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MetaCyc Reaction: 3.4.22.59

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 3.4.22.59

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: caspase-6

Enzyme Commission Synonyms: CASP-6, apoptotic protease Mch-2, Mch2

Taxonomic Range: Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -19.062378 Inferred by computational analysis [Latendresse13]

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 3.4.22.56) and caspase-7 (EC 3.4.22.60). 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 3.4.22.61) 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.

Citations: [Takahashi96, MacLachlan02, Lee06d, Kang02, Chang00, Cowling02]

Relationship Links: BRENDA:EC:3.4.22.59 , ENZYME:EC:3.4.22.59 , IUBMB-ExplorEnz:EC:3.4.22.59


References

Chang00: Chang HY, Yang X (2000). "Proteases for cell suicide: functions and regulation of caspases." Microbiol Mol Biol Rev 64(4);821-46. PMID: 11104820

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

Kang02: Kang BH, Ko E, Kwon OK, Choi KY (2002). "The structure of procaspase 6 is similar to that of active mature caspase 6." Biochem J 364(Pt 3);629-34. PMID: 12049625

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lee06d: 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

MacLachlan02: MacLachlan TK, El-Deiry WS (2002). "Apoptotic threshold is lowered by p53 transactivation of caspase-6." Proc Natl Acad Sci U S A 99(14);9492-7. PMID: 12089322

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


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Mon Apr 27, 2015, BIOCYC14B.