3.4.22.61: caspase-8
This is an abbreviated version!
For detailed information about caspase-8, go to the full flat file.
Word Map on EC 3.4.22.61
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3.4.22.61
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caspase-9
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bcl-2
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necrosis
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extrinsic
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bid
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tnf
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trail
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apoptosis-inducing
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parp
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pro-apoptotic
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anti-apoptotic
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leukemia
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fas-associated
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trail-induced
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tunel
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fasl
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annexin
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death-inducing
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factor-related
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caspase-dependent
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c-flips
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apoptosis-related
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xiap
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fas-mediated
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flip
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receptor-mediated
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nf-kappab
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polyadp-ribose
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jurkat
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necroptosis
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anti-fas
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deoxynucleotidyl
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adp-ribose
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pan-caspase
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z-vad-fmk
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tnf-related
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deltapsim
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mitochondria-dependent
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fas-induced
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survivin
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receptor-induced
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tnf-induced
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receptor-interacting
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mlkl
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mitochondria-mediated
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ripk1
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sub-g1
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apaf-1
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executioner
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drug development
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procaspase-3
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medicine
- 3.4.22.61
- caspase-9
- bcl-2
- necrosis
-
extrinsic
- bid
- tnf
-
trail
-
apoptosis-inducing
- parp
-
pro-apoptotic
-
anti-apoptotic
- leukemia
-
fas-associated
-
trail-induced
-
tunel
- fasl
-
annexin
-
death-inducing
-
factor-related
-
caspase-dependent
- c-flips
-
apoptosis-related
- xiap
-
fas-mediated
- flip
-
receptor-mediated
- nf-kappab
-
polyadp-ribose
-
jurkat
-
necroptosis
-
anti-fas
-
deoxynucleotidyl
- adp-ribose
-
pan-caspase
- z-vad-fmk
-
tnf-related
-
deltapsim
-
mitochondria-dependent
-
fas-induced
- survivin
-
receptor-induced
-
tnf-induced
-
receptor-interacting
- mlkl
-
mitochondria-mediated
- ripk1
-
sub-g1
- apaf-1
-
executioner
- drug development
- procaspase-3
- medicine
Reaction
strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-/-(Gly/Ser/Ala) =
Synonyms
apoptotic cysteine protease, apoptotic protease Mch-5, C14.004, CAP4, Casp8, caspase 8, caspase-8, cysteine aspartic acid protease 8, cysteine aspartic acid-specific protease, cysteine protease caspase-8, FADD-homologous ICE/CED-3-like protease, FADD-like ICE, FLICE, FLICE/MACH, ICE-like apoptotic protease 5, MACH, Mch5, More, MORT1-associated CED-3 homolog
ECTree
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Subunits
Subunits on EC 3.4.22.61 - caspase-8
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dimer
monomer
tetramer
additional information
dimer
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caspase-8 is activated by homodimerization, which also leads to autoproteolytic processing of the enzyme into multiple smaller species
dimer
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caspase proenzymes are induced to dimerize, and this dimerization leads to enzyme activation. In the case of caspase 8, dimerization is followed by interdomain cleavage events, first between the large and small subunits and subsequently between the large subunit and the prodomain. These cleavage events stabilize the caspase 8 homodimer and remove the prodomain, leading to formation of a fully active enzyme composed of two large and two small subunits
dimer
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dramatical conformation changes of the linker region undergo in order to bring cleavage sites, Asp374 and Asp384, to the vicinity of catalytic residue Cys283 from other protomer during dimerization of procaspase-8
dimer
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processed active enzyme, during dimerization, a loop containing a small helix translocates from the active site, mechanism, overview
dimer
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caspase-8 activation involves dimerization and subsequent interdomain autoprocessing of caspase-8 zymogens, overview. The catalytic domain of caspase-8 is crucial for its activity in the context of activation by homodimerization
dimer
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processed active enzyme, during dimerization, a loop containing a small helix translocates from the active site
monomer
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inactive zymogen, the monomeric form of caspase-8 has a typical caspase fold, consisting of a six-stranded beta sheet formed by five parallel and one anti-parallel beta strand, overview
monomer
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inactive zymogen, the monomeric form of caspase-8 has a typical caspase fold, consisting of a six-stranded beta sheet formed by five parallel and one anti-parallel beta strand, overview
tetramer
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dimer of dimers, separation of the large and small subunit after intra-dimeric cleavage in the linker region between the large and small subunit renders the linker region between the large subunit and the prodomain of caspase-8 susceptible for the further inter-dimeric cleavage. Under apoptotic stimuli, caspase-8 undergoes catalytic autocleavage to generate the proapoptotic mature tetramer to induce apoptosis
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LRRK2, FADD, and caspase-8 are components of a multiprotein complex
additional information
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caspases can only be active as dimers, since neither the active site dyad nor the substrate pocket can be formed in the monomeric form, structure analysis and comparison of caspase-8 monomeric zymogen and the substrate-bound, fully-processed, caspase-8 dimer, overview
additional information
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the C- and N-terminal end are necessary to stabilize dimer of caspase-8 and induce separation of the large and small subunit
additional information
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caspases can only be active as dimers, since neither the active site dyad nor the substrate pocket can be formed in the monomeric form, structure analysis and comparison of caspase-8 monomeric zymogen and the substrate-bound, fully-processed, caspase-8 dimer, overview