Coccolysin
| Coccolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.30 | ||||||||
| CAS no. | 156859-08-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Coccolysin (EC 3.4.24.30, Streptococcus thermophilus intracellular proteinase, EM 19000) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Preferential cleavage: -Leu, -Phe, -Tyr, -Ala
This endopeptidase is present in S. thermophilus and S. diacetilactis and S. faecalis.
References
- ^ Desmazeaud, M.J. (1974). "Propriétés générales et spécificité d’action d’une endopeptidase neutre intracellulaire de Streptococcus thermophilus". Biochimie. 56: 1173–1181. doi:10.1016/s0300-9084(74)80008-8. PMID 4451671.
- ^ Desmazeaud, M.J.; Zevaco, C. (1976). "General properties and substrate specificity of an intracellular neutral protease from Streptococcus diacetilactis'" (PDF). Ann. Biol. Anim. Biochem. Biophys. 16: 851–868. doi:10.1051/rnd:19760608.
- ^ Smith, R.A.G.; Green, J.; Kopper, P.H. (1980). "The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis". Arch. Biochem. Biophys. 202: 629–638. doi:10.1016/0003-9861(80)90471-3. PMID 6779709.
- ^ Mäkinen PL, Clewell DB, An F, Mäkinen KK (1989). "Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10)". J. Biol. Chem. 264: 3325–3334. PMID 2536744.
External links
- Coccolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
