EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.22.10 | more |
the enzyme performs autolytic activity and also cleaves the inactive mutant C192S |
Streptococcus pyogenes |
? |
- |
? |
3.4.22.10 | more |
the enzyme performs autolytic activity and also cleaves the inactive mutant C192S |
Streptococcus pyogenes A-20 |
? |
- |
? |
3.4.22.10 | more |
the enzyme performs autolytic processing to the mature protein, interaction overview |
Streptococcus pyogenes |
? |
- |
? |
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 |
Streptococcus pyogenes |
? |
- |
? |
3.4.22.10 | proSPE B C47S + H2O |
the proSPE B C47S mutant is also be used as the substrate for activity assay because it does not exhibit any enzyme activity and exists as a 42 kDa zymogen |
Streptococcus pyogenes |
? |
- |
? |
3.4.22.10 | more |
the three-dimensional structure and backbone dynamics of the 28 kDa mature SPE B (mSPE B) is determined: Interactions between the C-terminal loop and the active site residues in mSPE B are observed. The structural differences between mSPE B and zymogen proSPE B are the conformation of the C-terminal loop and the orientation of the catalytic His-195 residue. Dynamics analysis of mSPEB and the mSPEB/inhibitor complexes show that the catalytic and C-terminal loops are the most flexible regions, suggesting that the flexible C-terminal loop of SPE B may play an important role in controlling the substrate binding, resulting in its broad substrate specificity |
Streptococcus pyogenes |
? |
- |
? |
3.4.22.10 | more |
thus, although IgG might by a substrate for SpeB under certain environmental conditions, it seems unlikely that SpeB is part of the first line of defense against specific antibodies. Even though SpeB might not be directly involved in the attenuation of the adaptive immune response, its proteolytic activity towards streptococcal surface proteins, including IgG-binding proteins and the streptococcal C5a peptidase, could certainly be important for the modulation of the complement system |
Streptococcus pyogenes |
? |
- |
? |