Histolysin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.22.35 | ||||||||
CAS no. | 92228-52-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Histolysin (EC 3.4.22.35, histolysin, Entamoeba histolytica cysteine proteinase, amebapain, Entamoeba histolytica cysteine protease, Entamoeba histolytica neutral thiol proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg- in small molecule substrates including Z-Arg-Arg-!NHMec
This enzyme is present in the protozoan, Entamoeba histolytica.
References
- Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental Parasitology. 59 (3): 328–36. doi:10.1016/0014-4894(85)90088-8. PMID 2860002.
- Luaces AL, Barrett AJ (March 1988). "Affinity purification and biochemical characterization of histolysin, the major cysteine proteinase of Entamoeba histolytica". The Biochemical Journal. 250 (3): 903–9. doi:10.1042/bj2500903. PMC 1148941. PMID 2898937.
External links
- Histolysain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Proteases: cysteine proteases (EC 3.4.22) | |
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Caspase | |
Fruit-derived | |
Calpain | |
Cathepsin | |
Other |
Enzymes | |
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Regulation | |
Classification | |
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