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Literature summary for 3.5.1.24 extracted from

  • Mukherji, R.; Prabhune, A.
    Possible correlation between bile salt hydrolysis and AHL deamidation Staphylococcus epidermidis RM1, a potent quorum quencher and bile salt hydrolase producer (2015), Appl. Biochem. Biotechnol., 176, 140-150 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, two different genetic elements corresponding to each of the enzymatic activity are successfully amplified from the genomic DNA of the isolate, phylogenetic analysis Staphylococcus epidermidis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Staphylococcus epidermidis 9986
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycocholic acid + H2O Staphylococcus epidermidis
-
cholate + glycine
-
?
glycocholic acid + H2O Staphylococcus epidermidis RM1
-
cholate + glycine
-
?
glycodeoxycholic acid + H2O Staphylococcus epidermidis
-
deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O Staphylococcus epidermidis RM1
-
deoxycholate + glycine
-
?
additional information Staphylococcus epidermidis determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97) ?
-
?
additional information Staphylococcus epidermidis RM1 determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97) ?
-
?
taurocholic acid + H2O Staphylococcus epidermidis
-
cholate + taurine
-
?
taurocholic acid + H2O Staphylococcus epidermidis RM1
-
cholate + taurine
-
?
taurodeoxycholic acid + H2O Staphylococcus epidermidis
-
deoxycholate + taurine
-
?
taurodeoxycholic acid + H2O Staphylococcus epidermidis RM1
-
deoxycholate + taurine
-
?

Organism

Organism UniProt Comment Textmining
Staphylococcus epidermidis KJ571489 isolated from fermented soy curd
-
Staphylococcus epidermidis RM1 KJ571489 isolated from fermented soy curd
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycocholic acid + H2O
-
Staphylococcus epidermidis cholate + glycine
-
?
glycocholic acid + H2O
-
Staphylococcus epidermidis RM1 cholate + glycine
-
?
glycodeoxycholic acid + H2O
-
Staphylococcus epidermidis deoxycholate + glycine
-
?
glycodeoxycholic acid + H2O
-
Staphylococcus epidermidis RM1 deoxycholate + glycine
-
?
additional information determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97) Staphylococcus epidermidis ?
-
?
additional information determination of whole cell AHL acylase activity using a coupled assay with violacin producing Chromobacterium violaceum CV026. The amount of violacein synthesized by the biosensor strain CV026 is proportional to the amount of AHL remaining in the reaction mixture after incubation period. The enzymatic degradation of quorum sensing (QS) signal molecules is due to an AHL lactonase (EC 3.1.1.81) or AHL acylase (EC 3.5.1.97) Staphylococcus epidermidis RM1 ?
-
?
taurocholic acid + H2O
-
Staphylococcus epidermidis cholate + taurine
-
?
taurocholic acid + H2O
-
Staphylococcus epidermidis RM1 cholate + taurine
-
?
taurodeoxycholic acid + H2O
-
Staphylococcus epidermidis deoxycholate + taurine
-
?
taurodeoxycholic acid + H2O
-
Staphylococcus epidermidis RM1 deoxycholate + taurine
-
?

Synonyms

Synonyms Comment Organism
bile salt hydrolase
-
Staphylococcus epidermidis
BSH
-
Staphylococcus epidermidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Staphylococcus epidermidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
-
Staphylococcus epidermidis

General Information

General Information Comment Organism
metabolism Staphylococcus epidermidis strain RM1 possess both potent bile salt hydrolase (BSH) and N-acyl homoserine lactone (AHL, EC 3.1.1.81) cleavage activity, the single enzyme, that is not responsible for both the activities, is identified as bile salt hydrolase, two different genetic elements correspond to each of the enzymatic activity Staphylococcus epidermidis