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Clostripain
Sign in to saveAlso known as Clostridiopeptidase B
Clostripain (, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a cysteine protease that cleaves proteins on the carboxyl peptide bond of arginine. It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9 (at 8 °C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.
Protein · UniProt
Clostripain
- Gene
- cloSI
- Organism
- Hathewaya histolytica (Clostridium histolyticum)
- Length
- 526 aa
- Molecular mass
- 59,733 Da
- Evidence
- 1: Evidence at protein level
Cysteine endopeptidase with strict specificity
Swiss-Prot (reviewed) · via UniProt
Wikidata facts
Show 1 more fact
- EC enzyme number
- 3.4.22.8
via Wikidata · CC0
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Article
3 sectionsContents
- See also
- References
- External links
Clostripain (, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a cysteine protease that cleaves proteins on the carboxyl peptide bond of arginine. It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9 (at 8 °C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.
==See also== Benzoyl Ethyl ester