Coccolysin
From Wikipedia the free encyclopedia
| 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, S. diacetilactis and S. faecalis.
References[edit]
- ^ Desmazeaud MJ (1974). "[General properties and specificity of action of a neutral intracellular endopeptidase from Streptococcus thermophilus]". Biochimie. 56 (9): 1173–1181. doi:10.1016/s0300-9084(74)80008-8. PMID 4451671.
- ^ Desmazeaud MJ, Zevaco C (1976). "General properties and substrate specificity of an intracellular neutral protease from Streptococcus diaceti lactis" (PDF). Annales de Biologie Animale, Biochimie, et Biophysique. 16 (6): 851–868. doi:10.1051/rnd:19760608.
- ^ Smith RA, Green J, Kopper PH (July 1980). "The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis". Archives of Biochemistry and Biophysics. 202 (2): 629–638. doi:10.1016/0003-9861(80)90471-3. PMID 6779709.
- ^ Mäkinen PL, Clewell DB, An F, Mäkinen KK (February 1989). "Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10)". The Journal of Biological Chemistry. 264 (6): 3325–3334. doi:10.1016/S0021-9258(18)94069-X. PMID 2536744.
External links[edit]
- Coccolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
