Clostripain
| Clostripain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.8 | ||||||||
| CAS number | 9028-00-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Clostripain (EC 3.4.22.8, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine.[1][2] It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9 (at 8°C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.[3]
References
- ↑ Mitchell, W.M. (1977). "Cleavage at arginine residues by clostripain". Methods Enzymol. 47: 165–170. PMID 927173. doi:10.1016/0076-6879(77)47020-4.
- ↑ Gilles, A.-M.; Imhoff, J.-M.; Keil, B. (1979). "α-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain". J. Biol. Chem. 254: 1462–1468. PMID 762145.
- ↑ Gilles, A.-M.; Lecroisey, A.; Keil, B. (1984). "Primary structure of α-clostripain light chain". Eur. J. Biochem. 145: 469–476. PMID 6391922. doi:10.1111/j.1432-1033.1984.tb08579.x.
External links
- clostripain at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.8
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