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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Staphylococcus epidermidis | 9986 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus epidermidis | KJ571489 | isolated from fermented soy curd | - |
Staphylococcus epidermidis RM1 | KJ571489 | isolated from fermented soy curd | - |
Source Tissue | Comment | Organism | Textmining |
---|
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 | Comment | Organism |
---|---|---|
bile salt hydrolase | - |
Staphylococcus epidermidis |
BSH | - |
Staphylococcus epidermidis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Staphylococcus epidermidis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.7 | - |
- |
Staphylococcus epidermidis |
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 |