Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Engineering

Engineering 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.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1A
-
site-directed mutagenesis, residue Cys1 is situated at the tip of strand beta1, inactive mutant, structure analysis in comparison to the wild-type enzyme
T2A
-
site-directed mutagenesis, the mutant shows reduced activity and kcat, structure analysis in comparison to the wild-type enzyme
N79W
site-directed mutagenesis, the mutant shows a drastic decrease in both expression and BSH activity and no penicillin V acylase activity compared to the wild-type enzyme
N79Y
site-directed mutagenesis, the mutant shows good expression retaining about 88% wild-type BSH activity but has no penicillin V acylase activity
Y20W/N79W
site-directed mutagenesis, the mutant shows a drastic decrease in both expression and BSH activity and no penicillin V acylase activity compared to the wild-type enzyme
biotechnology
Lactobacillus spp.
-
enzyme activity and resistance to toxicity of bile salts are unrelated, but enzyme activity is important for Lactobacillus colonization of human intestine
C2S
site-directed mutagenesis, almost inactive mutant that shows very low remaining actiivty only with taurocholic acid
E270A
F65A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
N171A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
Q257A
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
Y24F
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
E270A
N171A
-
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
-
Y24F
-
site-directed mutagenesis, the mutant shows reduced activity and altered substrate specificity compared to wild-type
-
additional information