| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.22.- |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Caspase-3 can activate procaspase-2 (EC 3.4.22.55)."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "These caspases are responsible for the proteolysis of the majority of cellular polypeptides, [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family C14."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "This is not the case for caspase-7."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2000/01/rdf-schema#comment | "Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60)."xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2004/02/skos/core#prefLabel | "caspase-3"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11104820 |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11123933 |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16781734 |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8665848 |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9261102 |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2004/02/skos/core#altLabel | "CPP32"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2004/02/skos/core#altLabel | "CASP-3"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2004/02/skos/core#altLabel | "apopain"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://www.w3.org/2004/02/skos/core#altLabel | "yama protein"xsd:string |
| http://purl.uniprot.org/enzyme/3.4.22.56 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/3.4.22.56#SIPA7FA0DA69CCB7935 |