Biology:Streptopain

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Streptopain, also known as streptococcal pyrogenic exotoxin B (SpeB) is a streptococcal cysteine protease.[1][2][3][4] Other names include Streptococcus peptidase A, Streptococcus protease, and streptococcal cysteine proteinase. Streptopain catalyses the following chemical reaction

Preferential cleavage with hydrophobic residues at P2, P1 and P1'

It is isolated from the group A bacterium Streptococcus pyogenes and acts as a virulence factor.

See also

References

  1. "Streptococcal proteinase". Proteolytic Enzymes. Methods Enzymol.. 19. 1970. pp. 252–261. doi:10.1016/0076-6879(70)19019-7. ISBN 978-0-12-181881-4. 
  2. Boyer, P.D., ed (1971). "Streptococcal proteinase". The Enzymes (3rd ed.). New York: Academic Press. pp. 609–647. 
  3. "Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain". The Journal of Biological Chemistry 251 (7): 1955–9. April 1976. doi:10.1016/S0021-9258(17)33640-2. PMID 1270417. 
  4. "The mixed disulfide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis". The Journal of Biological Chemistry 259 (17): 11041–5. September 1984. doi:10.1016/S0021-9258(18)90619-8. PMID 6381494.