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Literature summary for 3.4.21.89 extracted from

  • Rao, S.; Bockstael, K.; Nath, S.; Engelborghs, Y.; Anne, J.; Geukens, N.
    Enzymatic investigation of the Staphylococcus aureus type I signal peptidase SpsB - implications for the search for novel antibiotics (2009), FEBS J., 276, 3222-3234.
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant SpsBs in Escherichia coli strain BL21(DE3) Staphylococcus aureus

Protein Variants

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

Inhibitors Comment Organism Structure
arylomycin A2
-
Staphylococcus aureus

KM Value [mM]

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

Organism UniProt Comment Textmining
Staphylococcus aureus
-
strain ATCC 65388, gene spsB
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
SPase
-
Staphylococcus aureus
SpsB
-
Staphylococcus aureus
type I signal peptidase
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
-
Staphylococcus aureus

pH Range

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 IC50 Value Maximum Comment Organism Inhibitor Structure
0.001
-
pH 8.0, 37°C Staphylococcus aureus arylomycin A2

kcat/KM [mM/s]

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