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
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cholic
-
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 (KM Value
KM Value on EC 3.5.1.24 - choloylglycine hydrolase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.028
glycochenodeoxycholate
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pH 6.5, 40°C, recombinant wild-type enzyme
0.042
taurochenodeoxycholate
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pH 6.5, 40°C, recombinant wild-type enzyme
0.91
glycochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH1, in presence of DTT
2.17
glycochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH2, in presence of DTT
2.48
glycochenodeoxycholic acid
pH 5.4, 37°C, recombinant enzyme
15.02
glycochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH1
15.04
glycochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH2
16.97
glycochenodeoxycholic acid
about, pH 5.0, 50°C, recombinant enzyme
0.5
glycocholic acid
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pH 5.8-6.3, temperature not specified in the publication
0.00308
glycodeoxycholic acid
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apparent value, calculated from a Lineweaver-Burk plot
0.00308
glycodeoxycholic acid
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pH not specified in the publication, temperature not specified in the publication
1.15
glycodeoxycholic acid
pH 5.4, 37°C, recombinant enzyme
9.94
glycodeoxycholic acid
about, pH 5.0, 50°C, recombinant enzyme
11.88
glycodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH2
14.12
glycodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH1
2.5 - 3
taurochenodeoxycholic acid
pH 5.4, 37°C, recombinant enzyme
4.49
taurochenodeoxycholic acid
about, pH 5.0, 50°C, recombinant enzyme
14.83
taurochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH2
17.16
taurochenodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH1
3.19
taurodeoxycholic acid
pH 5.4, 37°C, recombinant enzyme
9.28
taurodeoxycholic acid
about, pH 5.0, 50°C, recombinant enzyme
15.77
taurodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH1
18.12
taurodeoxycholic acid
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pH 6.5, 37°C, recombinant isozyme BSH2
additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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isozymes BSH1 and BSH2 are allosteric enzymes, and show positive cooperativity, catalytic efficiency and substrate preference, but with differences, overview. Michaelis-Menten kinetics in the presence of dithiothreitol, but not in its absence. Steady-state kinetics, overview
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additional information
additional information
the enzyme demonstrates unique enzyme kinetics of non-linear regression, thereby displaying positive cooperativity
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additional information
additional information
the enzyme demonstrates unique enzyme kinetics of non-linear regression, thereby displaying positive cooperativity, steady-state kinetics
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