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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

Reaction

glycocholate
+
H2O
=
cholate
 +
glycine

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.24 choloylglycine hydrolase

Crystallization

Crystallization on EC 3.5.1.24 - choloylglycine hydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 2.3-2.5 A resolution, molecular replacement
-
enzyme in complex with substrate taurodeoxycholate and as apoenzyme, complexed enzyme by hanging drop vapour diffusion method, 18°C, mixing of 0.003 ml protein solution and 0.002 ml reservoir solution, the latter containing 2.6 M ammonium sulfate, 0.1 M sodium citrate, pH 6.0, and 1 mM taurodeoxycholate, 3 days, apoenzyme crystals by sitting drop vapour diffusion method, 18°C, mixing of 0.0015 ml protein solution with 0.001 ml reservoir solution containing 25% PEG 4000, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, 3 days, orthorhombic crystals in both cases, X-ray diffraction structure determination and analysis at 1.7 and 2.1 A resolution, respectively
purified recombinant His-tagged wild-type enzyme and mutant C2A, hanging drop vapour diffusion method, mixing of 0.002 ml of 15-20 mg/ml protein solution and reservoir solution each, the latter containing 2 M ammonium sulfate and 5% isopropyl alcohol, 2-3 days, X-ray diffraction structure determination and analysis at 2.0 and 1.5 A resolution, respectively, molecular replacement using the crystal structure of BSH from Clostridium perfringenes (PDB ID 2RLC, chain A) as a template for the search model
purified enzyme is crystallized from 16 mg/ml protein solution containing 10 mM sodium acetate, pH 5.5, 400 mM NaCl, 1 mM DTT, 1 mM EDTA, and 10% v/v glycerol by mixing with crystallization solution containing 20% w/v PEG 3350, 0.2 M KH2PO4, pH 4.8, at 20°C, crystals are soaked with substrate glycocholic acid for complex formation, X-ray diffraction structure determination and analysis at 2.10 A resolution, the complexed crystal contains enzyme with glycocholic acid and cholic acid, analysis of enzyme complex stability by molecular dynamics simulations
purified recombinant His-tagged enzyme, sitting drop vapour diffusion method, mixing 200 nl of 16.0 mg/ml protein in 10 mM sodium acetate, pH 5.5, 400 mM NaCl, 1 mM DTT, 1 mM EDTA, and 10% glycerol with 200 nl of reservoir solution containing 20% PEG 3350, and 0.2 M potassium dihydrogen phosphate, pH 4.8, and equilibration against 0.15 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using the structure of Clostridium perfringens BSH as a starting model. Two BSH molecules are packed perfectly as a dimer in one asymmetric unit