Entry |
|
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 |
|
Genes |
HHW: | NCTC503_01794(cloSI_2) |
» show all
|
Reference |
|
Authors |
Mitchell WM. |
Title |
Cleavage at arginine residues by clostripain. |
Journal |
|
Reference |
|
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 |
|
Authors |
Gilles AM, Lecroisey A, Keil B |
Title |
Primary structure of alpha-clostripain light chain. |
Journal |
|
Sequence |
|
Other DBs |
ExplorEnz - The Enzyme Database: | 3.4.22.8 |
ExPASy - ENZYME nomenclature database: | 3.4.22.8 |
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