| IED ID | IndEnz0002007666 |
| Enzyme Type ID | protease007666 |
| Protein Name |
Histolysain EC 3.4.22.35 Cysteine proteinase 2 Histolysin |
| Gene Name | CPP2 EHI_033710 |
| Organism | Entamoeba histolytica |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Archamoebae Mastigamoebida Entamoebidae Entamoeba Entamoeba histolytica |
| Enzyme Sequence | MFAFICLLAIASAIDFNTWASKNNKHFTAIEKLRRRAIFNMNAKFVDSFNKIGSFKLSVDGPFAAMTNEEYRTLLKSKRTTEENGQVKYLNIQAPESVDWRKEGKVTPIRDQAQCGSCYTFGSLAALEGRLLIEKGGDANTLDLSEEHMVQCTRDNGNNGCNGGLGSNVYDYIIEHGVAKESDYPYTGSDSTCKTNVKSFAKITGYTKVPRNNEAELKAALSQGLVDVSIDASSAKFQLYKSGAYTDTKCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGDKGYINMVIEGNTCGVATDPLYPTGVQYL |
| Enzyme Length | 315 |
| Uniprot Accession Number | Q01958 |
| Absorption | |
| Active Site | ACT_SITE 118; /evidence=ECO:0000250; ACT_SITE 259; /evidence=ECO:0000250; ACT_SITE 279; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by leupeptin and such inhibitors of cysteine proteinases as L-transepoxysuccinyl-L-leucylamido-(4-guanidino)butane, peptidyldiazomethanes, iodoacetic acid and chicken cystatin. {ECO:0000269|PubMed:2898937}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec.; EC=3.4.22.35; Evidence={ECO:0000269|PubMed:2898937}; |
| DNA Binding | |
| EC Number | 3.4.22.35 |
| Enzyme Function | FUNCTION: Involved in the destruction of human tissue by E.histolytica. Can abolish adhesion and degrade matrix proteins such as collagen, laminin and fibronectin. May play an important role in pathogenicity. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 with azocasein as substrate, 7 with Z-Phe-Cit-NHMec, and 9.5 with Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec as substrate. {ECO:0000269|PubMed:2898937}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..13; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,688 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for Z-Arg-Arg-NHMec {ECO:0000269|PubMed:2898937}; KM=31.8 uM for Z-Phe-Arg-NHMec {ECO:0000269|PubMed:2898937}; Note=kcat is 130 sec(-1) with Z-Arg-Arg-NHMec as substrate and 0.4 sec(-1) with Z-Phe-Arg-NHMec as substrate.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.35; |