| EC |
3.4.22.8 |
| Accepted name: |
clostripain |
| Reaction: |
Preferential cleavage: Arg┼, including Arg┼Pro, but not Lys- |
| Other name(s): |
clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase |
| Comments: |
From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9028-00-6 |
| References: |
| 1. |
Mitchell, W.M. Cleavage at arginine residues by clostripain. Methods Enzymol. 47 (1977) 165–170. [DOI] [PMID: 927173] |
| 2. |
Gilles, A.-M., Imhoff, J.-M. and Keil, B. α-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain. J. Biol. Chem. 254 (1979) 1462–1468. [PMID: 762145] |
| 3. |
Gilles, A.-M., Lecroisey, A. and Keil, B. Primary structure of α-clostripain light chain. Eur. J. Biochem. 145 (1984) 469–476. [DOI] [PMID: 6391922] |
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| [EC 3.4.22.8 created 1961 as EC 3.4.4.20, transferred 1972 to EC 3.4.22.8] |
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