Application | Comment | Organism |
---|---|---|
analysis | development of a fluorescence resonance energy transfer-based assay method as a rapid and reliable tool in future research for the identification and validation of potential SPase I inhibitors | Staphylococcus epidermidis |
drug development | SPase I serves as a potentially interesting target for the development of antibacterials with another mode of action | Staphylococcus epidermidis |
Cloned (Comment) | Organism |
---|---|
SPase I isozymes, expression of His-tagged Sip2 and Sip3 in Escherichia coli strain BL21(DE3), subcloning in strain TG1 | Staphylococcus epidermidis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
arylomycin A2 | a lipohexapeptide SPase I inhibitor, complete inhibition of each of the isozymes at 0.0002 mM by 0.00625 mM inhibitor | Staphylococcus epidermidis | |
additional information | inhibition by a synthetic substrate-based peptide aldehyde with IC50 of 0.009 mM and 0.013 mM for Sip2 and Sip3, respectively | Staphylococcus epidermidis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-SceD protein + H2O | Staphylococcus epidermidis | substrate of Sip2 and Sip3 | SceD + presequence of pre-SceD | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus epidermidis | - |
isozymes Sip1, Sip2, and Sip3, strain 1457 | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged Sip2 and Sip3 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Staphylococcus epidermidis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | isozyme Sip1 lacks the catalytic lysine. Development of fluorogenic peptide substrates, protease substrates containing a fluorescent donor chromophore and a quenching acceptor chromophore on either side of the enzyme cleavage site, whose fluorescence is quenched by intramolecular resonance energy transfer, FRET, between donor and a cceptor until the substrate is cleaved by the enzyme allowing continuous measurements, method development and evaluation, overview | Staphylococcus epidermidis | ? | - |
? | |
pre-SceD protein + H2O | substrate of Sip2 and Sip3 | Staphylococcus epidermidis | SceD + presequence of pre-SceD | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Sip1 | - |
Staphylococcus epidermidis |
Sip2 | - |
Staphylococcus epidermidis |
Sip3 | - |
Staphylococcus epidermidis |
Spase I | - |
Staphylococcus epidermidis |
type I signal peptidase | - |
Staphylococcus epidermidis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Staphylococcus epidermidis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Staphylococcus epidermidis |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0004 | - |
pH 8.0, 37°C, recombinant isozyme Sip2 | Staphylococcus epidermidis | arylomycin A2 | |
0.0008 | - |
pH 8.0, 37°C, recombinant isozyme Sip3 | Staphylococcus epidermidis | arylomycin A2 |
General Information | Comment | Organism |
---|---|---|
physiological function | bacterial SPases I play a key role in protein secretion as they are responsible for the cleavage of signal peptides from secreted proteins | Staphylococcus epidermidis |