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Literature summary extracted from

  • Patel, A.K.; Singhania, R.R.; Pandey, A.; Chincholkar, S.B.
    Probiotic bile salt hydrolase: current developments and perspectives (2010), Appl. Biochem. Biotechnol., 162, 166-180.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.24 DNA and amino acid sequence determination, analysis, and comparison of BSH from strain PF01, expression in Escherichia coli strain BL21(DE3) Lactobacillus acidophilus
3.5.1.24 genes bsh are cloned and expressed in Escherichia coli Bifidobacterium longum
3.5.1.24 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 Lactiplantibacillus plantarum

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.24 additional information BSH from strain ATCC 4005 is immobilized on 0.5% gellan gum gel for potential economic utilization Lentilactobacillus buchneri
3.5.1.24 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 Lactiplantibacillus plantarum
3.5.1.24 additional information knockout of gene bshA gene of strain NCFM decreases the ability to hydrolyze the chenodeoxycholic containing bile salts, e.g., taurochenodeoxycholic acid and glycochenodeoxycholic acid Lactobacillus acidophilus
3.5.1.24 additional information substitution of the N-terminal Cys with Ser or Thr results in an inactive enzyme, which emphasizes the importance of the presence of cysteine. The enzyme is immobilized by micro-encapsulation showing low acid resistance Bifidobacterium longum
3.5.1.24 additional information the enzyme is immobilized by micro-encapsulation. The microcapsules metabolize glyco- and tauroconjugated bile salts at rates of 0.0102 and 0.00185 mmol/g microcapsule per hour, respectively, and show better acid resistance. They exhibit an improved deconjugation with 49.4% of glycoconjugates per h in a simulated human gastrointestinal model and complete deconjugation after 4 h Limosilactobacillus reuteri

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.24 iodoacetate strong inhibition Lactiplantibacillus plantarum
3.5.1.24 additional information BSH is vigorously inhibited by thiol enzyme inhibitors Bifidobacterium longum
3.5.1.24 periodic acid strong inhibition Lactiplantibacillus plantarum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.24 0.00308
-
glycodeoxycholic acid pH not specified in the publication, temperature not specified in the publication Brevibacillus sp.
3.5.1.24 0.5
-
glycocholic acid pH 5.8-6.3, temperature not specified in the publication Lactiplantibacillus plantarum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.24 35042
-
4 * 35042 Bifidobacterium longum
3.5.1.24 37000
-
x * 37000, BSH from strain CK102 Lactiplantibacillus plantarum
3.5.1.24 56000
-
2 * 56000 Brevibacillus sp.
3.5.1.24 125000 150000
-
Bifidobacterium longum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.24 glycocholic acid + H2O Lactiplantibacillus plantarum strain CK102 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
?
3.5.1.24 glycodeoxycholic acid + H2O Brevibacillus sp.
-
3alpha,12alpha-dihydroxy-5beta-cholanate + glycine
-
?
3.5.1.24 additional information Bifidobacterium longum BSH can hydrolyze all the six major human bile salts and at least two animal bile salts. BSH from five strains show a better deconjugation rate on glycine-conjugated bile salts than on taurine-conjugated forms ?
-
?
3.5.1.24 additional information Lactobacillus acidophilus BSH catalyzes the hydrolysis of amide bond in conjugated bile salts and free amino acids are released, which form the deconjugated bile acid, mainly cholic and quenodeoxycholic ?
-
?
3.5.1.24 additional information Lentilactobacillus buchneri strain JCM1069 exhibits hydrolase activity against the taurodeoxycholic acid but not against the taurocholic acid, although both acids have taurine as their amino acid moiety but vary in their steroid moieties at 7alpha position ?
-
?
3.5.1.24 additional information Brevibacillus sp. the enzyme hydrolyzes all of the six major human bile salts ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.24 Bifidobacterium longum
-
strain ATCC 11863
-
3.5.1.24 Brevibacillus sp.
-
-
-
3.5.1.24 Clostridium perfringens
-
-
-
3.5.1.24 Lactiplantibacillus plantarum
-
strain WCFS1 with four bsh genes, and strains CK102 and 80
-
3.5.1.24 Lactobacillus acidophilus
-
strain NCFM with genes bshA and bshB, and strain PF01
-
3.5.1.24 Lactobacillus johnsonii
-
strain 100-100, two different antigenic conjugated BSHs, BSHalpha and BSHbeta
-
3.5.1.24 Lentilactobacillus buchneri
-
strains ATCC 4005 and JCM1069
-
3.5.1.24 Limosilactobacillus fermentum
-
-
-
3.5.1.24 Limosilactobacillus reuteri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.24 recombinant BSH from strain PF01 purifed from recombinant Escherichia coli strrain BL21(DE3) Lactobacillus acidophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.24 glycochenodeoxycholic acid + H2O
-
Lactobacillus acidophilus 3alpha,7alpha-dihydroxy-5beta-cholanate + glycine
-
?
3.5.1.24 glycocholic acid + H2O strain CK102 Lactiplantibacillus plantarum 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
?
3.5.1.24 glycodeoxycholic acid + H2O
-
Brevibacillus sp. 3alpha,12alpha-dihydroxy-5beta-cholanate + glycine
-
?
3.5.1.24 additional information BSH can hydrolyze all the six major human bile salts and at least two animal bile salts. BSH from five strains show a better deconjugation rate on glycine-conjugated bile salts than on taurine-conjugated forms Bifidobacterium longum ?
-
?
3.5.1.24 additional information BSH catalyzes the hydrolysis of amide bond in conjugated bile salts and free amino acids are released, which form the deconjugated bile acid, mainly cholic and quenodeoxycholic Lactobacillus acidophilus ?
-
?
3.5.1.24 additional information strain JCM1069 exhibits hydrolase activity against the taurodeoxycholic acid but not against the taurocholic acid, although both acids have taurine as their amino acid moiety but vary in their steroid moieties at 7alpha position Lentilactobacillus buchneri ?
-
?
3.5.1.24 additional information the enzyme hydrolyzes all of the six major human bile salts Brevibacillus sp. ?
-
?
3.5.1.24 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 Lactiplantibacillus plantarum ?
-
?
3.5.1.24 additional information 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. No activity with taurocholic acid Lentilactobacillus buchneri ?
-
?
3.5.1.24 additional information BSHs is highly substrate-specific, the two isozymes, encoded by two bsh genes, show different substrate specificities. BSHs can identify its substrate, bile acids, on amino acid groups, glycine/taurine, and also on cholate steroid nucleus. BSH recognizes the cholate group. The recombinant BSH from strain PF01 is active with tauroconjugated bile salts, but not with glycoconjugated bile slats Lactobacillus acidophilus ?
-
?
3.5.1.24 additional information the SH group in the N-terminal cysteine is responsible for BSH activity, and amino acids, viz. Asp20, Tyr82, Asn175, and Arg228, are believed to take part actively along with Cys in catalysis of bile salts Bifidobacterium longum ?
-
?
3.5.1.24 taurochenodeoxycholic acid + H2O
-
Lactobacillus acidophilus 3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
?
3.5.1.24 taurodeoxycholic acid + H2O
-
Lentilactobacillus buchneri 3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.24 ? x * 37000, BSH from strain CK102 Lactiplantibacillus plantarum
3.5.1.24 homodimer 2 * 56000 Brevibacillus sp.
3.5.1.24 tetramer 4 * 35042 Bifidobacterium longum
3.5.1.24 trimer BSHalpha and BSHbeta are combined to form native homo- and heterotrimers Lactobacillus johnsonii

Synonyms

EC Number Synonyms Comment Organism
3.5.1.24 bile salt hydrolase
-
Lactiplantibacillus plantarum
3.5.1.24 bile salt hydrolase
-
Limosilactobacillus fermentum
3.5.1.24 bile salt hydrolase
-
Lentilactobacillus buchneri
3.5.1.24 bile salt hydrolase
-
Clostridium perfringens
3.5.1.24 bile salt hydrolase
-
Lactobacillus acidophilus
3.5.1.24 bile salt hydrolase
-
Limosilactobacillus reuteri
3.5.1.24 bile salt hydrolase
-
Bifidobacterium longum
3.5.1.24 bile salt hydrolase
-
Lactobacillus johnsonii
3.5.1.24 bile salt hydrolase
-
Brevibacillus sp.
3.5.1.24 BSH
-
Lactiplantibacillus plantarum
3.5.1.24 BSH
-
Limosilactobacillus fermentum
3.5.1.24 BSH
-
Lentilactobacillus buchneri
3.5.1.24 BSH
-
Clostridium perfringens
3.5.1.24 BSH
-
Lactobacillus acidophilus
3.5.1.24 BSH
-
Limosilactobacillus reuteri
3.5.1.24 BSH
-
Bifidobacterium longum
3.5.1.24 BSH
-
Lactobacillus johnsonii
3.5.1.24 BSH
-
Brevibacillus sp.
3.5.1.24 cholylglycine hydrolase
-
Lactobacillus acidophilus
3.5.1.24 More BSH is a member of Ntn hydrolase family Clostridium perfringens
3.5.1.24 More the enzyme is a member of the N-terminal nucleophil hydrolase superfamily, possessing the characteristic alphabetabetaalpha tetra-lamellar tertiary structure arrangement in it Bifidobacterium longum
3.5.1.24 probiotic bile salt hydrolase
-
Lactiplantibacillus plantarum
3.5.1.24 probiotic bile salt hydrolase
-
Limosilactobacillus fermentum
3.5.1.24 probiotic bile salt hydrolase
-
Lentilactobacillus buchneri
3.5.1.24 probiotic bile salt hydrolase
-
Clostridium perfringens
3.5.1.24 probiotic bile salt hydrolase
-
Lactobacillus acidophilus
3.5.1.24 probiotic bile salt hydrolase
-
Limosilactobacillus reuteri
3.5.1.24 probiotic bile salt hydrolase
-
Bifidobacterium longum
3.5.1.24 probiotic bile salt hydrolase
-
Lactobacillus johnsonii
3.5.1.24 probiotic bile salt hydrolase
-
Brevibacillus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.24 632
-
glycodeoxycholic acid pH not specified in the publication, temperature not specified in the publication Brevibacillus sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.1.24 Bifidobacterium longum BSH type B
-
4.45
3.5.1.24 Bifidobacterium longum BSH types A and C
-
4.65

Expression

EC Number Organism Comment Expression
3.5.1.24 Lactiplantibacillus plantarum rapid induction of BSH expression by bile up
3.5.1.24 Lentilactobacillus buchneri rapid induction of BSH expression by bile up
3.5.1.24 Lactobacillus acidophilus rapid induction of BSH expression by bile up

General Information

EC Number General Information Comment Organism
3.5.1.24 evolution the BSH from Bifidobactrium longum demonstrates a evolutionary relationship with penicillin V acylase Bifidobacterium longum
3.5.1.24 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 Lactiplantibacillus plantarum
3.5.1.24 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 Limosilactobacillus fermentum
3.5.1.24 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 Lentilactobacillus buchneri
3.5.1.24 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 Clostridium perfringens
3.5.1.24 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 Lactobacillus acidophilus
3.5.1.24 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 Limosilactobacillus reuteri
3.5.1.24 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 Bifidobacterium longum
3.5.1.24 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 Lactobacillus johnsonii
3.5.1.24 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 Brevibacillus sp.