|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: caspase-6
Enzyme Commission Synonyms: CASP-6, apoptotic protease Mch-2, Mch2
Enzyme Commission Summary:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|
Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 22.214.171.124) and caspase-7 (EC 126.96.36.199). These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype. Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 188.8.131.52) and leads to cytochrome c release from the mitochondria; the release of cytochrome c, which is an essential component of the intrinsic apoptosis pathway. Can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragementation in the final phases of apoptosis. Belongs to peptidase family C14.
Cowling02: Cowling V, Downward J (2002). "Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain." Cell Death Differ 9(10);1046-56. PMID: 12232792
Lee06e: Lee SC, Chan J, Clement MV, Pervaiz S (2006). "Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop." Proteomics 6(8);2386-94. PMID: 16518869
Takahashi96: Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, Moir RD, Goldman RD, Poirier GG, Kaufmann SH, Earnshaw WC (1996). "Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis." Proc Natl Acad Sci U S A 93(16);8395-400. PMID: 8710882
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493