| Clostripain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.8 | ||||||||
| CAS no. | 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]
See also
References
- ^ Mitchell WM (1977). Cleavage at arginine residues by clostripain. Methods in Enzymology. Vol. 47. pp. 165–70. doi: 10.1016/0076-6879(77)47020-4. PMID 927173.
- ^ Gilles AM, Imhoff JM, Keil B (March 1979). "alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain". The Journal of Biological Chemistry. 254 (5): 1462–8. PMID 762145.
- ^ Gilles AM, Lecroisey A, Keil B (December 1984). "Primary structure of alpha-clostripain light chain". European Journal of Biochemistry. 145 (3): 469–76. doi: 10.1111/j.1432-1033.1984.tb08579.x. PMID 6391922.
External links
- clostripain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.8
 | This hydrolase article is a stub. You can help Wikipedia by expanding it. |
| Clostripain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.8 | ||||||||
| CAS no. | 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]
See also
References
- ^ Mitchell WM (1977). Cleavage at arginine residues by clostripain. Methods in Enzymology. Vol. 47. pp. 165–70. doi: 10.1016/0076-6879(77)47020-4. PMID 927173.
- ^ Gilles AM, Imhoff JM, Keil B (March 1979). "alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain". The Journal of Biological Chemistry. 254 (5): 1462–8. PMID 762145.
- ^ Gilles AM, Lecroisey A, Keil B (December 1984). "Primary structure of alpha-clostripain light chain". European Journal of Biochemistry. 145 (3): 469–76. doi: 10.1111/j.1432-1033.1984.tb08579.x. PMID 6391922.
External links
- clostripain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.4.22.8
|
| This hydrolase article is a stub. You can help Wikipedia by expanding it. |