloyl-taurine.
CAS REGISTRY NUMBER
COMMENTARY
37289-07-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cholate-7-amido-4-methylcoumarin-3-acetic acid + H2O
cholate + 7-amino-4-methylcoumarin-3-acetic acid
i.e. CA-AMCA, synthetic fluorogenic substrate of BSH
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
strain CK102
-
-
?
glycocholic acid + H2O
cholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
isoform BSH1 shows much higher hydrolysis on glycodeoxycholic acid than isoforms BSH2, BSH3 and BSH4
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
additional information
?
-
development and evalauation of a sensitive and simple assay method for continuous monitoring of BSH activity, a continuous fluorescence assay (AMCA fluorescence) that can be used for characterization of BSH activity with purified protein, cell lysates, whole cells, and in human gut microbiome samples, overview. Continuous, non-destructive quantification of BSH activity in a human fecal microbiome sample containing recombinant BSH is demonstrated
-
-
?
additional information
?
-
-
the enzyme shows a preference for glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
the enzyme shows a preference for glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
-
BSHs BSHs is highly substrate-specific and can identify its substrate, bile acids, on amino acid groups, glycine/taurine, and also on cholate steroid nucleus. BSH recognizes the cholate group
-
-
?
additional information
?
-
-
isoform BSH1 prefers deoxycholic salts over chenodeoxycholic and cholic acid salts
-
-
?
additional information
?
-
-
the recombinant enzyme is more efficient in hydrolyzing glycoconjugated bile salts than tauroconjugated bile salts
-
-
?
additional information
?
-
isozyme BSH1 shows very high overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview
-
-
?
additional information
?
-
isozyme BSH1 shows very high overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview
-
-
?
additional information
?
-
isozyme BSH1 shows very high overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview
-
-
?
additional information
?
-
KU961675
isozyme BSH1 shows very high overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview
-
-
?
additional information
?
-
isozyme BSH2 shows very low overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview. Activity with taurodeoxycholic acid and taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH2 shows very low overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview. Activity with taurodeoxycholic acid and taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH2 shows very low overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview. Activity with taurodeoxycholic acid and taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
KU961675
isozyme BSH2 shows very low overall activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2. Substrate specificity, overview. Activity with taurodeoxycholic acid and taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH3 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview. Activity with taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH3 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview. Activity with taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH3 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview. Activity with taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
KU961675
isozyme BSH3 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview. Activity with taurochenodeoxycholic acid is below detection limit
-
-
?
additional information
?
-
isozyme BSH4 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview
-
-
?
additional information
?
-
isozyme BSH4 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview
-
-
?
additional information
?
-
isozyme BSH4 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview
-
-
?
additional information
?
-
KU961675
isozyme BSH4 activity compared to the other BSH isozymes from Lactobacillus plantarum strain GD2, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows a preference for glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
the enzyme shows a preference for glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
additional information
?
-
-
isoform BSH1 prefers deoxycholic salts over chenodeoxycholic and cholic acid salts
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
strain CK102
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
isoform BSH1 shows much higher hydrolysis on glycodeoxycholic acid than isoforms BSH2, BSH3 and BSH4
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sodium periodate
-
about 99% inhibition at 0.1-2 mM, complete inhibition at 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
glycocholic acid
-
pH 5.8-6.3, temperature not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
bile salt hydrolase, a hydrolytic and intracellular enzyme, can fold fully in the cytoplasm
additional information
bile salt hydrolase from Lactobacillus plantarum BBE7 could not be efficiently exported by PelB signal peptide of the general secretory (Sec) pathway
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
malfunction
survival of BSH-positive Lactobacillus plantarum is significantly prolonged in the host gastointestinal tract compared to BSH-deleted Lactobacillus plantarum
metabolism
a key mechanism by which the microbiota in mammalian gut modify bile is through deconjugation of bile salts through bile salt hydrolase (BSH) enzymatic activity, which is postulated to be a prerequisite for all further microbial metabolism. BSH activity in the gut is largely considered to be beneficial for the host
physiological function
evolution
malfunction
-
mechanisms underlying the effects of Lactobacillus overexpression of bile salt hydrolase in hypercholesterolemia. The liver mRNA levels of farnesoid X receptor (FXR) and small heterodimer partner (SHP) are significantly downregulated in the AR113 and pWQH01 groups compared to the high-cholesterol diet (HCD) and enzyme-lacking LC2W groups, whereas the mRNA expression of hepatic cholesterol 7alpha-hydroxylase (CYP7A1), liver X receptor (LXR) and low density lipoprotein receptor (LDLR) is significantly upregulated in the AR113 (wild-type, high activity) and pWQH01 (recombinant overexpressing) groups compared to the HCD group
physiological function
additional information
physiological function
bile salt hydrolase (BSH) activity of the gut microbiota modulates the properties of bile salts, which are produced by the liver. BSH facilitates hydrolysis of the amide bond between the bile acid and glycine/taurine. The enzyme is a key regulator of bile acid homeostasis
physiological function
BSH is important for lactic acid bacteria survival and adhesion in the host gut. Bile salt hydrolase (BSH) catalyzes the conversion of conjugated bile salts (mainly tauro- or glycol-conjugated bile salts) into free bile salts, and can significantly modulate the mouse gut microbiome
evolution
-
microbial bile salt hydrolases (BSHs), a member of cholylglycine hydrolase (CGH) family. BSH is evolutionarily related to penicillin V acylase (PVA) which hydrolyses a penicillin V and is also a member of CGH family. five of the six amino acids, C2, R16, D19, N170, and R223, supposed to be responsible for catalytic activity of BSH enzyme, are strictly conserved in all CGH family members, N79 is partially conserved in the family
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
the enzyme belongs to the bile salt hydrolases and the penicillin V acylase family, phylogenetic analysis
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
bile salt hydrolase (BSH) is an enzyme that catalyses the deconjugation of bile salt. Lactobacillus plantarum RYPR1 is analyzed upon prebiotic utilization (with commercially available prebiotics lactulose, inulin, xylitol, raffinose, and oligofructose P95), catalytic interactions, and molecular docking with taurocholic and glycocholic acid. Residues Asn12, Ile8, and Leu6 interact with substrate taurocholic acid, and Lys88 and Asp126 interact with glycocholic acid. Molecular dynamics simulations, analysis of dynamic protein stability
physiological function
bile salt hydrolase catalyzes the hydrolysis of glycine- or taurine-conjugated bile acids into the free bile acids and a glycine/taurine moiety, which will increase the de novo synthesis of bile acids from cholesterol in the human host, thus lowering the host serum cholesterol level
physiological function
-
microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans
physiological function
-
the enzyme exerts a cholesterol-reducing effect in vivo in the host, male C57BL/6J mice. Also the recombinant strain Lactobacillus casei pWQH01 overexpressing the enzyme from Lactobacillus plantarum strain AR113 shows a cholesterol-reducing effect in vivo in the host, both with a phenotype of reduced body weight. Effects of probiotics on the expression of key genes involved in bile acid and cholesterol metabolism in hypercholesterolemic mice, detailed overview
additional information
enzymatic hydrolysis of bile salts by BSH generally relies on a N-terminal nucleophilic cysteine that attacks the amide bond of a bile salt to free the amino acid and form an intermediate covalent enzyme-bile acid complex, which is subsequently hydrolyzed, and leaves the cysteine free to participate in another catalytic cycle
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
KU961675
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
-
residue N79 might be important for substrate binding and catalytic turnover of BSH. Structure homology modelling using the crystal structure of BSH from Enterococcus faecalis (PDB ID 4wl3.1.B) as template. The homology modelling and 3D structure of BSH indicates that N79 residue is located near the catalytic center and within the cavity of substrates accessory to the enzyme
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000 - 150000
37000
140000 - 150000
-
recombinant His-tagged enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N79V
-
site-directed mutagenesis, the V79 mutation results in a stable enzyme, but reduces the catalytic activity and alters the substrate specificity of the enzyme
additional information
additional information
generation of gene bsh deletion mutant Lactobacillus plantarum strains
additional information
-
generation of gene bsh deletion mutant Lactobacillus plantarum strains
additional information
-
BSH is microencapsulated by foodgrade whey protein-gum arabic, comparison to living Lactobacillus plantarum WCFS1 in vitro, endogenously producing BSH, for its catalytic efficacy. BSH efficacy is better against pancreatin and low gastric pH initially, but its activity decreases further due to proteolytic degradation, whereas WCFS1 cells withstands such conditions. Bile salt deconjugation rates of microencapsulated BSH overproducing cells of strain 80 are 0.0049 mmol/g microcapsule per h towards glycoconjugates and 0.00079 mmol/g microcapsule per h towards tauroconjugates in the simulated gastro-intestine
additional information
three twin-arginine signal peptides from twin-arginine translocation (Tat) pathway are synthesized, fused with bsh gene, inserted into expression vectors pET-20b(+) and pET-22b(+), and transformed into four different Escherichia coli hosts, respectively. Periplasmic export across the cytoplasmic membrane of bile salt hydrolase expressed in recombinant Escherichia coli by the twin-arginine signal peptides is achieved. Among the 24 recombinant bacteria obtained, Escherichia coli strain BL21(DE3) pLysS (pET-20b(+)-dmsA-bsh) shows the highest BSH activity in periplasmic fraction, which is further increased to 1.21 U/ml by orthogonal experimental design, overview. The presence of BSH in the periplasm is proven to be caused by the export rather than cell leakage. Export across the cytoplasmic membrane is initiated by the interaction of the signal peptides with the Tat export machinery, which in Escherichia coli is made up of the membrane protein TatABC
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
purified recombinant His-tagged enzyme, 37°C, 24 h, inactivation
734498
3
-
purified recombinant His-tagged enzyme, 37°C, 24 h, inactivation
734498
5
-
purified recombinant His-tagged enzyme, 37°C, 24 h, 50% activity remaining
734498
7 - 8
-
purified recombinant His-tagged enzyme, 37°C, 24 h, stable at
734498
9
-
purified recombinant His-tagged enzyme, 37°C, 24 h, 50% activity remaining
734498
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
purified recombinant His-tagged enzyme, pH 6.0, 60 min, 90% activity remaining
50
-
purified recombinant His-tagged enzyme, pH 6.0, 60 min, 20-30% activity remaining
60
-
purified recombinant His-tagged enzyme, pH 6.0, inactivation within 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) by nickel affinity chromatography
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
recombinant soluble His-tagged enzyme 39.34fold from Escherichia coli strain BL21(DE3) pLysS by ammonium sulfate fractionation, nickel affinity chromatography, and gel filtration, to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bsh, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strains BLR(DE3) and XL-1 Blue
-
gene bsh1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR(DE3), subcloning in Escherichia coli strain XL-1 Blue
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
gene bsh1, recombinant overexpression in enzyme-deficient Lactobacillus casei LC2W, the transformed strain is termed Lactobacillus casei pWQH01, quantitative real-time PCR gene expression analysis
-
gene bsh2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR(DE3), subcloning in Escherichia coli strain XL-1 Blue
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
gene bsh3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR(DE3), subcloning in Escherichia coli strain XL-1 Blue
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
gene bsh4, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR(DE3), subcloning in Escherichia coli strain XL-1 Blue
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS and usage of the twin-arginine translocation (Tat) pathway as an alternative for this secretory production, enzyme secretion by the twin-arginine signal peptide of DMSO reductase subunit DmsA from Escherichia coli, method, overview. Most of the enzyme is expresed in intracellular inclusion bodies, but some is secreted to the cell culture medium
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vector-free engineering by chromosomal integration of an exogenous cbh gene, encoding the conjugated BSH, is cloned and expressed in Lactobacillus casei strain LK1 with the aid of pSMA23-derived vectors
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is a target for BSH inhibitor development, overview
drug development
the enzyme is a target for BSH inhibitor development, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, H.; Doesburg, K.; Iwasaki, T.; Mierau, I.
Screening of lactic acid bacteria for bile salt hydrolase actictivity
J. Dairy Sci.
82
2530-2535
1999
Amylolactobacillus amylophilus, Bifidobacterium adolescentis, Bifidobacterium animalis, Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium longum, Bifidobacterium longum subsp. infantis, Bifidobacterium pseudolongum, Bifidobacterium thermophilum, Companilactobacillus farciminis, Fructilactobacillus sanfranciscensis, Lacticaseibacillus casei, Lacticaseibacillus paracasei, Lacticaseibacillus rhamnosus, Lactiplantibacillus plantarum, Lactobacillus acidophilus, Lactobacillus crispatus, Lactobacillus gasseri, Lactobacillus helveticus, Lactobacillus johnsonii, Lactobacillus kefiranofaciens, Lentilactobacillus buchneri, Lentilactobacillus hilgardii, Ligilactobacillus salivarius, Limosilactobacillus fermentum, no activity in Bifidobacterium coryneforme, no activity in Lactococcus lactis, no activity in Leuconostoc mesenteroides, no activity in Streptococcus thermophilus
Lambert, J.M.; Siezen, R.J.; de Vos, W.M.; Kleerebezem, M.
Improved annotation of conjugated bile acid hydrolase superfamily members in Gram-positive bacteria
Microbiology
154
2492-2500
2008
Bifidobacterium bifidum (Q6R974), Bifidobacterium longum (Q9KK62), Clostridium perfringens (P54965), Enterococcus faecium (Q83YZ2), Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum WCFS1 (Q06115), Lactobacillus johnsonii (Q9F660 and P97038), Listeria monocytogenes (Q8Y5J3)
Patel, A.K.; Singhania, R.R.; Pandey, A.; Chincholkar, S.B.
Probiotic bile salt hydrolase: current developments and perspectives
Appl. Biochem. Biotechnol.
162
166-180
2010
Bifidobacterium longum, Brevibacillus sp., Clostridium perfringens, Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lentilactobacillus buchneri, Limosilactobacillus fermentum, Lactobacillus johnsonii, Limosilactobacillus reuteri
Ren, J.; Sun, K.; Wu, Z.; Yao, J.; Guo, B.
All 4 bile salt hydrolase proteins are responsible for the hydrolysis activity in Lactobacillus plantarum ST-III
J. Food Sci.
76
M622-M628
2012
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ST-III
Dong, Z.; Zhang, J.; Lee, B.; Li, H.; Du, G.; Chen, J.
Secretory expression and characterization of a bile salt hydrolase from Lactobacillus plantarum in Escherichia coli
J. Mol. Catal. B
93
57-64
2013
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum BBE7
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Dong, Z.; Zhang, J.; Du, G.; Chen, J.; Li, H.; Lee, B.
Periplasmic export of bile salt hydrolase in Escherichia coli by the twin-arginine signal peptides
Appl. Biochem. Biotechnol.
177
458-471
2015
Lactiplantibacillus plantarum (B9V401), Lactiplantibacillus plantarum BBE7 (B9V401)
Yang, Y.; Liu, Y.; Zhou, S.; Huang, L.; Chen, Y.; Huan, H.
Bile salt hydrolase can improve Lactobacillus plantarum survival in gastrointestinal tract by enhancing their adhesion ability
FEMS Microbiol. Lett.
366
fnz100
2019
Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC BAA-793 (Q06115)
Oeztuerk, M.; Aydin, Y.; Kilicsaymaz, Z.; Oenal, C.; Ba, N.
Molecular cloning, characterization, and comparison of four bile salt hydrolase-related enzymes from Lactobacillus plantarum GD2 of human origin
Food Biotechnol.
32
191-205
2018
Lactiplantibacillus plantarum (A0A193H6Q2), Lactiplantibacillus plantarum (A0A1B1FMJ8), Lactiplantibacillus plantarum (A0A1I9RYI4), Lactiplantibacillus plantarum (KU961675), Lactiplantibacillus plantarum GD2 (A0A193H6Q2), Lactiplantibacillus plantarum GD2 (A0A1B1FMJ8), Lactiplantibacillus plantarum GD2 (A0A1I9RYI4), Lactiplantibacillus plantarum GD2 (KU961675)
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Wang, G.; Huang, W.; Xia, Y.; Xiong, Z.; Ai, L.
Cholesterol-lowering potentials of Lactobacillus strain overexpression of bile salt hydrolase on high cholesterol diet-induced hypercholesterolemic mice
Food Funct.
10
1684-1695
2019
Lactiplantibacillus plantarum, no activity in Lactobacillus casei strain LC2W, Lactiplantibacillus plantarum AR113
Yadav, R.; Singh, P.K.; Puniya, A.K.; Shukla, P.
Catalytic Interactions and molecular docking of bile salt hydrolase (BSH) from L. plantarum RYPR1 and its prebiotic utilization
Front. Microbiol.
7
2116
2016
Lactiplantibacillus plantarum (B9V401), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum RYPR1 (B9V401)
Oeztuerk, M.; Oenal, C.
Asparagine 79 is an important amino acid for catalytic activity and substrate specificity of bile salt hydrolase (BSH)
Mol. Biol. Rep.
46
4361-4368
2019
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum B14
Dong, Z.; Lee, B.H.
Bile salt hydrolases structure and function, substrate preference, and inhibitor development
Protein Sci.
27
1742-1754
2018
Bifidobacterium animalis (G0YYC2), Bifidobacterium animalis (Q53CP8), Bifidobacterium animalis Bi30 (G0YYC2), Bifidobacterium animalis KL612 (Q53CP8), Bifidobacterium bifidum (Q6R974), Bifidobacterium bifidum ATCC 11863 (Q6R974), Bifidobacterium longum subsp. Longum (Q9KK62), Bifidobacterium longum subsp. Longum SBT2928 (Q9KK62), Bifidobacterium longum subsp. suis (A0A087BL81), Bifidobacterium longum subsp. suis LMG 21814 (A0A087BL81), Bifidobacterium pseudocatenulatum (C0BTD8), Bifidobacterium pseudocatenulatum DSM 20438 (C0BTD8), Clostridium perfringens (P54965), Clostridium perfringens 13 (P54965), Clostridium perfringens type A (P54965), Enterococcus faecalis, Enterococcus faecalis NCIM 2403, Lacticaseibacillus rhamnosus (G4XR38), Lacticaseibacillus rhamnosus E9 (G4XR38), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum ATCC BAA-793 (Q06115), Lactiplantibacillus plantarum BBE7, Lactiplantibacillus plantarum NCIMB 8826 (Q06115), Lactobacillus acidophilus (Q5FK51), Lactobacillus acidophilus (Q5FKM3), Lactobacillus acidophilus ATCC 700396 (Q5FK51), Lactobacillus acidophilus ATCC 700396 (Q5FKM3), Lactobacillus acidophilus N2 (Q5FK51), Lactobacillus acidophilus N2 (Q5FKM3), Lactobacillus acidophilus NCFM (Q5FK51), Lactobacillus acidophilus NCFM (Q5FKM3), Lactobacillus acidophilus NCK56 (Q5FK51), Lactobacillus acidophilus NCK56 (Q5FKM3), Lactobacillus gasseri (A0A1Y0E209), Lactobacillus gasseri (B9V405), Lactobacillus gasseri Am1 (B9V405), Lactobacillus gasseri FR4 (A0A1Y0E209), Lactobacillus johnsonii, Lactobacillus johnsonii (A0A1B3PS02), Lactobacillus johnsonii (A0A4Z0GFP0), Lactobacillus johnsonii (P97038), Lactobacillus johnsonii (Q9F660), Lactobacillus johnsonii 100-100 (P97038), Lactobacillus johnsonii 100-100 (Q9F660), Lactobacillus johnsonii PF01, Lactobacillus johnsonii PF01 (A0A1B3PS02), Lactobacillus johnsonii PF01 (A0A4Z0GFP0), Ligilactobacillus salivarius, Ligilactobacillus salivarius (C7AQX8), Ligilactobacillus salivarius (C7AQX9), Ligilactobacillus salivarius (C7AQY2), Ligilactobacillus salivarius (J7H3P9), Ligilactobacillus salivarius (M1R367), Ligilactobacillus salivarius (M1R991), Ligilactobacillus salivarius (Q1WR93), Ligilactobacillus salivarius B-30514 (J7H3P9), Ligilactobacillus salivarius CGMCC 8198, Ligilactobacillus salivarius CGMCC 8198 (M1R367), Ligilactobacillus salivarius CGMCC 8198 (M1R991), Ligilactobacillus salivarius JCM1046 (C7AQX8), Ligilactobacillus salivarius LGM14476 (C7AQX9), Ligilactobacillus salivarius LGM14476 (C7AQY2), Ligilactobacillus salivarius UCC118 (Q1WR93), Limosilactobacillus fermentum (H6WSA2), Limosilactobacillus fermentum NCDO394 (H6WSA2), Limosilactobacillus reuteri (B5TQZ0), Limosilactobacillus reuteri CRL 1098 (B5TQZ0)
Brandvold, K.R.; Weaver, J.M.; Whidbey, C.; Wright, A.T.
A continuous fluorescence assay for simple quantification of bile salt hydrolase activity in the gut microbiome
Sci. Rep.
9
1359
2019
Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum NCIMB 8826 (Q06115), Lactiplantibacillus plantarum ATCC BAA-793 (Q06115)
EXTERNAL LINKS (specific for EC-Number 3.5.1.24)
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