| Histolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
Histolysin ( EC 3.4.22.35, histolysin, Entamoeba histolytica cysteine proteinase, amebapain, Entamoeba histolytica cysteine protease, Entamoeba histolytica neutral thiol proteinase) is an enzyme. [1] [2] 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.
- ^ 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.
- Histolysain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Histolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
Histolysin ( EC 3.4.22.35, histolysin, Entamoeba histolytica cysteine proteinase, amebapain, Entamoeba histolytica cysteine protease, Entamoeba histolytica neutral thiol proteinase) is an enzyme. [1] [2] 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.
- ^ 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.
- Histolysain at the U.S. National Library of Medicine Medical Subject Headings (MeSH)