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Literature summary for 3.5.1.24 extracted from

  • Oeztuerk, M.; Oenal, C.
    Asparagine 79 is an important amino acid for catalytic activity and substrate specificity of bile salt hydrolase (BSH) (2019), Mol. Biol. Rep., 46, 4361-4368 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene bsh, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strains BLR(DE3) and XL-1 Blue Lactiplantibacillus plantarum

Protein Variants

Protein Variants Comment Organism
N79V site-directed mutagenesis, the V79 mutation results in a stable enzyme, but reduces the catalytic activity and alters the substrate specificity of the enzyme Lactiplantibacillus plantarum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycochenodeoxycholic acid + H2O Lactiplantibacillus plantarum
-
chenodeoxycholate + glycine
-
?
glycochenodeoxycholic acid + H2O Lactiplantibacillus plantarum B14
-
chenodeoxycholate + glycine
-
?
glycocholic acid + H2O Lactiplantibacillus plantarum
-
cholate + glycine
-
?
glycocholic acid + H2O Lactiplantibacillus plantarum B14
-
cholate + glycine
-
?
glycodeoxycholic acid + H2O Lactiplantibacillus plantarum
-
deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O Lactiplantibacillus plantarum B14
-
deoxycholate + glycine
-
?
taurochenodeoxycholic acid + H2O Lactiplantibacillus plantarum
-
chenodeoxycholate + taurine
-
?
taurochenodeoxycholic acid + H2O Lactiplantibacillus plantarum B14
-
chenodeoxycholate + taurine
-
?
taurocholic acid + H2O Lactiplantibacillus plantarum
-
cholate + taurine
-
?
taurodeoxycholic acid + H2O Lactiplantibacillus plantarum
-
deoxycholate + taurine
-
?
taurodeoxycholic acid + H2O Lactiplantibacillus plantarum B14
-
deoxycholate + taurine
-
?

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum
-
-
-
Lactiplantibacillus plantarum B14
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycochenodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum chenodeoxycholate + glycine
-
?
glycochenodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum B14 chenodeoxycholate + glycine
-
?
glycocholic acid + H2O
-
Lactiplantibacillus plantarum cholate + glycine
-
?
glycocholic acid + H2O
-
Lactiplantibacillus plantarum B14 cholate + glycine
-
?
glycodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum B14 deoxycholate + glycine
-
?
taurochenodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum chenodeoxycholate + taurine
-
?
taurochenodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum B14 chenodeoxycholate + taurine
-
?
taurocholic acid + H2O
-
Lactiplantibacillus plantarum cholate + taurine
-
?
taurodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum deoxycholate + taurine
-
?
taurodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum B14 deoxycholate + taurine
-
?

Synonyms

Synonyms Comment Organism
bile salt hydrolase
-
Lactiplantibacillus plantarum
BSH
-
Lactiplantibacillus plantarum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Lactiplantibacillus plantarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Lactiplantibacillus plantarum

General Information

General Information Comment Organism
evolution microbial bile salt hydrolases (BSHs), a member of cholylglycine hydrolase (CGH) family. BSH is evolutionarily related to penicillin V acylase (PVA) which hydrolyses a penicillin V and is also a member of CGH family. five of the six amino acids, C2, R16, D19, N170, and R223, supposed to be responsible for catalytic activity of BSH enzyme, are strictly conserved in all CGH family members, N79 is partially conserved in the family Lactiplantibacillus plantarum
additional information residue N79 might be important for substrate binding and catalytic turnover of BSH. Structure homology modelling using the crystal structure of BSH from Enterococcus faecalis (PDB ID 4wl3.1.B) as template. The homology modelling and 3D structure of BSH indicates that N79 residue is located near the catalytic center and within the cavity of substrates accessory to the enzyme Lactiplantibacillus plantarum
physiological function microbial bile salt hydrolases (BSHs) catalyze the hydrolysis of glycine and taurine-linked bile salts in the small intestine of humans Lactiplantibacillus plantarum