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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.
In the Vinony graph
Within Vinony's link graph, Clostripain is referenced by 101 other articles, and connects out to PubMed, protein and International Standard Book Number.
Vinony files it under EC 3.4.22 and Post-translational modification.
Its subject is documented across 7 Wikipedia language editions.
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
- Instance of
- protein
- Part of
- cysteine protease
Show 1 more fact
- EC enzyme number
- 3.4.22.8
via Wikidata · CC0
~1 min read
Encyclopedic overview
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
Excerpted from Wikipedia’s “Clostripain” article, available under the CC BY-SA 4.0 licence.