Clostripain
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.8 clostripain
Clostripain is a cysteine endopeptidase from the bacterium Clostridium histolyticum, requiring Ca2+ and inhibited by EDTA, and the type example of peptidase family C11. It preferentially cleaves Arg-/-, including Arg-/-Pro, but does not cleave Lys-. In the bacterium it contributes to extracellular protein degradation and tissue invasion. In the laboratory it is used as a specific Arg-C protease for peptide mapping. It features a cysteine-protease fold activated by Ca2+ and with a strict Arg specificity pocket.
Clostripain is a cysteine endopeptidase from the bacterium Clostridium histolyticum, requiring Ca2+ and inhibited by EDTA, and the type example of peptidase family C11. It preferentially cleaves Arg-/-, including Arg-/-Pro, but does not cleave Lys-. In the bacterium it contributes to extracellular protein degradation and tissue invasion. In the laboratory it is used as a specific Arg-C protease for peptide mapping. It features a cysteine-protease fold activated by Ca2+ and with a strict Arg specificity pocket.
References:
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