KEGG   ENZYME: 3.4.22.8Help
Entry
EC 3.4.22.8                 Enzyme                                 

Name
clostripain;
clostridiopeptidase B;
clostridium histolyticum proteinase B;
alpha-clostridipain;
clostridiopeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage: Arg!, including Arg!Pro, but not Lys-
Comment
From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11.
History
EC 3.4.22.8 created 1961 as EC 3.4.4.20, transferred 1972 to EC 3.4.22.8
Orthology
K08587  clostripain
Genes
CPE: CPE0846
CPF: CPF_0840(cloSI)
CPR: CPR_0833(cloSI)
CNO: NT01CX_1195
CBO: CBO1920(closI)
CBA: CLB_1857(cloSI)
CBH: CLC_1864(cloSI)
CBY: CLM_2137(cloSI)
CBL: CLK_1375(cloSI)
CBB: CLD_2707(cloSI)
CBI: CLJ_B2122(cloSI)
CBN: CbC4_5035
CBF: CLI_1984(cloSI)
CBM: CBF_1967(cloSI)
CLD: CLSPO_c19150(cloSI)
 » show all
Taxonomy
Reference
1  [PMID:927173]
  Authors
Mitchell WM.
  Title
Cleavage at arginine residues by clostripain.
  Journal
Methods Enzymol 47:165-70 (1977)
DOI:10.1016/0076-6879(77)47020-4
Reference
2  [PMID:762145]
  Authors
Gilles AM, Imhoff JM, Keil B.
  Title
alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain.
  Journal
J Biol Chem 254:1462-8 (1979)
Reference
3  [PMID:6391922]
  Authors
Gilles AM, Lecroisey A, Keil B.
  Title
Primary structure of alpha-clostripain light chain.
  Journal
Eur J Biochem 145:469-76 (1984)
DOI:10.1111/j.1432-1033.1984.tb08579.x
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.8
IUBMB Enzyme Nomenclature: 3.4.22.8
ExPASy - ENZYME nomenclature database: 3.4.22.8
BRENDA, the Enzyme Database: 3.4.22.8
CAS: 9028-00-6

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