3.5.1.24: choloylglycine hydrolase
This is an abbreviated version!
For detailed information about choloylglycine hydrolase, go to the full flat file.
Word Map on EC 3.5.1.24
-
3.5.1.24
-
lactobacillus
-
cholesterol
-
deconjugation
-
plantarum
-
microbiota
-
cholesterol-lowering
-
bifidobacterium
-
taurodeoxycholic
-
cholic
-
taurocholic
-
glycocholic
-
drug development
-
glycodeoxycholic
-
farnesoid
-
co-aggregation
-
pentosaceus
-
rhamnosus
-
glycine-conjugated
-
pentosus
-
pediococcus
-
acylase
-
fermentum
-
auto-aggregation
-
taurine-conjugated
-
rogosa
-
medicine
-
food industry
-
taurochenodeoxycholic
-
oxgall
-
nutrition
- 3.5.1.24
- lactobacillus
- cholesterol
-
deconjugation
- plantarum
- microbiota
-
cholesterol-lowering
- bifidobacterium
-
taurodeoxycholic
-
cholic
-
taurocholic
-
glycocholic
- drug development
-
glycodeoxycholic
-
farnesoid
-
co-aggregation
- pentosaceus
- rhamnosus
-
glycine-conjugated
- pentosus
- pediococcus
- acylase
- fermentum
-
auto-aggregation
-
taurine-conjugated
-
rogosa
- medicine
- food industry
- taurochenodeoxycholic
-
oxgall
- nutrition
Reaction
Synonyms
BAH1, BFS26_06805, bile acid hydrolase, bile salt hydrolase, Bile-Salt-Hydrolase, BSH, BSH A, BSH B, BSH C, BSH1, BSH12, BSH2, BSH3, BSH4, BSH47, BSH56, BSHA, BSHB, BSHC, BT2086, C3745_01535, CBAH, CBH, CBSHalpha, CBSHbeta, CGH, cholylglycine hydrolase, Conjugated bile acid hydrolase, conjugated bile salt hydrolase, conjugated bile salt hydrolase alpha peptide, conjugated bile salt hydrolase beta, EFBG_01849, EfBSH, glycocholase, LaciP, LgBSH, linear amide C-N hydrolase, LJ1412, LJ_0056, LJ_1147, LsalN1, lsBSH, More, probiotic bile salt hydrolase, salt hydrolase
ECTree
Advanced search results
Subunits
Subunits on EC 3.5.1.24 - choloylglycine hydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
homodimer
homotetramer
oligomer
tetramer
trimer
additional information
?
x * 37000, about, sequence calculation, x * 37000-40000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 37000, about, sequence calculation, x * 37000-40000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 36500, SDS-PAGE
?
x * 36000, SDS-PAGE
?
x * 37000, SDS-PAGE
?
x * 37500, SDS-PAGE
?
x * 35700, SDS-PAGE
?
x * 36100, SDS-PAGE
?
x * 36490, sequence calculation, x * 36500, recombinant His6-tagged enzyme, SDS-PAGE
?
Limosilactobacillus fermentum NCDO394
-
x * 36490, sequence calculation, x * 36500, recombinant His6-tagged enzyme, SDS-PAGE
-
homotetramer
Ligilactobacillus salivarius LMG14476
-
4 * 36000, recombinant isozyme BSH1, SDS-PAGE
-
homotetramer
Ligilactobacillus salivarius LMG14476
-
4 * 36000, recombinant isozyme BSH2, SDS-PAGE
-
-
secondary structure, the enzyme possesses an alphabetabetaalpha tetra-lamellar tertiary structure arrangement, crystal structure analysis
tetramer
the enzyme contains an N-terminal thiol hydrolase activity site, quarternary structure, crystal structure analysis, overview
trimer
-
alpha1,beta2, bile salt hydrolase C, 1 * 42000 + 2 * 38000, SDS-PAGE
trimer
-
BSHalpha and BSHbeta are combined to form native homo- and heterotrimers
trimer
-
alpha1,beta2, bile salt hydrolase C, 1 * 42000 + 2 * 38000, SDS-PAGE
-
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. Three-dimensional structure analysis, 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. Three-dimensional structure analysis, overview
additional information
overall structures of GCA-soaked lsBSH complex. It consists of two tetramers, which are composed of chains A, B, C, D, E, F, G and H. In each lsBSH tetramer, one monomer is in complex with the substrate glycocholic acid, while the remaining monomers are in complex with the product cholic acid. Molecular dynamic simulations using lsBSH-GCA complex (PDB ID 5Y7P) as template. Structure comparisons, overview
additional information
-
overall structures of GCA-soaked lsBSH complex. It consists of two tetramers, which are composed of chains A, B, C, D, E, F, G and H. In each lsBSH tetramer, one monomer is in complex with the substrate glycocholic acid, while the remaining monomers are in complex with the product cholic acid. Molecular dynamic simulations using lsBSH-GCA complex (PDB ID 5Y7P) as template. Structure comparisons, overview
additional information
Ligilactobacillus salivarius NRRL B-30514
-
overall structures of GCA-soaked lsBSH complex. It consists of two tetramers, which are composed of chains A, B, C, D, E, F, G and H. In each lsBSH tetramer, one monomer is in complex with the substrate glycocholic acid, while the remaining monomers are in complex with the product cholic acid. Molecular dynamic simulations using lsBSH-GCA complex (PDB ID 5Y7P) as template. Structure comparisons, overview
-