Clostripain
| Clostripain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.8 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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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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
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<references />, or <references group="..." />External links
- clostripain at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.8
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