Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Jusko, M.; Potempa, J.; Kantyka, T.; Bielecka, E.; Miller, H.; Kalinska, M.; Dubin, G.; Garred, P.; Shaw, L.; Blom, A.
    Staphylococcal proteases aid in evasion of the human complement system (2014), J. Innate Immun., 6, 31-46.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.29 extracellular
-
 Staphylococcus aureus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.29 Ca2+ required, metalloproteinase Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.29 Staphylococcus aureus
-
-
-
3.4.24.29 Staphylococcus aureus V8-BC10
-
-
-

Synonyms

EC Number Synonyms Comment Organism
3.4.24.29 Aur
-
 Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.29 37
-
 assay at Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.29 7.4
-
 assay at Staphylococcus aureus

General Information

EC Number General Information Comment Organism
3.4.24.29 metabolism four major extracellular proteases of Staphylococcus aureus are potent complement inhibitors: cysteine proteases staphopain A and staphopain B, the serine protease V8, and the metalloproteinase aureolysin cause a drastic decrease in the haemolytic activity of serum, whereas two serine-protease like enzymes, SplD and SplE, have no effect. The four enzymes inhibit all pathways of complement due to the efficient degradation of several crucial components Staphylococcus aureus
3.4.24.29 physiological function the enzyme acts as host complement inhibitor Staphylococcus aureus