EC Number |
Natural Substrates |
---|
3.4.22.10 | immunoglobulin G + H2O |
cleavage site is LLG-G in gamma-chain |
3.4.22.10 | immunoglobulin M + H2O |
cleavage sites are the heavy chains |
3.4.22.10 | Laminin + H2O |
- |
3.4.22.10 | M protein + H2O |
- |
3.4.22.10 | more |
the enzyme activates a 66000 Da matrix metalloprotease produced by human endothelial cells, a process that may contribute to endothelial cell damage, tissue destruction, and hemodynamic derangement |
3.4.22.10 | more |
by removal of M1 protein and protein H from the streptococcal surface the enzyme regulates the bacterial cell-cell interactions, and perhaps also interactions with epithelial cells. Through expression of streptopain the enzyme can modify the composition of the surface proteins in response to environmental conditions. Such a mechanism will facilitate the adaption of the bacterium to its host |
3.4.22.10 | more |
the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells |
3.4.22.10 | more |
the expression of the enzyme contributes to soft tissue pathology, including necrosis, and is required for efficient systemic dissemination of the organism from the initial site of skin inoculation |
3.4.22.10 | more |
release of biological active kinins from kininogens present in human plasma |
3.4.22.10 | more |
the enzyme is an important virulence factor |