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

BRENDA support

Literature summary for 3.5.1.24 extracted from

  • Dong, Z.; Zhang, J.; Du, G.; Chen, J.; Li, H.; Lee, B.
    Periplasmic export of bile salt hydrolase in Escherichia coli by the twin-arginine signal peptides (2015), Appl. Biochem. Biotechnol., 177, 458-471 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information three twin-arginine signal peptides from twin-arginine translocation (Tat) pathway are synthesized, fused with bsh gene, inserted into expression vectors pET-20b(+) and pET-22b(+), and transformed into four different Escherichia coli hosts, respectively. Periplasmic export across the cytoplasmic membrane of bile salt hydrolase expressed in recombinant Escherichia coli by the twin-arginine signal peptides is achieved. Among the 24 recombinant bacteria obtained, Escherichia coli strain BL21(DE3) pLysS (pET-20b(+)-dmsA-bsh) shows the highest BSH activity in periplasmic fraction, which is further increased to 1.21 U/ml by orthogonal experimental design, overview. The presence of BSH in the periplasm is proven to be caused by the export rather than cell leakage. Export across the cytoplasmic membrane is initiated by the interaction of the signal peptides with the Tat export machinery, which in Escherichia coli is made up of the membrane protein TatABC Lactiplantibacillus plantarum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm bile salt hydrolase, a hydrolytic and intracellular enzyme, can fold fully in the cytoplasm Lactiplantibacillus plantarum 5737
-
additional information bile salt hydrolase from Lactobacillus plantarum BBE7 could not be efficiently exported by PelB signal peptide of the general secretory (Sec) pathway Lactiplantibacillus plantarum
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycodeoxycholic acid + H2O Lactiplantibacillus plantarum
-
deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O Lactiplantibacillus plantarum BBE7
-
deoxycholate + glycine
-
?

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum B9V401
-
-
Lactiplantibacillus plantarum BBE7 B9V401
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O
-
Lactiplantibacillus plantarum BBE7 deoxycholate + glycine
-
?

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
physiological function bile salt hydrolase catalyzes the hydrolysis of glycine- or taurine-conjugated bile acids into the free bile acids and a glycine/taurine moiety, which will increase the de novo synthesis of bile acids from cholesterol in the human host, thus lowering the host serum cholesterol level Lactiplantibacillus plantarum