Biology:Streptopain
From HandWiki
| Streptopain | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.22.10 | ||||||||
| CAS number | 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 | ||||||||
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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'
This enzyme is isolated from the bacterium, group A Streptococcus.
References
- ↑ "Streptococcal proteinase". Methods Enzymol. 19: 252–261. 1970. doi:10.1016/0076-6879(70)19019-7.
- ↑ Boyer, P.D., ed (1971). "Streptococcal proteinase". The Enzymes (3rd ed.). New York: Academic Press. pp. 609–647.
- ↑ "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. PMID 1270417.
- ↑ "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. PMID 6381494.
External links
- Streptopain at the US National Library of Medicine Medical Subject Headings (MeSH)
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