3.5.1.24: choloylglycine hydrolase
This is an abbreviated version!
For detailed information about choloylglycine hydrolase, go to the full flat file.
Word Map on EC 3.5.1.24
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3.5.1.24
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lactobacillus
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cholesterol
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deconjugation
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plantarum
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microbiota
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cholesterol-lowering
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bifidobacterium
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taurodeoxycholic
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cholic
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taurocholic
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glycocholic
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drug development
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glycodeoxycholic
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farnesoid
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co-aggregation
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pentosaceus
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rhamnosus
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glycine-conjugated
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pentosus
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pediococcus
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acylase
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fermentum
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auto-aggregation
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taurine-conjugated
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rogosa
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medicine
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food industry
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taurochenodeoxycholic
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oxgall
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nutrition
- 3.5.1.24
- lactobacillus
- cholesterol
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deconjugation
- plantarum
- microbiota
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cholesterol-lowering
- bifidobacterium
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taurodeoxycholic
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cholic
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taurocholic
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glycocholic
- drug development
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glycodeoxycholic
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farnesoid
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co-aggregation
- pentosaceus
- rhamnosus
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glycine-conjugated
- pentosus
- pediococcus
- acylase
- fermentum
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auto-aggregation
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taurine-conjugated
-
rogosa
- medicine
- food industry
- taurochenodeoxycholic
-
oxgall
- nutrition
Reaction
Synonyms
BAH1, BFS26_06805, bile acid hydrolase, bile salt hydrolase, Bile-Salt-Hydrolase, BSH, BSH A, BSH B, BSH C, BSH1, BSH12, BSH2, BSH3, BSH4, BSH47, BSH56, BSHA, BSHB, BSHC, BT2086, C3745_01535, CBAH, CBH, CBSHalpha, CBSHbeta, CGH, cholylglycine hydrolase, Conjugated bile acid hydrolase, conjugated bile salt hydrolase, conjugated bile salt hydrolase alpha peptide, conjugated bile salt hydrolase beta, EFBG_01849, EfBSH, glycocholase, LaciP, LgBSH, linear amide C-N hydrolase, LJ1412, LJ_0056, LJ_1147, LsalN1, lsBSH, More, probiotic bile salt hydrolase, salt hydrolase
ECTree
3.5.1.24 choloylglycine hydrolaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.5.1.24 - choloylglycine hydrolase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cholate
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uncompetitive inhibition of glycocholic acid hydrolysis
phenylmethylsulfonyl fluoride
90.9% residual activity at 0.5 mM
Sodium periodate
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about 99% inhibition at 0.1-2 mM, complete inhibition at 10 mM
taurine
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uncompetitive inhibition of glycocholic acid hydrolysis
taurocholic acid
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competitive inhibition of glycocholic acid hydrolysis
4-chloromercuriacetate
over 98% inhibition at 0.01 mM
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4-chloromercuriacetate
over 98% inhibition at 0.01 mM
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caffeic acid phenethyl ester
71.8% inhibition of recombinant enzyme at 5 mM, 80% at 10 mM, 50% at 03125 mM
demeclocycline
99.6% inhibition of recombinant enzyme at 2.5 mM
doxycycline
98.3% inhibition of recombinant enzyme at 2.5 mM
epicatechin monogallate
52.8% inhibition of recombinant enzyme at 5 mM
methacycline
99.2% inhibition of recombinant enzyme at 2.5 mM
oxytetracycline
99.6% inhibition of recombinant enzyme at 2.5 mM
Penicillin V
Pen V, modulating effect of the non-substrate ligand Pen V on the hydrolysing ability of EfBSH towards bile acid such as glycodeoxycholic acid, competitive inhibition of BSH activity by Pen V
purpurogallin
36.1% inhibition of recombinant enzyme at 5 mM
riboflavin
96.5% inhibition of recombinant enzyme at 0.5 mM, 50% at 0.016 mM
additional information
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BSH is vigorously inhibited by thiol enzyme inhibitors
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additional information
no effect on enzyme activity by EDTA. Penicilin V (Pen V) is expected to cause competitive inhibition of BSH activity, but EfBSH shows enhanced activity towards glycodeoxycholic acid in the presence of Pen V, and no inhibition is observed, contrary to the expected results
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additional information
chloroform, 2-mercaptoethanol and EDTA show poor effects on the enzyme activity. Proteinase K almost completely abolishes the enzyme activity, strong inhibition by pepsin. The enzyme is not affected by alpha-amylase and catalase, and only slightly by lysozyme
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additional information
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chloroform, 2-mercaptoethanol and EDTA show poor effects on the enzyme activity. Proteinase K almost completely abolishes the enzyme activity, strong inhibition by pepsin. The enzyme is not affected by alpha-amylase and catalase, and only slightly by lysozyme
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additional information
the broad substrate specificity nature of Lactobacillus salivarius enzyme may make it an ideal candidate for screening desired BSH inhibitors targeting various BSH enzymes
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additional information
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the broad substrate specificity nature of Lactobacillus salivarius enzyme may make it an ideal candidate for screening desired BSH inhibitors targeting various BSH enzymes
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additional information
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identification of bile salt hydrolase inhibitors using an efficient high-throughput screening system, method optimization, overview; no inhibition by folic acid at 1.5 mM and bacitracin at 5 mM
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