KEGG   ENZYME: 3.4.22.8
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
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
CPECPE0846
CPFCPF_0840(cloSI)
CPRCPR_0833(cloSI)
CBOCBO1920(closI)
CBACLB_1857(cloSI)
CBHCLC_1864(cloSI)
CBYCLM_2137(cloSI)
CBLCLK_1375(cloSI)
CBBCLD_2707(cloSI)
CBICLJ_B2122(cloSI)
CBNCbC4_5035
CBFCLI_1984(cloSI)
CBMCBF_1967(cloSI)
CBJH04402_01934
CLDCLSPO_c19150(cloSI)
CGASJ1C67_07395(cloSI)
HHWNCTC503_01794(cloSI_2)
VPYHZI73_17075(cloSI)
TRIDYE50_06990
 » show all
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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