Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the activity of the truncated SpsB increases in the presence of a non-ionic detergent | Staphylococcus aureus |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type and mutant SpsBs in Escherichia coli strain BL21(DE3) | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | a truncated derivative of SpsB, which is nine amino acids longer at the N-terminus compared to the self-cleavage product, retains activity | Staphylococcus aureus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
arylomycin A2 | - |
Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | enzyme follows simple first-order kinetics, pseudo-first-order rate constant, overview | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
strain ATCC 65388, gene spsB | - |
Purification (Comment) | Organism |
---|---|
recombimant His-tagged wild-type and mutant SpsBs from Escherichia coli strain BL21(DE3) by ultracentrifugation and nickel affinity chromatography | Staphylococcus aureus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
continuous fluorometric assay for specific activity measurements | Staphylococcus aureus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | in vitro preprotein processing by SpsB, overview. SpsB undergoes self-cleavage and, although the catalytic serine is retained in the self-cleavage product, a very low residual enzymatic activity remains. Self-cleavage at one amino acid before the catalytic serine | Staphylococcus aureus | ? | - |
? | |
SpsB + H2O | self-cleavage | Staphylococcus aureus | ? | - |
? | |
Staphylococcus epidermidis SceD preprotein + H2O | specific cleavage at a single cleavage site located at the A-S bond | Staphylococcus aureus | Staphylococcus epidermidis SceD protein + SceD protein prepeptide fragment | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SPase | - |
Staphylococcus aureus |
SpsB | - |
Staphylococcus aureus |
type I signal peptidase | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.9 | - |
- |
Staphylococcus aureus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
pH-rate profile reveals apparent pKa values of 6.6 and 8.7 | Staphylococcus aureus |
5 | 12 | activity range, inactive at or below pH 4.0 and at or above pH 13.0, profile, overview | Staphylococcus aureus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.001 | - |
pH 8.0, 37°C | Staphylococcus aureus | arylomycin A2 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.059 | - |
SpsB | pH 8.0, 37°C, self-cleavage, truncated enzyme mutant | Staphylococcus aureus | |
1.85 | - |
SpsB | pH 8.0, 37°C, self-cleavage, full-length enzyme | Staphylococcus aureus |