Streptopain
Streptopain (EC 3.4.22.10, Streptococcus peptidase A, streptococcal cysteine proteinase, Streptococcus protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Preferential cleavage with hydrophobic residues at P2, P1 and P1'
| 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 | ||||||||
| |||||||||
This enzyme is isolated from the bacterium, group A Streptococcus.
References
- Elliott SD, Liu TY (1970). "Streptococcal proteinase". Methods Enzymol. 19: 252–261. doi:10.1016/0076-6879(70)19019-7.
- 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. 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. PMID 6381494.
External links
- Streptopain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.