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Information on EC 3.5.1.24 - choloylglycine hydrolase and Organism(s) Clostridium perfringens and UniProt Accession P54965
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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: Clostridium perfringens
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
CBAH
-
-
-
-
Conjugated bile acid hydrolase
-
-
-
-
glycocholase
-
-
-
-
bile salt hydrolase
-
-
-
-
BSH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycocholate + H2O = cholate + glycine
substrate binding pocket and active site structure, taurine has a reversed orientation pointing with its sulfo group towards Cys2 and leaving the active site with its amino group ahead, overview
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
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
activity assay
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
3,12-dioxo-5beta-cholanoylglycine + H2O
3,12-dioxo-5beta-cholanate + Gly
-
-
-
-
?
3,12-dioxo-5beta-cholanoyltaurine + H2O
3,12-dioxo-5beta-cholanate + taurine
-
-
-
-
?
3,7-dioxo-5beta-cholanoylglycine + H2O
3,7-dioxo-5beta-cholanate + Gly
-
-
-
-
?
3,7-dioxo-5beta-cholanoyltaurine + H2O
3,7-dioxo-5beta-cholanate + taurine
-
-
-
-
?
3-oxo-5beta-cholanoylglycine + H2O
3-oxo-5beta-cholanate + Gly
-
-
-
-
?
3-oxo-5beta-cholanoyltaurine + H2O
3-oxo-5beta-cholanate + taurine
-
-
-
-
?
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oylglycine + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyltaurine + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
3alpha,7alpha,12alpha-trihydroxy-5beta-homocholan-24-oylglycine + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-homocholanate + glycine
-
-
-
-
?
3alpha,7alpha,12alpha-trihydroxy-5beta-homocholan-24-oyltaurine + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-homocholanate + taurine
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholanoyl-alpha-aminomethanesulfonic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + aminomethanesulfonic acid
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholanoyl-beta-Ala + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + beta-Ala
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholanoyl-DL-Ala + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + DL-Ala
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholanoylsarcosine + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + sarcosine
-
low activity
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholestan-26-oylglycine + H2O
3alpha,7alpha-dihydroxy-5beta-cholestanate + Gly
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-cholestan-26-oyltaurine + H2O
3alpha,7alpha-dihydroxy-5beta-cholestanate + taurine
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-homocholanoylglycine + H2O
3alpha,7alpha-dihydroxy-5beta-homocholanate + Gly
-
-
-
-
?
3alpha,7alpha-dihydroxy-5beta-homocholanoyltaurine + H2O
3alpha,7alpha-dihydroxy-5beta-homocholanate + taurine
-
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoylglycine + H2O
3alpha,7beta-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
3alpha,7beta-dihydroxy-5beta-cholanoyltaurine + H2O
3alpha,7beta-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
3alpha-hydroxy-12-oxo-5beta-cholanoylglycine + H2O
3alpha-hydroxy-12-oxo-5beta-cholanate + Gly
-
-
-
-
?
3alpha-hydroxy-12-oxo-5beta-cholanoyltaurine + H2O
3alpha-hydroxy-12-oxo-5beta-cholanate + taurine
-
-
-
-
?
3alpha-hydroxy-7-oxo-5beta-cholanylglycine + H2O
3alpha-hydroxy-7-oxo-5beta-cholanate + Gly
-
-
-
-
?
3alpha-hydroxy-7-oxo-5beta-cholanyltaurine + H2O
3alpha-hydroxy-7-oxo-5beta-cholanate + taurine
-
-
-
-
?
3beta,7alpha-dihydroxy-5beta-cholanoylglycine + H2O
3beta,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
3beta,7alpha-dihydroxy-5beta-cholanoyltaurine + H2O
3beta,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
3beta,7beta-dihydroxy-5beta-cholanoylglycine + H2O
3beta,7beta-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
3beta,7beta-dihydroxy-5beta-cholanoyltaurine + H2O
3beta,7beta-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
cholyl-alpha-aminomethanesulfonic acid + H2O
cholic acid + aminomethanesulfonic acid
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
additional information
?
-
the enzyme shows a preference for tauro-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
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, 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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
the enzyme contains an N-terminal thiol hydrolase activity site, quarternary structure, crystal structure analysis, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with substrate taurodeoxycholate and as apoenzyme, complexed enzyme by hanging drop vapour diffusion method, 18°C, mixing of 0.003 ml protein solution and 0.002 ml reservoir solution, the latter containing 2.6 M ammonium sulfate, 0.1 M sodium citrate, pH 6.0, and 1 mM taurodeoxycholate, 3 days, apoenzyme crystals by sitting drop vapour diffusion method, 18°C, mixing of 0.0015 ml protein solution with 0.001 ml reservoir solution containing 25% PEG 4000, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, 3 days, orthorhombic crystals in both cases, X-ray diffraction structure determination and analysis at 1.7 and 2.1 A resolution, respectively
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is a target for BSH inhibitor development, overview
medicine
protein encapsulation is an excellent tool to protect enzymes during transit through gastric conditions and release enzyme activity in the proximal small intestine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nair, P.P.; Gordon, M.; Reback, J.
The enzymatic cleavage of the carbon-nitrogen bond in 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine
J. Biol. Chem.
242
7-11
1967
Clostridium perfringens
Batta, A.K.; Salen, G.; Shefer, S.
Substrate specificity of cholylglycine hydrolase for the hydrolysis of bile acid conjugates
J. Biol. Chem.
259
15035-15039
1984
Clostridium perfringens
Knarreborg, A.; Engberg, R.M.; Jensen, S.K.; Jensen, B.B.
Quantitative determination of bile salt hydrolase activity in bacteria isolated from the small intestine of chickens
Appl. Environ. Microbiol.
68
6425-6428
2002
Clostridium perfringens, Enterococcus faecalis, Enterococcus faecium, Ligilactobacillus salivarius, Ligilactobacillus aviarius, Streptococcus alactolyticus
Rossocha, M.; Schultz-Heienbrok, R.; von Moeller, H.; Coleman, J.P.; Saenger, W.
Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product
Biochemistry
44
5739-5748
2005
Clostridium perfringens (P54965), Clostridium perfringens
Lambert, J.M.; Weinbreck, F.; Kleerebezem, M.
In vitro analysis of protection of the enzyme bile salt hydrolase against enteric conditions by whey protein-gum arabic microencapsulation
J. Agric. Food Chem.
56
8360-8364
2008
Lactiplantibacillus plantarum WCFS1, Clostridium perfringens (P54965)
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
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)
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