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
| Streptopain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.10 | ||||||||
| CAS no. | 9025-51-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 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
editReferences
edit- ^ Elliott SD, Liu TY (1970). Streptococcal proteinase. Methods Enzymol. Vol. 19. pp. 252–261. doi:10.1016/0076-6879(70)19019-7. ISBN 978-0-12-181881-4.
- ^ Liu TY, Elliott SD (1971). "Streptococcal proteinase". In Boyer, P.D. (ed.). The Enzymes (3rd ed.). New York: Academic Press. pp. 609–647.
- ^ Tai JY, Kortt AA, Liu TY, Elliott SD (April 1976). "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. doi:10.1016/S0021-9258(17)33640-2. PMID 1270417.
- ^ Lo SS, Fraser BA, Liu TY (September 1984). "The mixed disulfide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis". The Journal of Biological Chemistry. 259 (17): 11041–5. doi:10.1016/S0021-9258(18)90619-8. PMID 6381494.
External links
edit- Streptopain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
