Clostripain

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
Search PMC articles PubMed articles NCBI proteins

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

• Benzoyl
• Ethyl ester

References

1. 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.
2. 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.
3. 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