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
-
deconjugation
- plantarum
- microbiota
-
cholesterol-lowering
- bifidobacterium
-
taurodeoxycholic
-
cholic
-
taurocholic
-
glycocholic
- drug development
-
glycodeoxycholic
-
farnesoid
-
co-aggregation
- pentosaceus
- rhamnosus
-
glycine-conjugated
- pentosus
- pediococcus
- acylase
- fermentum
-
auto-aggregation
-
taurine-conjugated
-
rogosa
- medicine
- food industry
- taurochenodeoxycholic
-
oxgall
- nutrition
Reaction
Synonyms
BAH1, BFS26_06805, bile acid hydrolase, bile salt hydrolase, Bile-Salt-Hydrolase, BSH, BSH A, BSH B, BSH C, BSH1, BSH12, BSH2, BSH3, BSH4, BSH47, BSH56, BSHA, BSHB, BSHC, BT2086, C3745_01535, CBAH, CBH, CBSHalpha, CBSHbeta, CGH, cholylglycine hydrolase, Conjugated bile acid hydrolase, conjugated bile salt hydrolase, conjugated bile salt hydrolase alpha peptide, conjugated bile salt hydrolase beta, EFBG_01849, EfBSH, glycocholase, LaciP, LgBSH, linear amide C-N hydrolase, LJ1412, LJ_0056, LJ_1147, LsalN1, lsBSH, More, probiotic bile salt hydrolase, salt hydrolase
ECTree
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Reaction
Reaction on EC 3.5.1.24 - choloylglycine hydrolase
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glycocholate + H2O = cholate + glycine
substrate binding pocket and active site structure, taurine has a reversed orientation pointing with its sulfo group towards Cys2 and leaving the active site with its amino group ahead, overview
glycocholate + H2O = cholate + glycine
substrate specificity and active site structure, residues Cys1, Arg17, Asp20, Asn174, and Arg227 are important for catalysis, Trp21 plays a selective role in binding of bile salt while it suppresses productive binding of substrate analogue penicillin V
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