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
-
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
- 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
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
3.5.1.24 choloylglycine hydrolaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.5.1.24 - choloylglycine hydrolase
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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
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
-
-
-
-
?
cholate-7-amido-4-methylcoumarin-3-acetic acid + H2O
cholate + 7-amino-4-methylcoumarin-3-acetic acid
cholyl-alpha-aminomethanesulfonic acid + H2O
cholic acid + aminomethanesulfonic acid
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholate + H2O
3alpha,12alpha-dihydroxy-5-beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycolithocholic acid + H2O
lithocholate + glycine
-
preferred substrate
-
-
?
glycoursodeoxycholic acid + H2O
ursodeoxycholate + glycine
-
moderate activity
-
-
?
tauro-beta-muricholic acid + H2O
beta-muricholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
taurine + deoxycholate
-
-
-
-
?
taurolithocholic acid + H2O
lithocholate + taurine
-
preferred substrate
-
-
?
tauroursodeoxycholic acid + H2O
ursodeoxycholate + taurine
-
moderate activity
-
-
?
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
-
-
?
cholate-7-amido-4-methylcoumarin-3-acetic acid + H2O
cholate + 7-amino-4-methylcoumarin-3-acetic acid
Lactiplantibacillus plantarum ATCC BAA-793
i.e. CA-AMCA, synthetic fluorogenic substrate of BSH
-
-
?
cholate-7-amido-4-methylcoumarin-3-acetic acid + H2O
cholate + 7-amino-4-methylcoumarin-3-acetic acid
Lactiplantibacillus plantarum NCIMB 8826
i.e. CA-AMCA, synthetic fluorogenic substrate of BSH
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
-
-
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
-
-
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
-
-
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
-
-
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
low activity
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
low activity
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
about 75% activity compared to glycocholic acid
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
about 75% activity compared to glycocholic acid
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Bifidobacterium bifidum ATCC 11863
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Bifidobacterium longum subsp. suis LMG 21814
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Enterococcus faecalis NCIM 2403
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Enterococcus faecalis NCIM 2403
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Lactiplantibacillus plantarum ATCC BAA-793
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Lactiplantibacillus plantarum NCIMB 8826
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
moderate activity
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
moderate activity
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius CGMCC 8198
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius JCM1046
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius LGM14476
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius LMG14476
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Ligilactobacillus salivarius NRRL B-30514
best substrate
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Limosilactobacillus fermentum NCDO394
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
Limosilactobacillus reuteri CRL 1098
-
-
-
?
glycocholate + H2O
cholate + glycine
preferred substrate
-
-
?
glycocholate + H2O
cholate + glycine
Limosilactobacillus fermentum NCDO394
preferred substrate
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
activity assay
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
-
activity assay
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
100% activity
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
100% activity
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
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
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
best substrate
-
-
?
glycocholic acid + H2O
cholate + glycine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
best substrate
-
-
?
glycocholic acid + H2O
cholate + glycine
high activity
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
low activity
-
-
?
glycocholic acid + H2O
cholate + glycine
low activity
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
high activity
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
high activity
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
about 80% activity compared to glycocholic acid
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Bifidobacterium longum subsp. suis LMG 21814
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
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
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Lactiplantibacillus plantarum ATCC BAA-793
-
-
-
?
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
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
low activity
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
low activity
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Limosilactobacillus reuteri CRL 1098
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Limosilactobacillus reuteri CRL 1100
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
Limosilactobacillus reuteri CRL 1101
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
glycohyodeoxycholate + H2O
glycine + hyodeoxycholate
-
-
-
-
?
glycoursodeoxycholate + H2O
glycine + ursodeoxycholate
-
-
-
-
?
glycoursodeoxycholate + H2O
glycine + ursodeoxycholate
-
-
-
-
?
tauro-beta-muricholic acid + H2O
taurine + beta-muricholic acid
-
i.e. TbetaMCA, synthetic fluorogenic substrate of BSH
-
-
?
tauro-beta-muricholic acid + H2O
taurine + beta-muricholic acid
-
i.e. TbetaMCA, synthetic fluorogenic substrate of BSH
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
taurine + chenodeoxycholate
-
-
-
-
?
taurochenodeoxycholate + H2O
taurine + chenodeoxycholate
-
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
about 15% activity compared to glycocholic acid
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
about 15% activity compared to glycocholic acid
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Bifidobacterium bifidum ATCC 11863
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Bifidobacterium longum subsp. suis LMG 21814
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Enterococcus faecalis NCIM 2403
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Enterococcus faecalis NCIM 2403
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Lactiplantibacillus plantarum ATCC BAA-793
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Lactiplantibacillus plantarum NCIMB 8826
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius CGMCC 8198
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius JCM1046
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius LGM14476
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius LMG14476
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Limosilactobacillus fermentum NCDO394
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
Limosilactobacillus reuteri CRL 1098
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
about 20% activity compared to glycocholic acid
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
about 20% activity compared to glycocholic acid
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
hydrolyzing activity against tauroconjugated bile salts, but not glycoconjugated bile salts
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
preferred substrate
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
high activity
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
less than 20% activity compared to glycocholic acid
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
Bifidobacterium longum subsp. suis LMG 21814
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
Lactiplantibacillus plantarum ATCC BAA-793
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
A0A193H6Q2, A0A1B1FMJ8, A0A1I9RYI4, KU961675
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
very low activity
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
Ligilactobacillus salivarius NRRL B-30514
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
KJ571489
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
KJ571489
-
-
-
?
additional information
?
-
-
comparisons of substrate specificity and selective BSH activity in the human gut bacterial phylum Bacteroidetes, overview
-
-
?
additional information
?
-
-
selectivity for deconjugating C12 = H but not C12 = OH core primary bile acids. No activity with glycocholic acid and taurocholic acid, taurochenodeoxycholic acid is a poor substrate
-
-
?
additional information
?
-
-
comparisons of substrate specificity and selective BSH activity in the human gut bacterial phylum Bacteroidetes, overview
-
-
?
additional information
?
-
-
selectivity for deconjugating C12 = H but not C12 = OH core primary bile acids. No activity with glycocholic acid and taurocholic acid, taurochenodeoxycholic acid is a poor substrate
-
-
?
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
?
-
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
?
-
Bifidobacterium animalis KL612
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 exhibits clear preference for glycine-conjugated bile salts over taurine-conjugated forms
-
-
?
additional information
?
-
the enzyme exhibits clear preference for glycine-conjugated bile salts over taurine-conjugated forms
-
-
?
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
?
-
Bifidobacterium bifidum ATCC 11863
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 catalyzes the deconjugation of glycine- or taurine-linked bile salts
-
-
?
additional information
?
-
-
substrate specificity profile, overview
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
Bifidobacterium longum subsp. suis LMG 21814
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
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
the enzyme shows a preference for both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
the enzyme shows a preference for both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
substrate specificity of the purified enzyme, overview
-
-
?
additional information
?
-
-
catalyzes the hydrolysis of glycine- and taurine-conjugated bile salts to amino acid residues and free bile salts
-
-
?
additional information
?
-
-
the enzyme hydrolyzes all of the six major human bile salts
-
-
?
additional information
?
-
the enzyme contributes to the establishment of a successful infection through the oral route in mice, CGH confers the ability to the organism to resist the antimicrobial action of bile salts
-
-
?
additional information
?
-
-
the enzyme contributes to the establishment of a successful infection through the oral route in mice, CGH confers the ability to the organism to resist the antimicrobial action of bile salts
-
-
?
additional information
?
-
the enzyme contributes to the establishment of a successful infection through the oral route in mice, CGH confers the ability to the organism to resist the antimicrobial action of bile salts
-
-
?
additional information
?
-
-
the enzyme contributes to the establishment of a successful infection through the oral route in mice, CGH confers the ability to the organism to resist the antimicrobial action of bile salts
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the enzyme preforms autocatalytic processing, mechanism, overview. The wild-type enzyme also exhibits penicillin V acylase activity
-
-
?
additional information
?
-
-
the enzyme preforms autocatalytic processing, mechanism, overview. The wild-type enzyme also exhibits penicillin V acylase activity
-
-
?
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
-
-
?
additional information
?
-
Enterococcus faecalis NCIM 2403
-
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
-
-
?
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 recombinant BSH enzyme exhibits the highest affinity for glychochenodeoxycholic acid and higher affinities for glycine-conjugated bile acids than for taurine-conjugated bile acids, overview
-
-
?
additional information
?
-
the recombinant BSH enzyme exhibits the highest affinity for glychochenodeoxycholic acid and higher affinities for glycine-conjugated bile acids than for taurine-conjugated bile acids, 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
?
-
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
?
-
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
-
-
?
additional information
?
-
Lactiplantibacillus plantarum ATCC BAA-793
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
?
-
Lactiplantibacillus plantarum ATCC BAA-793
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 recombinant enzyme is more efficient in hydrolyzing glycoconjugated bile salts than tauroconjugated bile salts
-
-
?
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
?
-
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 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 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
?
-
Lactiplantibacillus plantarum NCIMB 8826
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
?
-
Lactiplantibacillus plantarum NCIMB 8826
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
?
-
-
isoform BSH1 prefers deoxycholic salts over chenodeoxycholic and cholic acid salts
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the enzyme shows a preference for both tauro- and 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 both tauro- and 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
?
-
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 both tauro- and 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 both tauro- and 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
?
-
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 both tauro- and 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 both tauro- and 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
?
-
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 both tauro- and 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 both tauro- and 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
?
-
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 both tauro- and 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 both tauro- and 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
?
-
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
?
-
purified recombinant LgBSH exhibits substrate specificity toward glyco-conjugated bile salts (GCA and GDCA) compared to tauro-conjugated bile salts. Substrate specificity of LgBSH, overview
-
-
?
additional information
?
-
-
purified recombinant LgBSH exhibits substrate specificity toward glyco-conjugated bile salts (GCA and GDCA) compared to tauro-conjugated bile salts. Substrate specificity of LgBSH, overview
-
-
?
additional information
?
-
substrate specificity of BSH from Lactobacillus gasseri strain ATCC 33323, the enzyme shows a preference for the glycine-conjugated bile salts. No activity with taurochenodeoxycholic acid
-
-
?
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
?
-
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
?
-
substrate specificity of BSH from Lactobacillus gasseri strain ATCC 33323, the enzyme shows a preference for the glycine-conjugated bile salts. No activity with taurochenodeoxycholic acid
-
-
?
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
?
-
purified recombinant LgBSH exhibits substrate specificity toward glyco-conjugated bile salts (GCA and GDCA) compared to tauro-conjugated bile salts. Substrate specificity of LgBSH, overview
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
-
the enzyme shows a preference for both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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
?
-
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
?
-
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
?
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
the enzyme shows a preference for both tauro- and 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 both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
no significant enzymatic activity is detected for BSH12 with glycocholic acid, taurocholic acid, glycodeoxycholic acid, and taurodeoxycholic acid
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
recombinant BSH47 efficiently hydrolyzes tauro-conjugated bile salts, whereas no BSH activity is detected for glyco-conjugated bile salts in transformed Escherichia coli strain SE1
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, overview
-
-
?
additional information
?
-
-
isoyzme BSH A hydrolyses tauro-conjugated bile salts, whereas isozyme BSH C hydrolyses glycoconjugated bile salts. The enzymes have no preferential activities towards a specific cholyl moiety, the isozymes differ in their substrate specificities, 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
-
-
?
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
?
-
-
oxgall is a substrate for the enzyme from different strains, overview
-
-
?
additional information
?
-
Lactobacillus spp.
-
enzyme activity is important for Lactobacillus colonization of human intestine
-
?
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
-
-
?
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
-
-
?
additional information
?
-
broad substrate specificity
-
-
?
additional information
?
-
the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity
-
-
?
additional information
?
-
-
the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity
-
-
?
additional information
?
-
-
the enzyme shows a preference for both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both glyco- and tauro-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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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 both tauro- and 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
?
-
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
?
-
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
?
-
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
?
-
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 tauro-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 tauro-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 tauro-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 tauro-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 tauro-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 tauro-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 tauro-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 tauro-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
?
-
Ligilactobacillus salivarius CGMCC 8198
-
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
?
-
Ligilactobacillus salivarius CGMCC 8198
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
?
-
Ligilactobacillus salivarius CGMCC 8198
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
?
-
Ligilactobacillus salivarius CGMCC 8198
-
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius CGMCC 8198
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius CGMCC 8198
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius CGMCC 8198
-
the enzyme shows a preference for both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
Ligilactobacillus salivarius CGMCC 8198
the enzyme shows a preference for both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
Ligilactobacillus salivarius CGMCC 8198
the enzyme shows a preference for both tauro- and glyco-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
Ligilactobacillus salivarius JCM1046
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius LGM14476
the enzyme shows a preference for both glyco- and tauro-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
Ligilactobacillus salivarius LGM14476
the enzyme shows a preference for both glyco- and tauro-conjugated bile acids. Structural basis for the substrate preference of BSHs, and potential mechanism of substrate recognition, overview
-
-
?
additional information
?
-
Ligilactobacillus salivarius LGM14476
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius LGM14476
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
-
-
?
additional information
?
-
Ligilactobacillus salivarius NRRL B-30514
broad substrate specificity
-
-
?
additional information
?
-
Ligilactobacillus salivarius NRRL B-30514
the Lactobacillus salivarius enzyme displays potent hydrolysis activity towards both glycoconjugated and tauroconjugated bile salts with broad substrate specificity
-
-
?
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 recombinant enzyme hydrolyzes six major human bile salts with a slight preference towards glycine-conjugated bile salts, the enzyme shows a broad range of substrate specificity, overview. The enzyme also slightly prefers to hydrolyze conjugated cholates over conjugated deoxycholates and chenodeoxycholates
-
-
?
additional information
?
-
-
the recombinant enzyme hydrolyzes six major human bile salts with a slight preference towards glycine-conjugated bile salts, the enzyme shows a broad range of substrate specificity, overview. The enzyme also slightly prefers to hydrolyze conjugated cholates over conjugated deoxycholates and chenodeoxycholates
-
-
?
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
?
-
Limosilactobacillus fermentum NCDO394
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
?
-
Limosilactobacillus fermentum NCDO394
the recombinant enzyme hydrolyzes six major human bile salts with a slight preference towards glycine-conjugated bile salts, the enzyme shows a broad range of substrate specificity, overview. The enzyme also slightly prefers to hydrolyze conjugated cholates over conjugated deoxycholates and chenodeoxycholates
-
-
?
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
?
-
Limosilactobacillus reuteri CRL 1098
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
?
-
-
catalyzes the deconjugation of conjugated bile acids to liberate free primary bile acids and amino acids
-
-
?
additional information
?
-
KJ571489
determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97)
-
-
?
additional information
?
-
-
determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97)
-
-
?
additional information
?
-
KJ571489
determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97)
-
-
?
