Clostridiopeptidase

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Overview

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. doi:10.1016/0076-6879(77)47020-4. 
  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. doi:10.1111/j.1432-1033.1984.tb08579.x. 

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