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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
cholic acid + H2O
? + glycine
-
-
-
-
?
cholyl-alpha-aminomethanesulfonic acid + H2O
cholic acid + aminomethanesulfonic acid
-
-
-
-
?
cholyl-beta-Ala + H2O
cholic acid + beta-Ala
-
-
-
-
?
cholyl-DL-Ala + H2O
cholic acid + DL-Ala
-
-
-
-
?
cholylsarcosine + H2O
cholic acid + sarcosine
-
low activity
-
-
?
cholyltaurine + H2O
cholic acid + taurine
-
-
-
-
?
glyco-conjugated bile acid + H2O
?
-
-
-
-
?
glycochenodeoxycholate + H2O
glycine + chenodeoxycholate
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + Gly
glycochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
glycocholate + H2O
cholate + glycine
glycocholate + H2O
glycine + cholate
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + Gly
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
glycocholic acid + H2O
?
-
-
-
?
glycocholic acid + H2O
cholate + glycine
glycocholic acid + H2O
cholic acid + glycine
glycodeoxycholate + H2O
3alpha,12alpha-dihydroxy-5-beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + Gly
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
glycohyodeoxycholate + H2O
glycine + hyodeoxycholate
glycolithocholic acid + H2O
lithocholate + glycine
-
preferred substrate
-
-
?
glycoursodeoxycholate + H2O
glycine + ursodeoxycholate
glycoursodeoxycholic acid + H2O
ursodeoxycholate + glycine
-
moderate activity
-
-
?
tauro-beta-muricholic acid + H2O
beta-muricholate + taurine
-
-
-
-
?
tauro-beta-muricholic acid + H2O
taurine + beta-muricholic acid
tauro-conjugated bile acid + H2O
?
-
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
taurochenodeoxycholate + H2O
taurine + chenodeoxycholate
taurochenodeoxycholic acid + H2O
3alpha,7alpha-dihydroxy-5beta-cholanate + taurine
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
taurocholate + H2O
taurine + cholate
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
taurocholic acid + H2O
cholate + taurine
taurodeoxycholate + H2O
taurine + deoxycholate
taurodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + taurine
taurodeoxycholic acid + H2O
deoxycholate + taurine
taurodeoxycholic acid + H2O
taurine + deoxycholate
-
-
-
-
?
taurohyodeoxycholic acid + H2O
?
-
-
-
-
?
taurolithocholic acid + H2O
lithocholate + taurine
-
preferred substrate
-
-
?
tauroursodeoxycholic acid + H2O
?
-
-
-
-
?
tauroursodeoxycholic acid + H2O
ursodeoxycholate + taurine
-
moderate activity
-
-
?
additional information
?
-
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
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
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
preferred substrate
-
-
?
glycocholate + H2O
cholate + glycine
preferred substrate
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
glycocholate + H2O
glycine + cholate
-
-
-
-
?
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
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
best substrate
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
best substrate
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
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
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
KJ571489
-
-
-
?
glycocholic acid + H2O
cholate + glycine
KJ571489
-
-
-
?
glycocholic acid + H2O
cholic acid + glycine
-
-
-
?
glycocholic acid + H2O
cholic acid + glycine
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
glycodeoxycholate + H2O
glycine + deoxycholate
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
best substrate
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
glycohyodeoxycholate + H2O
glycine + hyodeoxycholate
-
-
-
-
?
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
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
chenodeoxycholate + taurin
-
-
-
?
taurochenodeoxycholate + H2O
taurine + chenodeoxycholate
-
-
-
-
?
taurochenodeoxycholate + H2O
taurine + chenodeoxycholate
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
-
?
taurocholate + H2O
taurine + cholate
-
-
-
-
?
taurocholate + H2O
taurine + cholate
-
deconjugation
-
-
?
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
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
low activity
-
-
?
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
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
KJ571489
-
-
-
?
taurocholic acid + H2O
cholate + taurine
KJ571489
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
?
-
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
?
-
-
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
?
-
-
substrate specificity, 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
?
-
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
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-
?
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
?
-
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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 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 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 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
?
-
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 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
?
-
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 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
?
-
-
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)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cholic acid + H2O
? + glycine
-
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
glycocholate + H2O
cholate + glycine
glycocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
glycocholic acid + H2O
cholate + glycine
glycodeoxycholic acid + H2O
3alpha,12alpha-dihydroxy-5beta-cholanate + glycine
-
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
glycolithocholic acid + H2O
lithocholate + glycine
-
preferred substrate
-
-
?
glycoursodeoxycholic acid + H2O
ursodeoxycholate + glycine
-
moderate activity
-
-
?
tauro-beta-muricholic acid + H2O
beta-muricholate + taurine
-
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + taurine
taurocholate + H2O
taurine + cholate
-
-
-
?
taurocholic acid + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + taurine
taurocholic acid + H2O
cholate + taurine
taurodeoxycholate + H2O
taurine + deoxycholate
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
taurolithocholic acid + H2O
lithocholate + taurine
-
preferred substrate
-
-
?
tauroursodeoxycholic acid + H2O
ursodeoxycholate + taurine
-
moderate activity
-
-
?
additional information
?
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycochenodeoxycholic acid + H2O
chenodeoxycholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
-
-
-
?
glycocholate + H2O
cholate + glycine
preferred substrate
-
-
?
glycocholate + H2O
cholate + glycine
preferred substrate
-
-
?
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
-
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
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
-
-
-
?
glycocholic acid + H2O
cholate + glycine
KJ571489
-
-
-
?
glycocholic acid + H2O
cholate + glycine
KJ571489
-
-
-
?
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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
-
best substrate
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
glycodeoxycholic acid + H2O
deoxycholate + glycine
KJ571489
-
-
-
?
taurochenodeoxycholic acid + H2O
chenodeoxycholate + 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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
-
-
-
?
taurocholic acid + H2O
cholate + taurine
KJ571489
-
-
-
?
taurocholic acid + H2O
cholate + taurine
KJ571489
-
-
-
?
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
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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-
-
?
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
KJ571489
-
-
-
?
taurodeoxycholic acid + H2O
deoxycholate + taurine
KJ571489
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?
additional information
?
-
-
comparisons of substrate specificity and selective BSH activity in the human gut bacterial phylum Bacteroidetes, overview
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?
additional information
?
-
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comparisons of substrate specificity and selective BSH activity in the human gut bacterial phylum Bacteroidetes, overview
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-
?
additional information
?
-
the enzyme exhibits clear preference for glycine-conjugated bile salts over taurine-conjugated forms
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?
additional information
?
-
the enzyme exhibits clear preference for glycine-conjugated bile salts over taurine-conjugated forms
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-
?
additional information
?
-
-
the enzyme catalyzes the deconjugation of glycine- or taurine-linked bile salts
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?
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
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?
additional information
?
-
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catalyzes the hydrolysis of glycine- and taurine-conjugated bile salts to amino acid residues and free bile salts
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?
additional information
?
-
-
the enzyme hydrolyzes all of the six major human bile salts
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?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
-
isoform BSH1 prefers deoxycholic salts over chenodeoxycholic and cholic acid salts
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-
?
additional information
?
-
-
isoform BSH1 prefers deoxycholic salts over chenodeoxycholic and cholic acid salts
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-
?
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
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-
?
additional information
?
-
Escherichia coli strain SE1 expressing recombinant BSH56 efficiently hydrolyzes both tauro- and glyco-conjugated bile salts
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-
?
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
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-
?
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
?
-
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
?
-
-
oxgall is a substrate for the enzyme from different strains, overview
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-
?
additional information
?
-
Lactobacillus spp.
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enzyme activity is important for Lactobacillus colonization of human intestine
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?
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
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-
?
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)
-
-
?
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evolution
-
the BSH from Bifidobactrium longum demonstrates a evolutionary relationship with penicillin V acylase
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme
evolution
comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme
evolution
bile salt hydrolase (BSH) is a member of the N-terminal nucleophile hydrolase superfamily. Structure comparisons
evolution
bile salt hydrolase (BSH), a member of cholylglycine hydrolase family, catalyzes the de-conjugation of bile acids and is evolutionarily related to penicillin V acylase (PVA) that hydrolyses a different substrate such as penicillin V. Enterococcus faecalis bile salt hydrolase (BSH) has a manifold higher hydrolase activity compared to other known BSHs and displays unique allosteric catalytic property. The structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. An evolution-mediated subordination of the pre-peptide excision site results in loss of pre-peptide in EfBSH and other related cholylglycine hydrolases
evolution
enzyme BSH from Lactobacillus rhamnosus strain E9 belongs to the Ntn hydrolase super family, members of which are known to have conserved N-terminal cysteine residue (Cys1) in the active center. The enzyme is phylogenetically distant to the BSHs from other Lactobacillus spp. and genera but exhibits a close phylogenetic relationship with penicilling V acylase (PVA) from Bacillus sphaericus
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
evolution
-
microbial bile salt hydrolases (BSHs), a member of cholylglycine hydrolase (CGH) family. BSH is evolutionarily related to penicillin V acylase (PVA) which hydrolyses a penicillin V and is also a member of CGH family. five of the six amino acids, C2, R16, D19, N170, and R223, supposed to be responsible for catalytic activity of BSH enzyme, are strictly conserved in all CGH family members, N79 is partially conserved in the family
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
evolution
the enzyme belongs to the bile salt hydrolases and the penicillin V acylase family, phylogenetic analysis
evolution
-
various Lactobacillus species deconjugate bile acids in the human gastrointestinal tract (GIT) through the action of bile salt hydrolase (BSH) enzymes, screening of the Lactobacillus BSH repertoire across 170 sequenced species, CD-HIT clustering of BSH proteins, sequence determinations, and phylogenetic analysis, overview. Mapping the occurrence of BSH and PVA proteins onto a Lactobacillus phylogenetic tree
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
bile salt hydrolase (BSH) is a member of the N-terminal nucleophile hydrolase superfamily. Structure comparisons
-
evolution
-
comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme
-
evolution
-
comparative genomic, structural and biochemical analysis of the enzyme from Lactobacillus acidophilus and Lactobacillus salivarius, overview. The enzymes share similar structure by showing the typical canonic alphabetabetaalpha-folding pattern. The critical amino acids are also superimposed very well, particularly with respect to the typical Cys2, which serves as an N-terminal nucleophile, and Arg16, which play a potentially essential role in catalytic functioning of the enzyme
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
microbial bile salt hydrolases (BSHs), a member of cholylglycine hydrolase (CGH) family. BSH is evolutionarily related to penicillin V acylase (PVA) which hydrolyses a penicillin V and is also a member of CGH family. five of the six amino acids, C2, R16, D19, N170, and R223, supposed to be responsible for catalytic activity of BSH enzyme, are strictly conserved in all CGH family members, N79 is partially conserved in the family
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
the enzyme belongs to the bile salt hydrolases and the penicillin V acylase family, phylogenetic analysis
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
isolates of lactic acid bacteria (LAB) from flowers are genotyped and screened for the bile salt hydrolase activity on agar supplemented with 0.5% w/v taurodeoxycholic acid. The isolates are divided into two groups based on their phenotypic characteristics and 16S rRNA gene sequence analysis of the representative isolates. DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. Group I consists of 10 isolates, which are FM1-1, FM1-2, FM2-3, FM4-1, FM4-2, FM11-1, FM11-2, FM11-3, FM12-1, and FM12-2. Group II consists of six isolates, which are FM3-1, FM13-1, FM14-1, FM14-2, FM16-1, and FM16-2. Eleven isolates, including FM1-1, FM1-2, FM2-3, FM3-1, FM4-2, FM11-2, FM12-1, FM12-2, FM14-1, FM14-2, and FM16-2, exhibit bile salt hydrolase activity. All LAB isolates show cholesterol assimilation ability ranging from 9.57% to 51.69%. The isolate FM11-2 efficiently assimilates cholesterol with 51.69%
-
evolution
-
phylogenetic tree
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
enzyme BSH from Lactobacillus rhamnosus strain E9 belongs to the Ntn hydrolase super family, members of which are known to have conserved N-terminal cysteine residue (Cys1) in the active center. The enzyme is phylogenetically distant to the BSHs from other Lactobacillus spp. and genera but exhibits a close phylogenetic relationship with penicilling V acylase (PVA) from Bacillus sphaericus
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
sequence and phylogenetic analysis, family tree of BSH members with characterized substrate preference, overview
-
evolution
-
phylogenetic tree
-
malfunction
-
mechanisms underlying the effects of Lactobacillus overexpression of bile salt hydrolase in hypercholesterolemia. The liver mRNA levels of farnesoid X receptor (FXR) and small heterodimer partner (SHP) are significantly downregulated in the AR113 and pWQH01 groups compared to the high-cholesterol diet (HCD) and enzyme-lacking LC2W groups, whereas the mRNA expression of hepatic cholesterol 7alpha-hydroxylase (CYP7A1), liver X receptor (LXR) and low density lipoprotein receptor (LDLR) is significantly upregulated in the AR113 (wild-type, high activity) and pWQH01 (recombinant overexpressing) groups compared to the HCD group
malfunction
survival of BSH-positive Lactobacillus plantarum is significantly prolonged in the host gastointestinal tract compared to BSH-deleted Lactobacillus plantarum
malfunction
two serine residues next to nucleophile cysteine are essential for autocalytic processing to remove precursor peptide, but since a pre-peptide is absent in EfBSH the mutation of these serines is tolerated
malfunction
-
using isogenic strains of wild-type and BSH-deleted Bacteroides thetaiotaomicron, the levels of the bile acid tauro-beta-muricholic acid in monocolonized gnotobiotic mice are selectively modulated. Bacteroides thetaiotaomicron BSH mutant-colonized mice display altered metabolism, including reduced weight gain and respiratory exchange ratios, as well as transcriptional changes in metabolic, circadian rhythm, and immune pathways in the gut and liver
malfunction
-
mechanisms underlying the effects of Lactobacillus overexpression of bile salt hydrolase in hypercholesterolemia. The liver mRNA levels of farnesoid X receptor (FXR) and small heterodimer partner (SHP) are significantly downregulated in the AR113 and pWQH01 groups compared to the high-cholesterol diet (HCD) and enzyme-lacking LC2W groups, whereas the mRNA expression of hepatic cholesterol 7alpha-hydroxylase (CYP7A1), liver X receptor (LXR) and low density lipoprotein receptor (LDLR) is significantly upregulated in the AR113 (wild-type, high activity) and pWQH01 (recombinant overexpressing) groups compared to the HCD group
-
malfunction
-
survival of BSH-positive Lactobacillus plantarum is significantly prolonged in the host gastointestinal tract compared to BSH-deleted Lactobacillus plantarum
-
malfunction
-
using isogenic strains of wild-type and BSH-deleted Bacteroides thetaiotaomicron, the levels of the bile acid tauro-beta-muricholic acid in monocolonized gnotobiotic mice are selectively modulated. Bacteroides thetaiotaomicron BSH mutant-colonized mice display altered metabolism, including reduced weight gain and respiratory exchange ratios, as well as transcriptional changes in metabolic, circadian rhythm, and immune pathways in the gut and liver
-
metabolism
a key mechanism by which the microbiota in mammalian gut modify bile is through deconjugation of bile salts through bile salt hydrolase (BSH) enzymatic activity, which is postulated to be a prerequisite for all further microbial metabolism. BSH activity in the gut is largely considered to be beneficial for the host
metabolism
KJ571489
Staphylococcus epidermidis strain RM1 possess both potent bile salt hydrolase (BSH) and N-acyl homoserine lactone (AHL, EC 3.1.1.81) cleavage activity, the single enzyme, that is not responsible for both the activities, is identified as bile salt hydrolase, two different genetic elements correspond to each of the enzymatic activity
metabolism
-
a key mechanism by which the microbiota in mammalian gut modify bile is through deconjugation of bile salts through bile salt hydrolase (BSH) enzymatic activity, which is postulated to be a prerequisite for all further microbial metabolism. BSH activity in the gut is largely considered to be beneficial for the host
-
metabolism
-
a key mechanism by which the microbiota in mammalian gut modify bile is through deconjugation of bile salts through bile salt hydrolase (BSH) enzymatic activity, which is postulated to be a prerequisite for all further microbial metabolism. BSH activity in the gut is largely considered to be beneficial for the host
-
metabolism
-
Staphylococcus epidermidis strain RM1 possess both potent bile salt hydrolase (BSH) and N-acyl homoserine lactone (AHL, EC 3.1.1.81) cleavage activity, the single enzyme, that is not responsible for both the activities, is identified as bile salt hydrolase, two different genetic elements correspond to each of the enzymatic activity
-
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH is an enzyme produced by several bacterial species in the human or animal gastrointestinal tract that catalyzes the glycine- or taurine-linked bile salt deconjugation reaction. Presence of bile salt hydrolase in probiotics renders them more tolerant to bile salts, which also helps to reduce the blood cholesterol level of the host, physiological functions of probiotics, overview
physiological function
-
BSH plays a role in bile tolerance
physiological function
bile salt hydrolase (BSH) activity of the gut microbiota modulates the properties of bile salts, which are produced by the liver. BSH facilitates hydrolysis of the amide bond between the bile acid and glycine/taurine. The enzyme is a key regulator of bile acid homeostasis
physiological function
bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycineconjugated or taurine-conjugated bile acids. BSH enzyme catalyzes the deconjugation of glycine-conjugated or taurine-conjugated bile acids, which is an essential gateway reaction in the metabolism of bile acids in the small intestine
physiological function
bile salt hydrolase (BSH) is an enzyme that catalyses the deconjugation of bile salt. Lactobacillus plantarum RYPR1 is analyzed upon prebiotic utilization (with commercially available prebiotics lactulose, inulin, xylitol, raffinose, and oligofructose P95), catalytic interactions, and molecular docking with taurocholic and glycocholic acid. Residues Asn12, Ile8, and Leu6 interact with substrate taurocholic acid, and Lys88 and Asp126 interact with glycocholic acid. Molecular dynamics simulations, analysis of dynamic protein stability
physiological function
bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms
physiological function
bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms. Isozyme BSH47 exerts significant anti-giardial effects when tested in a murine model of giardiasis via Giardia duodenalis strain WB6
physiological function
-
bile salt hydrolase (BSH)-like activities of Lactobacilli protect against pathogenic infection with Giardia duodenalis. Giardia duodenalis is a protozoan parasite responsible for giardiasis, a disease characterized by intestinal malabsorption, diarrhea and abdominal pain in a large number of mammal species. Giardiasis is one of the most common intestinal parasitic diseases in the world. Several strains are tested, overview. The two most active strains in vitro are Lactobacillus johnsonii strain La1 and Lactobacillus gasseri strain CNCM I-4884. Only Lactobacillus gasseri strain CNCM I-4884 is able to significantly antagonize parasite growth with a dramatic reduction of the Giardia duodenalis strain WB6 trophozoites load in the small intestine
physiological function
bile salt hydrolase catalyzes the hydrolysis of glycine- or taurine-conjugated bile acids into the free bile acids and a glycine/taurine moiety, which will increase the de novo synthesis of bile acids from cholesterol in the human host, thus lowering the host serum cholesterol level
physiological function
BSH is important for lactic acid bacteria survival and adhesion in the host gut. Bile salt hydrolase (BSH) catalyzes the conversion of conjugated bile salts (mainly tauro- or glycol-conjugated bile salts) into free bile salts, and can significantly modulate the mouse gut microbiome
physiological function
mechanism of action of the BSH of probiotics against hypercholesterolemia related diseases
physiological function
-
microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans
physiological function
-
the enzyme exerts a cholesterol-reducing effect in vivo in the host, male C57BL/6J mice. Also the recombinant strain Lactobacillus casei pWQH01 overexpressing the enzyme from Lactobacillus plantarum strain AR113 shows a cholesterol-reducing effect in vivo in the host, both with a phenotype of reduced body weight. Effects of probiotics on the expression of key genes involved in bile acid and cholesterol metabolism in hypercholesterolemic mice, detailed overview
physiological function
-
the enzyme exerts a cholesterol-reducing effect in vivo in the host, male C57BL/6J mice. Also the recombinant strain Lactobacillus casei pWQH01 overexpressing the enzyme from Lactobacillus plantarum strain AR113 shows a cholesterol-reducing effect in vivo in the host, both with a phenotype of reduced body weight. Effects of probiotics on the expression of key genes involved in bile acid and cholesterol metabolism in hypercholesterolemic mice, detailed overview
-
physiological function
-
bile salt hydrolase (BSH) activity of the gut microbiota modulates the properties of bile salts, which are produced by the liver. BSH facilitates hydrolysis of the amide bond between the bile acid and glycine/taurine. The enzyme is a key regulator of bile acid homeostasis
-
physiological function
-
bile salt hydrolase catalyzes the hydrolysis of glycine- or taurine-conjugated bile acids into the free bile acids and a glycine/taurine moiety, which will increase the de novo synthesis of bile acids from cholesterol in the human host, thus lowering the host serum cholesterol level
-
physiological function
-
bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms. Isozyme BSH47 exerts significant anti-giardial effects when tested in a murine model of giardiasis via Giardia duodenalis strain WB6
-
physiological function
-
bile salt hydrolase (BSH)-like activities from the probiotic Lactobacillus johnsonii strain La1 may contribute to the anti-giardial activity displayed by this strain. Giardia duodenalis (syn. G. lamblia, G. intestinalis) is the protozoan parasite responsible for giardiasis, themost common and widely spread intestinal parasitic disease worldwide, affecting both humans and animals. After cysts ingestion (through either contaminated food or water), Giardia excysts in the upper intestinal tract to release replicating trophozoites that are responsible for the production of symptoms
-
physiological function
-
BSH is important for lactic acid bacteria survival and adhesion in the host gut. Bile salt hydrolase (BSH) catalyzes the conversion of conjugated bile salts (mainly tauro- or glycol-conjugated bile salts) into free bile salts, and can significantly modulate the mouse gut microbiome
-
physiological function
-
bile salt hydrolase (BSH) activity of the gut microbiota modulates the properties of bile salts, which are produced by the liver. BSH facilitates hydrolysis of the amide bond between the bile acid and glycine/taurine. The enzyme is a key regulator of bile acid homeostasis
-
physiological function
-
mechanism of action of the BSH of probiotics against hypercholesterolemia related diseases
-
physiological function
-
bile salt hydrolase (BSH) is a gut-bacterial enzyme that negatively influences host fat digestion and energy harvesting. The BSH enzyme activity functions as a gateway reaction in the small intestine by the deconjugation of glycineconjugated or taurine-conjugated bile acids. BSH enzyme catalyzes the deconjugation of glycine-conjugated or taurine-conjugated bile acids, which is an essential gateway reaction in the metabolism of bile acids in the small intestine
-
physiological function
-
microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans
-
physiological function
-
bile salt hydrolase (BSH)-like activities of Lactobacilli protect against pathogenic infection with Giardia duodenalis. Giardia duodenalis is a protozoan parasite responsible for giardiasis, a disease characterized by intestinal malabsorption, diarrhea and abdominal pain in a large number of mammal species. Giardiasis is one of the most common intestinal parasitic diseases in the world. Several strains are tested, overview. The two most active strains in vitro are Lactobacillus johnsonii strain La1 and Lactobacillus gasseri strain CNCM I-4884. Only Lactobacillus gasseri strain CNCM I-4884 is able to significantly antagonize parasite growth with a dramatic reduction of the Giardia duodenalis strain WB6 trophozoites load in the small intestine
-
physiological function
-
bile salt hydrolase (BSH) is an enzyme that catalyses the deconjugation of bile salt. Lactobacillus plantarum RYPR1 is analyzed upon prebiotic utilization (with commercially available prebiotics lactulose, inulin, xylitol, raffinose, and oligofructose P95), catalytic interactions, and molecular docking with taurocholic and glycocholic acid. Residues Asn12, Ile8, and Leu6 interact with substrate taurocholic acid, and Lys88 and Asp126 interact with glycocholic acid. Molecular dynamics simulations, analysis of dynamic protein stability
-
additional information
-
effect of oral administration to Wistar rats of the immobilized bile salt hydrolase enzyme on serum cholesterol, triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia, overview
additional information
-
probiotic organisms colonizing the host gastrointestinal tract need to be bile salt tolerant
additional information
structure modeling, overview
additional information
-
structure modeling, overview
additional information
enzymatic hydrolysis of bile salts by BSH generally relies on a N-terminal nucleophilic cysteine that attacks the amide bond of a bile salt to free the amino acid and form an intermediate covalent enzyme-bile acid complex, which is subsequently hydrolyzed, and leaves the cysteine free to participate in another catalytic cycle
additional information
enzyme structure homology model of LgBSH using the structure of Enterococcus faecalis BSH (PDB ID 4WL3) as a template. Residues involved in catalysis are identified based on the superimposed structure, including Cys1, Arg16, Asp19, Asn79, Asn171, and Arg224. Molecular docking analysis of ligands
additional information
-
enzyme structure homology model of LgBSH using the structure of Enterococcus faecalis BSH (PDB ID 4WL3) as a template. Residues involved in catalysis are identified based on the superimposed structure, including Cys1, Arg16, Asp19, Asn79, Asn171, and Arg224. Molecular docking analysis of ligands
additional information
expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
additional information
expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
KU961675
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
additional information
identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
additional information
-
identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
additional information
-
residue N79 might be important for substrate binding and catalytic turnover of BSH. Structure homology modelling using the crystal structure of BSH from Enterococcus faecalis (PDB ID 4wl3.1.B) as template. The homology modelling and 3D structure of BSH indicates that N79 residue is located near the catalytic center and within the cavity of substrates accessory to the enzyme
additional information
the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
additional information
-
the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
additional information
the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
additional information
the structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. The substrate binding pocket shows reduced volume owing to altered loop conformations and increased hydrophobicity contributed by a higher ratio of hydrophobic to hydrophilic groups present. The aromatic residues F18, Y20 and F65 participate in substrate binding. Effective polar complementarity present for the three hydroxyl groups of glycocholic acid substrate in the binding site contributing to higher substrate specificity and efficient catalysis. These are unique features characteristics of this BSH enzyme and thought to contribute to its higher activity and specificity towards bile salts as well as allosteric effects. Substrate docking and molecular dynamics simulation studies, overview
additional information
-
the structural analysis reveals a reduced secondary structure content compared to other known BSH structures, particularly devoid of an anti-parallel beta-sheet in the assembly loop and part of a beta-strand is converted to increase the length of a substrate binding loop 2. The substrate binding pocket shows reduced volume owing to altered loop conformations and increased hydrophobicity contributed by a higher ratio of hydrophobic to hydrophilic groups present. The aromatic residues F18, Y20 and F65 participate in substrate binding. Effective polar complementarity present for the three hydroxyl groups of glycocholic acid substrate in the binding site contributing to higher substrate specificity and efficient catalysis. These are unique features characteristics of this BSH enzyme and thought to contribute to its higher activity and specificity towards bile salts as well as allosteric effects. Substrate docking and molecular dynamics simulation studies, overview
additional information
-
enzymatic hydrolysis of bile salts by BSH generally relies on a N-terminal nucleophilic cysteine that attacks the amide bond of a bile salt to free the amino acid and form an intermediate covalent enzyme-bile acid complex, which is subsequently hydrolyzed, and leaves the cysteine free to participate in another catalytic cycle
-
additional information
-
enzymatic hydrolysis of bile salts by BSH generally relies on a N-terminal nucleophilic cysteine that attacks the amide bond of a bile salt to free the amino acid and form an intermediate covalent enzyme-bile acid complex, which is subsequently hydrolyzed, and leaves the cysteine free to participate in another catalytic cycle
-
additional information
-
enzyme structure homology model of LgBSH using the structure of Enterococcus faecalis BSH (PDB ID 4WL3) as a template. Residues involved in catalysis are identified based on the superimposed structure, including Cys1, Arg16, Asp19, Asn79, Asn171, and Arg224. Molecular docking analysis of ligands
-
additional information
-
expression of BSH1 increases the bile salt stress tolerance of lactic acid bacteria (LAB)
-
additional information
-
the active site in lsBSH is located in a shallow and water-exposed cavity formed by beta-sheets and four loops, loops 1-4. Loops 2 and 3 shape and partially close the active site of lsBSH from water exposure. Cys2 and Asn171 are critical for enzymatic activity, while Tyr24, Phe65 and Gln257 contribute to the substrate specificity. Structural insights into BSH-substrate interactions, the mechanism of catalysis, and substrate specificity, overview. Enzyme BSH is an N-terminal nucleophilic (Ntn) hydrolase. The enzyme undergoes an autocatalytic cleavage of the N-terminal residue to expose the cysteine residue to act as a nucleophile
-
additional information
-
identification of residues involved in catalysis and substrate specificity, structure-function analysis of BSH
-
additional information
-
structure modeling, overview
-
additional information
-
residue N79 might be important for substrate binding and catalytic turnover of BSH. Structure homology modelling using the crystal structure of BSH from Enterococcus faecalis (PDB ID 4wl3.1.B) as template. The homology modelling and 3D structure of BSH indicates that N79 residue is located near the catalytic center and within the cavity of substrates accessory to the enzyme
-
additional information
-
five putative active site residues, Cys2, Arg16, Asp19, Asn170, and Arg223 (bsh-1 enzyme amino acid numbering), are found in all four bsh proteins (BSH1-4) of Lactobacillus plantarum strain GD2, while the amino acid motifs around the active sites of BSH enzymes are not conserved among the four isozymes
-
additional information
-
the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
-
additional information
-
the active-site residues Cys2, Arg16, Asp19,Asn79, Asn170, and Arg223 are conserved
-
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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
brenda
Stellwag, E.J.; Hylemon, P.B.
Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis
Biochim. Biophys. Acta
452
165-176
1976
Bacteroides fragilis
brenda
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
brenda
Elkins, C.A.; Savage, D.C.
Identification of genes encoding conjugated bile salt hydrolase and transport in Lactobacillus johnsonii 100-100
J. Bacteriol.
180
4344-4349
1998
Lactobacillus johnsonii, Lactobacillus johnsonii 100-100
brenda
Lundeen, S.G.; Savage, D.C.
Multiple forms of bile salt hydrolase from Lactobacillus sp. strain 100-100
J. Bacteriol.
174
7217-7220
1992
Lactobacillus johnsonii, Lactobacillus johnsonii 100-100
brenda
Bateup, J.M.; McConnell, M.A.; Jenkinson, H.F.; Tannock, G.W.
Comparison of Lactobacillus strains with respect to bile salt hydrolase activity, colonization of the gastrointestinal tract and growth rate of the murine host
Appl. Environ. Microbiol.
61
1147-1149
1995
Lactobacillus delbrueckii, Lactobacillus sp., Lactobacillus sp. 100-14, Lactobacillus sp. 100-93
brenda
Lundeen, S.G.; Savage, D.S.
Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100
J. Bacteriol.
172
4171-4177
1990
Lactobacillus sp., Lactobacillus sp. 100-100
brenda
De Smet, I.; de Boever, P.; Verstraete, W.
Cholesterol lowering in pig through enhanced bacterial bile salt hydrolase activity
Br. J. Nutr.
79
185-194
1998
Limosilactobacillus reuteri
brenda
Tanaka, H.; Doesburg, K.; Iwasaki, T.; Mierau, I.
Screening of lactic acid bacteria for bile salt hydrolase actictivity
J. Dairy Sci.
82
2530-2535
1999
Amylolactobacillus amylophilus, Bifidobacterium adolescentis, Bifidobacterium animalis, Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium longum, Bifidobacterium longum subsp. infantis, Bifidobacterium pseudolongum, Bifidobacterium thermophilum, Companilactobacillus farciminis, Fructilactobacillus sanfranciscensis, Lacticaseibacillus casei, Lacticaseibacillus paracasei, Lacticaseibacillus rhamnosus, Lactiplantibacillus plantarum, Lactobacillus acidophilus, Lactobacillus crispatus, Lactobacillus gasseri, Lactobacillus helveticus, Lactobacillus johnsonii, Lactobacillus kefiranofaciens, Lentilactobacillus buchneri, Lentilactobacillus hilgardii, Ligilactobacillus salivarius, Limosilactobacillus fermentum, no activity in Bifidobacterium coryneforme, no activity in Lactococcus lactis, no activity in Leuconostoc mesenteroides, no activity in Streptococcus thermophilus
brenda
Corzo, G.; Gilliland, S.E.
Bile salt hydrolase activity of three strains of Lactobacillus acidophilus
J. Dairy Sci.
82
472-480
1999
Lactobacillus acidophilus
brenda
Kumar, R.S.; Brannigan, J.A.; Pundle, A.; Prabhune, A.; Dodson, G.G.; Suresh, C.G.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of conjugated bile salt hydrolase from Bifidobacterium longum
Acta Crystallogr. Sect. D
60
1665-1667
2004
Bifidobacterium longum
brenda
Moser, S.A.; Savage, D.C.
Bile salt hydrolase activity and resistance to toxicity of conjugated bile salts are unrelated properties in lactobacilli
Appl. Environ. Microbiol.
67
3476-3480
2001
Lactobacillus spp.
brenda
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 aviarius, Ligilactobacillus salivarius, Streptococcus alactolyticus
brenda
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Clostridium perfringens (P54965), Clostridium perfringens
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Delpino, M.V.; Marchesini, M.I.; Estein, S.M.; Comerci, D.J.; Cassataro, J.; Fossati, C.A.; Baldi, P.C.
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Brucella abortus (Q2YS20), Brucella abortus, Brucella abortus 2308 (Q2YS20), Brucella abortus 2308
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Xanthomonas maltophilia CBS 897.97 as a source of new 7beta- and 7alpha-hydroxysteroid dehydrogenases and cholylglycine hydrolase: improved biotransformations of bile acids
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Bos taurus, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia CBS 897.97
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Kumar, R.S.; Suresh, C.G.; Brannigan, J.A.; Dodson, G.G.; Gaikwad, S.M.
Bile salt hydrolase, the member of Ntn-hydrolase family: differential modes of structural and functional transitions during denaturation
IUBMB Life
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Bifidobacterium longum
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Oh, H.K.; Lee, J.Y.; Lim, S.J.; Kim, M.J.; Kim, G.B.; Kim, J.H.; Hong, S.K.; Kang, D.K.
Molecular cloning and characterization of a bile salt hydrolase from Lactobacillus acidophilus PF01
J. Microbiol. Biotechnol.
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Lactobacillus acidophilus
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Sridevi, N.; Prabhune, A.A.
Brevibacillus sp: A novel thermophilic source for the production of bile salt hydrolase
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Lambert, J.M.; Bongers, R.S.; de Vos, W.M.; Kleerebezem, M.
Functional analysis of four bile salt hydrolase and penicillin acylase family members in Lactobacillus plantarum WCFS1
Appl. Environ. Microbiol.
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Lactiplantibacillus plantarum WCFS1 (B9V401)
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Martoni, C.; Bhathena, J.; Urbanska, A.M.; Prakash, S.
Microencapsulated bile salt hydrolase producing Lactobacillus reuteri for oral targeted delivery in the gastrointestinal tract
Appl. Microbiol. Biotechnol.
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Bifidobacterium bifidum, Bifidobacterium longum subsp. infantis, Bifidobacterium longum, Limosilactobacillus reuteri
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Sridevi, N.; Srivastava, S.; Khan, B.M.; Prabhune, A.A.
Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp
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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
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Lactiplantibacillus plantarum WCFS1, Clostridium perfringens (P54965)
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Microbiology
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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)
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Jones, B.V.; Begley, M.; Hill, C.; Gahan, C.G.; Marchesi, J.R.
Functional and comparative metagenomic analysis of bile salt hydrolase activity in the human gut microbiome
Proc. Natl. Acad. Sci. USA
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Lacticaseibacillus casei
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Patel, A.K.; Singhania, R.R.; Pandey, A.; Chincholkar, S.B.
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Bifidobacterium longum, Brevibacillus sp., Clostridium perfringens, Lactobacillus acidophilus, Lactiplantibacillus plantarum, Lentilactobacillus buchneri, Limosilactobacillus fermentum, Lactobacillus johnsonii, Limosilactobacillus reuteri
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Sridevi, N.; Vishwe, P.; Prabhune, A.
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Lentilactobacillus buchneri
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Ahmed, N.; Ajmal, S.; Pervez, S.
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Lactobacillus sp.
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Bustos, A.Y.; Saavedra, L.; de Valdez, G.F.; Raya, R.R.; Taranto, M.P.
Relationship between bile salt hydrolase activity, changes in the internal pH and tolerance to bile acids in lactic acid bacteria
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Enterococcus faecium, Lactobacillus acidophilus, Limosilactobacillus reuteri, no activity in Lactobacillus delbrueckii strain CRL 494, no activity in Lactobacillus delbrueckii strain CRL 454, no activity in Lactobacillus acidophilus strain CRL 1072, no activity in Lactobacillus plantarum strain CRL 573, no activity in Lactobacillus casei strain CRL 203, Limosilactobacillus reuteri CRL 1100, Limosilactobacillus reuteri CRL 1101, Limosilactobacillus reuteri CRL 1098, Lactobacillus acidophilus CRL 44, Enterococcus faecium CRL 183
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Ren, J.; Sun, K.; Wu, Z.; Yao, J.; Guo, B.
All 4 bile salt hydrolase proteins are responsible for the hydrolysis activity in Lactobacillus plantarum ST-III
J. Food Sci.
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ST-III
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Jarocki, P.
Molecular characterization of bile salt hydrolase from Bifidobacterium animalis subsp. lactis Bi30
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Bifidobacterium animalis subsp. lactis (G0YYC2), Bifidobacterium animalis subsp. lactis Bi30 (G0YYC2)
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Wang, Z.; Zeng, X.; Mo, Y.; Smith, K.; Guo, Y.; Lin, J.
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Ligilactobacillus salivarius (J7H3P9), Ligilactobacillus salivarius, Ligilactobacillus salivarius NRRL B-30514 (J7H3P9)
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Chae, J.P.; Valeriano, V.D.; Kim, G.B.; Kang, D.K.
Molecular cloning, characterization and comparison of bile salt hydrolases from Lactobacillus johnsonii PF01
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Lactobacillus johnsonii (A0A1B3PS02), Lactobacillus johnsonii (A0A4S2CHH9), Lactobacillus johnsonii (A0A4Z0GFP0), Lactobacillus johnsonii PF01 (A0A1B3PS02), Lactobacillus johnsonii PF01 (A0A4S2CHH9), Lactobacillus johnsonii PF01 (A0A4Z0GFP0), Lactobacillus johnsonii PF01
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Dong, Z.; Zhang, J.; Lee, B.; Li, H.; Du, G.; Chen, J.
Secretory expression and characterization of a bile salt hydrolase from Lactobacillus plantarum in Escherichia coli
J. Mol. Catal. B
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum BBE7
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Bi, J.; Fang, F.; Lu, S.; Du, G.; Chen, J.
New insight into the catalytic properties of bile salt hydrolase
J. Mol. Catal. B
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Ligilactobacillus salivarius, Ligilactobacillus salivarius LMG14476
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Kumar, R.; Rajkumar, H.; Kumar, M.; Varikuti, S.R.; Athimamula, R.; Shujauddin, M.; Ramagoni, R.; Kondapalli, N.
Molecular cloning, characterization and heterologous expression of bile salt hydrolase (Bsh) from Lactobacillus fermentum NCDO394
Mol. Biol. Rep.
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2013
Limosilactobacillus fermentum (H6WSA2), Limosilactobacillus fermentum, Limosilactobacillus fermentum NCDO394 (H6WSA2)
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Lin, J.; Negga, R.; Zeng, X.; Smith, K.
Effect of bile salt hydrolase inhibitors on a bile salt hydrolase from Lactobacillus acidophilus
Pathogens
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2014
Lactobacillus acidophilus (A5HKP3), Lactobacillus acidophilus, Ligilactobacillus salivarius (J7H3P9), Ligilactobacillus salivarius, Ligilactobacillus salivarius NRRL B-30514 (J7H3P9), Lactobacillus acidophilus PF01 (A5HKP3)
brenda
Jarocki, P.; Podlesny, M.; Glibowski, P.; Targonski, Z.
A new insight into the physiological role of bile salt hydrolase among intestinal bacteria from the genus Bifidobacterium
PLoS ONE
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Bifidobacterium longum, Bifidobacterium longum (A0A087D2Y1), Bifidobacterium longum (I3QNT4), no activity in Bifidobacterium asteroides DSM 20089, no activity in Bifidobacterium coryneforme DSM 20216, no activity in Lactobacillus rhamnosus strain NRRL B-442, Bifidobacterium adolescentis (I3QNS7), Bifidobacterium animalis (I3QNS8), Bifidobacterium animalis (I3QNS9), Bifidobacterium bifidum (I3QNT0), Bifidobacterium breve (I3QNT2), Bifidobacterium pseudocatenulatum (I3QNT6), Bifidobacterium pseudocatenulatum, Bifidobacterium pseudolongum (L0CM48), Bifidobacterium pseudocatenulatum DSM 20224 (I3QNT6), Bifidobacterium bifidum DSM 20456 (I3QNT0), Bifidobacterium animalis NRRL B-41406 (I3QNS8), Bifidobacterium animalis NRRL B-41405 (I3QNS9), Bifidobacterium pseudocatenulatum DSM 20439 (I3QNT6), Bifidobacterium longum NRRL B-41409, Bifidobacterium longum NRRL B-41407 (A0A087D2Y1), Bifidobacterium longum ATCC 15697 (I3QNT4), Bifidobacterium breve DSM 20091 (I3QNT2), Bifidobacterium breve NRRL B-41408 (I3QNT2), Bifidobacterium pseudolongum DSM 20095 (L0CM48), Bifidobacterium adolescentis DSM 20087 (I3QNS7)
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Smith, K.; Zeng, X.; Lin, J.
Discovery of bile salt hydrolase inhibitors using an efficient high-throughput screening system
PLoS ONE
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Ligilactobacillus salivarius
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Xu, F.; Guo, F.; Hu, X.J.; Lin, J.
Crystal structure of bile salt hydrolase from Lactobacillus salivarius
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2016
Ligilactobacillus salivarius (J7GY78), Ligilactobacillus salivarius, Ligilactobacillus salivarius NRRL B-30514 (J7GY78)
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Mukherji, R.; Prabhune, A.
Possible correlation between bile salt hydrolysis and AHL deamidation Staphylococcus epidermidis RM1, a potent quorum quencher and bile salt hydrolase producer
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Staphylococcus epidermidis (KJ571489), Staphylococcus epidermidis, Staphylococcus epidermidis RM1 (KJ571489)
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Dong, Z.; Zhang, J.; Du, G.; Chen, J.; Li, H.; Lee, B.
Periplasmic export of bile salt hydrolase in Escherichia coli by the twin-arginine signal peptides
Appl. Biochem. Biotechnol.
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2015
Lactiplantibacillus plantarum (B9V401), Lactiplantibacillus plantarum BBE7 (B9V401)
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Chand, D.; Panigrahi, P.; Varshney, N.; Ramasamy, S.; Suresh, C.G.
Structure and function of a highly active bile salt hydrolase (BSH) from Enterococcus faecalis and post-translational processing of BSH enzymes
Biochim. Biophys. Acta
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2018
Enterococcus faecalis (Q83YZ2), Enterococcus faecalis
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Bi, J.; Liu, S.; Du, G.; Chen, J.
Bile salt tolerance of Lactococcus lactis is enhanced by expression of bile salt hydrolase thereby producing less bile acid in the cells
Biotechnol. Lett.
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2016
Ligilactobacillus salivarius (C7AQX9), Ligilactobacillus salivarius (C7AQY2), Ligilactobacillus salivarius LMG14476 (C7AQX9), Ligilactobacillus salivarius LMG14476 (C7AQY2)
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Yao, L.; Seaton, S.C.; Ndousse-Fetter, S.; Adhikari, A.A.; DiBenedetto, N.; Mina, A.I.; Banks, A.S.; Bry, L.; Devlin, A.S.
A selective gut bacterial bile salt hydrolase alters host metabolism
eLife
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Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron VPI-5482
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Yang, Y.; Liu, Y.; Zhou, S.; Huang, L.; Chen, Y.; Huan, H.
Bile salt hydrolase can improve Lactobacillus plantarum survival in gastrointestinal tract by enhancing their adhesion ability
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Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC BAA-793 (Q06115)
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Kaya, Y.; Koek, M.; Oeztuerk, M.
Molecular cloning, expression and characterization of bile salt hydrolase from Lactobacillus rhamnosus E9 strain
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2017
Lacticaseibacillus rhamnosus (G4XR38), Lacticaseibacillus rhamnosus E9 (G4XR38)
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Oeztuerk, M.; Aydin, Y.; Kilicsaymaz, Z.; Oenal, C.; Ba, N.
Molecular cloning, characterization, and comparison of four bile salt hydrolase-related enzymes from Lactobacillus plantarum GD2 of human origin
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32
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2018
Lactiplantibacillus plantarum (A0A193H6Q2), Lactiplantibacillus plantarum (A0A1B1FMJ8), Lactiplantibacillus plantarum (A0A1I9RYI4), Lactiplantibacillus plantarum (KU961675), Lactiplantibacillus plantarum GD2 (A0A193H6Q2), Lactiplantibacillus plantarum GD2 (A0A1B1FMJ8), Lactiplantibacillus plantarum GD2 (A0A1I9RYI4), Lactiplantibacillus plantarum GD2 (KU961675)
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Ba, N.; Oeztuerk, M.
Molecular cloning and characterization of bile salt hydrolase from Lactobacillus gasseri ATCC 33323 strain
Food Biotechnol.
32
95-111
2018
Lactobacillus gasseri (A0A1V0FWZ3), Lactobacillus gasseri ATCC 33323 (A0A1V0FWZ3)
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Wang, G.; Huang, W.; Xia, Y.; Xiong, Z.; Ai, L.
Cholesterol-lowering potentials of Lactobacillus strain overexpression of bile salt hydrolase on high cholesterol diet-induced hypercholesterolemic mice
Food Funct.
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2019
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum AR113, no activity in Lactobacillus casei strain LC2W
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Yadav, R.; Singh, P.K.; Puniya, A.K.; Shukla, P.
Catalytic Interactions and molecular docking of bile salt hydrolase (BSH) from L. plantarum RYPR1 and its prebiotic utilization
Front. Microbiol.
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Lactiplantibacillus plantarum (B9V401), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum RYPR1 (B9V401)
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Rani, R.P.; Anandharaj, M.; Ravindran, A.D.
Characterization of bile salt hydrolase from Lactobacillus gasseri FR4 and demonstration of its substrate specificity and inhibitory mechanism using molecular docking analysis
Front. Microbiol.
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1004
2017
Lactobacillus gasseri (B9V405), Lactobacillus gasseri, Lactobacillus gasseri FR4 (B9V405)
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Allain, T.; Chaouch, S.; Thomas, M.; Vallee, I.; Buret, A.; Langella, P.; Grellier, P.; Polack, B.; Bermudez-Humaran, L.; Florent, I.
Bile-salt-hydrolases from the probiotic strain Lactobacillus johnsonii La1 mediate anti-giardial activity in vitro and in vivo
Front. Microbiol.
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2707
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Lactobacillus johnsonii (Q74IV4), Lactobacillus johnsonii (Q74JG0), Lactobacillus johnsonii (Q74LX7), Lactobacillus johnsonii La1 (Q74IV4), Lactobacillus johnsonii La1 (Q74JG0), Lactobacillus johnsonii La1 (Q74LX7)
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Allain, T.; Chaouch, S.; Thomas, M.; Travers, M.A.; Valle, I.; Langella, P.; Grellier, P.; Polack, B.; Florent, I.; Bermudez-Humaran, L.G.
Bile salt hydrolase activities a novel target to screen anti-giardia Lactobacilli?
Front. Microbiol.
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Lactobacillus gasseri, Lactobacillus gasseri CNCM I-4884
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Nuhwa, R.; Tanasupawat, S.; Taweechotipatr, M.; Sitdhipol, J.; Savarajara, A.
Bile salt hydrolase activity and cholesterol assimilation of lactic acid bacteria isolated from flowers
J. Appl. Pharm. Sci.
9
106-110
2019
Enterococcus sp., Enterococcus gallinarum, Enterococcus lactis, Enterococcus durans (A0A023J8T6), Lactiplantibacillus plantarum subsp. plantarum (A0A1U9X493), Enterococcus durans NBRC 100479 (A0A023J8T6), Enterococcus gallinarum NBRC 100675, Lactiplantibacillus plantarum subsp. plantarum ATCC 14917 (A0A1U9X493), Enterococcus lactis DSM 23655
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Oeztuerk, M.; Oenal, C.
Asparagine 79 is an important amino acid for catalytic activity and substrate specificity of bile salt hydrolase (BSH)
Mol. Biol. Rep.
46
4361-4368
2019
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum B14
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OFlaherty, S.; Briner Crawley, A.; Theriot, C.M.; Barrangou, R.
The Lactobacillus bile salt hydrolase repertoire reveals niche-specific adaptation
mSphere
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2018
Lactobacillus sp.
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Chand, D.; Ramasamy, S.; Suresh, C.
A highly active bile salt hydrolase from Enterococcus faecalis shows positive cooperative kinetics
Process Biochem.
51
263-269
2016
Enterococcus faecalis (C7CXJ5), Enterococcus faecium (Q83YZ2), Enterococcus faecalis NCIM 2403 (C7CXJ5), Enterococcus faecalis T2 (C7CXJ5)
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Dong, Z.; Lee, B.H.
Bile salt hydrolases structure and function, substrate preference, and inhibitor development
Protein Sci.
27
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2018
Enterococcus faecalis, Lactiplantibacillus plantarum, Lactiplantibacillus plantarum (Q06115), Lactobacillus johnsonii, Lactobacillus johnsonii (A0A1B3PS02), Lactobacillus johnsonii (A0A4Z0GFP0), Lactobacillus johnsonii (P97038), Lactobacillus johnsonii (Q9F660), Ligilactobacillus salivarius, Ligilactobacillus salivarius (C7AQX8), Ligilactobacillus salivarius (C7AQX9), Ligilactobacillus salivarius (C7AQY2), Ligilactobacillus salivarius (J7H3P9), Ligilactobacillus salivarius (M1R367), Ligilactobacillus salivarius (M1R991), Ligilactobacillus salivarius (Q1WR93), Bifidobacterium longum subsp. suis (A0A087BL81), Lactobacillus gasseri (A0A1Y0E209), Lactobacillus gasseri (B9V405), Limosilactobacillus reuteri (B5TQZ0), Bifidobacterium pseudocatenulatum (C0BTD8), Bifidobacterium animalis (G0YYC2), Bifidobacterium animalis (Q53CP8), Lacticaseibacillus rhamnosus (G4XR38), Limosilactobacillus fermentum (H6WSA2), Clostridium perfringens (P54965), Lactobacillus acidophilus (Q5FK51), Lactobacillus acidophilus (Q5FKM3), Bifidobacterium bifidum (Q6R974), Bifidobacterium longum subsp. Longum (Q9KK62), Lactiplantibacillus plantarum NCIMB 8826 (Q06115), Lactiplantibacillus plantarum BBE7, Lactiplantibacillus plantarum ATCC BAA-793 (Q06115), Lactobacillus gasseri FR4 (A0A1Y0E209), Lactobacillus johnsonii 100-100 (P97038), Lactobacillus johnsonii 100-100 (Q9F660), Bifidobacterium longum subsp. Longum SBT2928 (Q9KK62), Bifidobacterium longum subsp. suis LMG 21814 (A0A087BL81), Bifidobacterium animalis KL612 (Q53CP8), Ligilactobacillus salivarius CGMCC 8198, Ligilactobacillus salivarius CGMCC 8198 (M1R367), Ligilactobacillus salivarius CGMCC 8198 (M1R991), Lactobacillus acidophilus NCFM (Q5FK51), Lactobacillus acidophilus NCFM (Q5FKM3), Ligilactobacillus salivarius UCC118 (Q1WR93), Clostridium perfringens type A (P54965), Ligilactobacillus salivarius JCM1046 (C7AQX8), Clostridium perfringens 13 (P54965), Bifidobacterium bifidum ATCC 11863 (Q6R974), Lactobacillus gasseri Am1 (B9V405), Lactobacillus acidophilus ATCC 700396 (Q5FK51), Lactobacillus acidophilus ATCC 700396 (Q5FKM3), Ligilactobacillus salivarius LGM14476 (C7AQX9), Ligilactobacillus salivarius LGM14476 (C7AQY2), Limosilactobacillus reuteri CRL 1098 (B5TQZ0), Lactobacillus johnsonii PF01, Lactobacillus johnsonii PF01 (A0A1B3PS02), Lactobacillus johnsonii PF01 (A0A4Z0GFP0), Lactobacillus acidophilus NCK56 (Q5FK51), Lactobacillus acidophilus NCK56 (Q5FKM3), Bifidobacterium animalis Bi30 (G0YYC2), Lactobacillus acidophilus N2 (Q5FK51), Lactobacillus acidophilus N2 (Q5FKM3), Enterococcus faecalis NCIM 2403, Bifidobacterium pseudocatenulatum DSM 20438 (C0BTD8), Limosilactobacillus fermentum NCDO394 (H6WSA2), Lacticaseibacillus rhamnosus E9 (G4XR38), Ligilactobacillus salivarius B-30514 (J7H3P9)
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Xu, F.; Hu, X.J.; Singh, W.; Geng, W.; Tikhonova, I.G.; Lin, J.
The complex structure of bile salt hydrolase from Lactobacillus salivarius reveals the structural basis of substrate specificity
Sci. Rep.
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12438
2019
Ligilactobacillus salivarius (C7AQX8), Ligilactobacillus salivarius, Ligilactobacillus salivarius NRRL B-30514 (C7AQX8)
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Brandvold, K.R.; Weaver, J.M.; Whidbey, C.; Wright, A.T.
A continuous fluorescence assay for simple quantification of bile salt hydrolase activity in the gut microbiome
Sci. Rep.
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1359
2019
Lactiplantibacillus plantarum (Q06115), Lactiplantibacillus plantarum NCIMB 8826 (Q06115), Lactiplantibacillus plantarum ATCC BAA-793 (Q06115)
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