Streptopain
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.10 streptopain
Streptopain is a cysteine endopeptidase from group A Streptococcus, formed from its proenzyme by limited proteolysis and serving as the type example of peptidase family C10. It cleaves peptide bonds with hydrophobic residues at the P2, P1 and P1' positions, and contributes to streptococcal virulence by degrading host immunoglobulins, complement factors and extracellular matrix proteins. In the bacterium it supports tissue invasion and immune evasion. It features a papain-related catalytic fold with a distinctive specificity pocket adapted for hydrophobic residues.
Streptopain is a cysteine endopeptidase from group A Streptococcus, formed from its proenzyme by limited proteolysis and serving as the type example of peptidase family C10. It cleaves peptide bonds with hydrophobic residues at the P2, P1 and P1' positions, and contributes to streptococcal virulence by degrading host immunoglobulins, complement factors and extracellular matrix proteins. In the bacterium it supports tissue invasion and immune evasion. It features a papain-related catalytic fold with a distinctive specificity pocket adapted for hydrophobic residues.
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