Clostripain

From Wikipedia, the free encyclopedia
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][3] It was isolated from Clostridium histolyticum. The optimum pH of the enzyme is 7.4~7.8.

References

  1. ↑ Mitchell, W.M. (1977). "Cleavage at arginine residues by clostripain". Methods Enzymol. 47: 165–170. PMID 927173. 
  2. ↑ Gilles, A.-M., Imhoff, J.-M. and 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. 
  3. ↑ Gilles, A.-M., Lecroisey, A. and Keil, B. (1984). "Primary structure of α-clostripain light chain". Eur. J. Biochem. 145: 469–476. PMID 6391922. 

External links

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