3.5.1.24: choloylglycine hydrolase
This is an abbreviated version!
For detailed information about choloylglycine hydrolase, go to the full flat file.
Word Map on EC 3.5.1.24
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3.5.1.24
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lactobacillus
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cholesterol
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deconjugation
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plantarum
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microbiota
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cholesterol-lowering
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bifidobacterium
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taurodeoxycholic
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cholic
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taurocholic
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glycocholic
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drug development
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glycodeoxycholic
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farnesoid
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co-aggregation
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pentosaceus
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rhamnosus
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glycine-conjugated
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pentosus
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pediococcus
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acylase
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fermentum
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auto-aggregation
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taurine-conjugated
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rogosa
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medicine
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food industry
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taurochenodeoxycholic
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oxgall
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nutrition
- 3.5.1.24
- lactobacillus
- cholesterol
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deconjugation
- plantarum
- microbiota
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cholesterol-lowering
- bifidobacterium
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taurodeoxycholic
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cholic
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taurocholic
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glycocholic
- drug development
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glycodeoxycholic
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farnesoid
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co-aggregation
- pentosaceus
- rhamnosus
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glycine-conjugated
- pentosus
- pediococcus
- acylase
- fermentum
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auto-aggregation
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taurine-conjugated
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rogosa
- medicine
- food industry
- taurochenodeoxycholic
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oxgall
- nutrition
Reaction
Synonyms
BAH1, BFS26_06805, bile acid hydrolase, bile salt hydrolase, Bile-Salt-Hydrolase, BSH, BSH A, BSH B, BSH C, BSH1, BSH12, BSH2, BSH3, BSH4, BSH47, BSH56, BSHA, BSHB, BSHC, BT2086, C3745_01535, CBAH, CBH, CBSHalpha, CBSHbeta, CGH, cholylglycine hydrolase, Conjugated bile acid hydrolase, conjugated bile salt hydrolase, conjugated bile salt hydrolase alpha peptide, conjugated bile salt hydrolase beta, EFBG_01849, EfBSH, glycocholase, LaciP, LgBSH, linear amide C-N hydrolase, LJ1412, LJ_0056, LJ_1147, LsalN1, lsBSH, More, probiotic bile salt hydrolase, salt hydrolase
ECTree
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General Information
General Information on EC 3.5.1.24 - choloylglycine hydrolase
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evolution
malfunction
metabolism
physiological function
additional information
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the BSH from Bifidobactrium longum demonstrates a evolutionary relationship with penicillin V acylase
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
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
evolution
bile salt hydrolase (BSH) is a member of the N-terminal nucleophile hydrolase superfamily. Structure comparisons
evolution
bile salt hydrolase (BSH), a member of cholylglycine hydrolase family, catalyzes the de-conjugation of bile acids and is evolutionarily related to penicillin V acylase (PVA) that hydrolyses a different substrate such as penicillin V. Enterococcus faecalis bile salt hydrolase (BSH) has a manifold higher hydrolase activity compared to other known BSHs and displays unique allosteric catalytic property. The structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. An evolution-mediated subordination of the pre-peptide excision site results in loss of pre-peptide in EfBSH and other related cholylglycine hydrolases
evolution
enzyme BSH from Lactobacillus rhamnosus strain E9 belongs to the Ntn hydrolase super family, members of which are known to have conserved N-terminal cysteine residue (Cys1) in the active center. The enzyme is phylogenetically distant to the BSHs from other Lactobacillus spp. and genera but exhibits a close phylogenetic relationship with penicilling V acylase (PVA) from Bacillus sphaericus
evolution
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isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
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isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
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isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
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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
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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
evolution
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various Lactobacillus species deconjugate bile acids in the human gastrointestinal tract (GIT) through the action of bile salt hydrolase (BSH) enzymes, screening of the Lactobacillus BSH repertoire across 170 sequenced species, CD-HIT clustering of BSH proteins, sequence determinations, and phylogenetic analysis, overview. Mapping the occurrence of BSH and PVA proteins onto a Lactobacillus phylogenetic tree
evolution
Lactiplantibacillus plantarum NCIMB 8826
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Lactiplantibacillus plantarum ATCC BAA-793
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Bifidobacterium longum subsp. suis LMG 21814
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Bifidobacterium animalis KL612
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Ligilactobacillus salivarius CGMCC 8198
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Ligilactobacillus salivarius NRRL B-30514
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bile salt hydrolase (BSH) is a member of the N-terminal nucleophile hydrolase superfamily. Structure comparisons
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evolution
Ligilactobacillus salivarius NRRL B-30514
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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
-
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
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Ligilactobacillus salivarius JCM1046
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
Bifidobacterium bifidum ATCC 11863
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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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
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
Ligilactobacillus salivarius LGM14476
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
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isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
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evolution
Limosilactobacillus reuteri CRL 1098
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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the enzyme belongs to the bile salt hydrolases and the penicillin V acylase family, phylogenetic analysis
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
Enterococcus faecalis NCIM 2403
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
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evolution
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
Limosilactobacillus fermentum NCDO394
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sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
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enzyme BSH from Lactobacillus rhamnosus strain E9 belongs to the Ntn hydrolase super family, members of which are known to have conserved N-terminal cysteine residue (Cys1) in the active center. The enzyme is phylogenetically distant to the BSHs from other Lactobacillus spp. and genera but exhibits a close phylogenetic relationship with penicilling V acylase (PVA) from Bacillus sphaericus
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
-
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
malfunction
survival of BSH-positive Lactobacillus plantarum is significantly prolonged in the host gastointestinal tract compared to BSH-deleted Lactobacillus plantarum
malfunction
two serine residues next to nucleophile cysteine are essential for autocalytic processing to remove precursor peptide, but since a pre-peptide is absent in EfBSH the mutation of these serines is tolerated
malfunction
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using isogenic strains of wild-type and BSH-deleted Bacteroides thetaiotaomicron, the levels of the bile acid tauro-beta-muricholic acid in monocolonized gnotobiotic mice are selectively modulated. Bacteroides thetaiotaomicron BSH mutant-colonized mice display altered metabolism, including reduced weight gain and respiratory exchange ratios, as well as transcriptional changes in metabolic, circadian rhythm, and immune pathways in the gut and liver
malfunction
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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
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malfunction
Lactiplantibacillus plantarum ATCC BAA-793
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survival of BSH-positive Lactobacillus plantarum is significantly prolonged in the host gastointestinal tract compared to BSH-deleted Lactobacillus plantarum
-
malfunction
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using isogenic strains of wild-type and BSH-deleted Bacteroides thetaiotaomicron, the levels of the bile acid tauro-beta-muricholic acid in monocolonized gnotobiotic mice are selectively modulated. Bacteroides thetaiotaomicron BSH mutant-colonized mice display altered metabolism, including reduced weight gain and respiratory exchange ratios, as well as transcriptional changes in metabolic, circadian rhythm, and immune pathways in the gut and liver
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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
metabolism
KJ571489
Staphylococcus epidermidis strain RM1 possess both potent bile salt hydrolase (BSH) and N-acyl homoserine lactone (AHL, EC 3.1.1.81) cleavage activity, the single enzyme, that is not responsible for both the activities, is identified as bile salt hydrolase, two different genetic elements correspond to each of the enzymatic activity
metabolism
Lactiplantibacillus plantarum NCIMB 8826
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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
-
metabolism
Lactiplantibacillus plantarum ATCC BAA-793
-
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
-
metabolism
-
Staphylococcus epidermidis strain RM1 possess both potent bile salt hydrolase (BSH) and N-acyl homoserine lactone (AHL, EC 3.1.1.81) cleavage activity, the single enzyme, that is not responsible for both the activities, is identified as bile salt hydrolase, two different genetic elements correspond to each of the enzymatic activity
-
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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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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) 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
bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycineconjugated or taurine-conjugated bile acids. BSH enzyme catalyzes the deconjugation of glycine-conjugated or taurine-conjugated bile acids, which is an essential gateway reaction in the metabolism of bile acids in the small intestine
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 (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms
physiological function
bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms. Isozyme BSH47 exerts significant anti-giardial effects when tested in a murine model of giardiasis via Giardia duodenalis strain WB6
physiological function
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bile salt hydrolase (BSH)-like activities of Lactobacilli protect against pathogenic infection with Giardia duodenalis. Giardia duodenalis is a protozoan parasite responsible for giardiasis, a disease characterized by intestinal malabsorption, diarrhea and abdominal pain in a large number of mammal species. Giardiasis is one of the most common intestinal parasitic diseases in the world. Several strains are tested, overview. The two most active strains in vitro are Lactobacillus johnsonii strain La1 and Lactobacillus gasseri strain CNCM I-4884. Only Lactobacillus gasseri strain CNCM I-4884 is able to significantly antagonize parasite growth with a dramatic reduction of the Giardia duodenalis strain WB6 trophozoites load in the small intestine
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
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
physiological function
mechanism of action of the BSH of probiotics against hypercholesterolemia related diseases
physiological function
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microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans
physiological function
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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
physiological function
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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
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physiological function
Lactiplantibacillus plantarum NCIMB 8826
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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
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physiological function
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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
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physiological function
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bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms. Isozyme BSH47 exerts significant anti-giardial effects when tested in a murine model of giardiasis via Giardia duodenalis strain WB6
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physiological function
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bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms
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physiological function
Lactiplantibacillus plantarum ATCC BAA-793
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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
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physiological function
Lactiplantibacillus plantarum ATCC BAA-793
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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
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physiological function
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mechanism of action of the BSH of probiotics against hypercholesterolemia related diseases
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physiological function
Ligilactobacillus salivarius NRRL B-30514
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bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycineconjugated or taurine-conjugated bile acids. BSH enzyme catalyzes the deconjugation of glycine-conjugated or taurine-conjugated bile acids, which is an essential gateway reaction in the metabolism of bile acids in the small intestine
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physiological function
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microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans
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physiological function
Lactobacillus gasseri CNCM I-4884
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bile salt hydrolase (BSH)-like activities of Lactobacilli protect against pathogenic infection with Giardia duodenalis. Giardia duodenalis is a protozoan parasite responsible for giardiasis, a disease characterized by intestinal malabsorption, diarrhea and abdominal pain in a large number of mammal species. Giardiasis is one of the most common intestinal parasitic diseases in the world. Several strains are tested, overview. The two most active strains in vitro are Lactobacillus johnsonii strain La1 and Lactobacillus gasseri strain CNCM I-4884. Only Lactobacillus gasseri strain CNCM I-4884 is able to significantly antagonize parasite growth with a dramatic reduction of the Giardia duodenalis strain WB6 trophozoites load in the small intestine
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physiological function
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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
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effect of oral administration to Wistar rats of the immobilized bile salt hydrolase enzyme on serum cholesterol, triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia, overview
additional information
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probiotic organisms colonizing the host gastrointestinal tract need to be bile salt tolerant
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
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
additional information
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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
additional information
expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
additional information
expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
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
identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
additional information
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identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
additional information
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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
additional information
the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
additional information
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the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
additional information
the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
additional information
the structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. The substrate binding pocket shows reduced volume owing to altered loop conformations and increased hydrophobicity contributed by a higher ratio of hydrophobic to hydrophilic groups present. The aromatic residues F18, Y20 and F65 participate in substrate binding. Effective polar complementarity present for the three hydroxyl groups of glycocholic acid substrate in the binding site contributing to higher substrate specificity and efficient catalysis. These are unique features characteristics of this BSH enzyme and thought to contribute to its higher activity and specificity towards bile salts as well as allosteric effects. Substrate docking and molecular dynamics simulation studies, overview
additional information
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the structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. The substrate binding pocket shows reduced volume owing to altered loop conformations and increased hydrophobicity contributed by a higher ratio of hydrophobic to hydrophilic groups present. The aromatic residues F18, Y20 and F65 participate in substrate binding. Effective polar complementarity present for the three hydroxyl groups of glycocholic acid substrate in the binding site contributing to higher substrate specificity and efficient catalysis. These are unique features characteristics of this BSH enzyme and thought to contribute to its higher activity and specificity towards bile salts as well as allosteric effects. Substrate docking and molecular dynamics simulation studies, overview
additional information
Lactiplantibacillus plantarum NCIMB 8826
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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
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additional information
Lactiplantibacillus plantarum ATCC BAA-793
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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
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additional information
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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
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additional information
Ligilactobacillus salivarius LMG14476
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expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
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additional information
Ligilactobacillus salivarius NRRL B-30514
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the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
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additional information
Ligilactobacillus salivarius NRRL B-30514
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identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
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additional information
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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
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additional information
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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
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additional information
Enterococcus faecalis NCIM 2403
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the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
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additional information
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the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
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