3.4.22.62: caspase-9
This is an abbreviated version!
For detailed information about caspase-9, go to the full flat file.
Word Map on EC 3.4.22.62
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3.4.22.62
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caspase-3
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bcl-2
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parp
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anti-apoptotic
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pro-apoptotic
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tunel
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necrosis
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apoptosis-related
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caspase-dependent
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apoptosis-inducing
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jnk
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apaf-1
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annexin
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extrinsic
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cyclin
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leukemia
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bid
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neuroprotective
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depolarization
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polyadp-ribose
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survivin
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hoechst
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z-vad-fmk
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antiproliferative
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adp-ribose
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xiap
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iodide
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deoxynucleotidyl
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mitochondria-dependent
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mitochondria-mediated
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cisplatin
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dutp
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fadd
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procaspase-3
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caspase-mediated
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pan-caspase
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fas-mediated
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trail
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fas-associated
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trail-induced
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bcl-2-associated
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apoptogenic
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pharmacology
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cdc25c
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puma
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transferase-mediated
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executioner
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factor-related
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deltapsim
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medicine
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tunel-positive
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sub-g1
- 3.4.22.62
- caspase-3
- bcl-2
- parp
-
anti-apoptotic
-
pro-apoptotic
-
tunel
- necrosis
-
apoptosis-related
-
caspase-dependent
-
apoptosis-inducing
- jnk
- apaf-1
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annexin
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extrinsic
- cyclin
- leukemia
- bid
-
neuroprotective
-
depolarization
-
polyadp-ribose
- survivin
-
hoechst
- z-vad-fmk
-
antiproliferative
- adp-ribose
- xiap
- iodide
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deoxynucleotidyl
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mitochondria-dependent
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mitochondria-mediated
- cisplatin
- dutp
- fadd
- procaspase-3
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caspase-mediated
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pan-caspase
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fas-mediated
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trail
-
fas-associated
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trail-induced
-
bcl-2-associated
-
apoptogenic
- pharmacology
- cdc25c
- puma
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transferase-mediated
-
executioner
-
factor-related
-
deltapsim
- medicine
-
tunel-positive
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sub-g1
Reaction
strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-/-Xaa =
Synonyms
APAF, Apaf-3, apoptotic protease activating factor 3, apoptotic protease Mch-6, C14.010, CASP-9, casp9, casp9-gamma, caspase 9, caspase-9, ICE-LAP6, ICE-like apoptotic protease 6, Mch6
ECTree
3.4.22.62 caspase-9Advanced search results
results (
results (Activating Compound
Activating Compound on EC 3.4.22.62 - caspase-9
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2S)-1-([2-[(2S)-2-aminopropanoyl]-1-(prop-2-en-1-yl)hydrazinyl]carbonyl)-N-(diphenylmethyl)pyrrolidine-2-carboxamide (non-preferred name)
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(2S)-1-([2-[(2S)-2-aminopropanoyl]-1-(prop-2-yn-1-yl)hydrazinyl]carbonyl)-N-(diphenylmethyl)pyrrolidine-2-carboxamide (non-preferred name)
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(2S)-1-([2-[(2S)-2-aminopropanoyl]-1-benzylhydrazinyl]carbonyl)-N-(diphenylmethyl)pyrrolidine-2-carboxamide (non-preferred name)
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(2S)-1-([2-[(2S)-2-aminopropanoyl]-1-methylhydrazinyl]carbonyl)-N-(diphenylmethyl)pyrrolidine-2-carboxamide (non-preferred name)
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(2S)-1-([2-[(2S)-2-aminopropanoyl]hydrazinyl]carbonyl)-N-(diphenylmethyl)pyrrolidine-2-carboxamide (non-preferred name)
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adenosine
extracellular adenosine induces apoptosis by activating caspase-9 and caspase-3 in association with mitochondrial damage via A2a adenosine receptors, induction dose-dependent (1-20 mM) and time-dependent (24-72 h)
cordycepin
i.e. 3'-deoxyadenosine, cells treated with 100 mM and 1 mM for 24 h, expression of caspase-9, Western blot analysis
NO
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NO generated during hypoxia leads to activation of caspase-9 and results in initiation of caspase-cascade-dependent hypoxic neuronal death
staurosporine
initiates apoptosis, 25% of the cells are apoptotic in staurosporine-treated cultures, 1 microM for 4 h, used as a positive control for caspase-9 activation in C2C12 cells, mitochondrial changes in apoptotic but not in differentiating cells
APAF-1
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proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator
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APAF-1
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caspase-9, Bcl-Xl and Apaf-1 form a ternary complex. Caspase-9 likely represents a direct downstream target of Agaf-1 and its activation appears critical for the propagation of death signals
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APAF-1
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caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation
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APAF-1
interaction with APAF-1 promotes auto-cleavage and activation of caspase-9
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additional information
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activation of caspase-9 1 h after treatment with a combination of 8-methoxypsoralen and ultraviolet-A radiation
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additional information
treatment of HL-60 cells with 1 microM benzo[a]pyrene-7,8-diol-9,10-epoxide (BPDE) elicits induction of caspase-9 activity
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additional information
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treatment of HL-60 cells with 1 microM benzo[a]pyrene-7,8-diol-9,10-epoxide (BPDE) elicits induction of caspase-9 activity
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additional information
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activation of caspase-9 requires mitochondrial release of cytochrome c to the cytoplasm during apoptosis
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additional information
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treatment with the NSAID FR122047 promotes apoptosis and caspase activation in MCF-7 cells
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additional information
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activation of caspase-9 via proteolytic cleavage. Design and synthesis of azapeptide activators of apoptosis mediated by caspase-9 in cancer cells, a set of azapeptides was designed based on the Ala-Val-Pro-Ile peptide (derived from second mitochondria-derived activator of caspase, Smac, protein) to activate caspase-9 and induce apoptosis in breast cancer cells. overview
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additional information
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caspase-9 is activated on the apoptosome complex. Through its higher affinity, procaspase-9 displaces processed caspase-9 from the apoptosome, thereby closing the proteolytic timer cycle. Dimerisation of caspase-9 results in rapid autocatalytic cleavage, yielding caspase-9 (p35/p12)
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additional information
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the uncleaved monomeric zymogen of caspase-9 has very low activity, which is increased upon dimerization. In dimeric caspase-9 cleavage at a specific aspartate residue in the intersubuint linker between the large and small subunits is required for caspase-9 to attain increased activity. Full enzymatic activity is achieved only upon interaction with the apoptosome, a multicomponent, heptameric caspase-9 activating platform
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additional information
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the zymogen caspase-9 has very low activity as a monomer. Activity increases upon dimerization and increases even more profoundly upon interaction with the apoptosome, a heptameric complex formed from association of Apaf-1 and cytochrome c in an ATP-dependent process. Caspase-9 does not require intersubunit cleavage for activation
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additional information
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benzene, tendency to increase caspase-9 expression after 12 days of oral benzene treatment to p53KO mice
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additional information
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atorvastatin induces apoptosis in vitro, dose dependent effect, first detectable after 20 h, increased activity of caspase-9 to 407% and of caspase-3 to 540% after treatment with atorvastatin and/or mevalonic acid (125 microM), with and without the kinase-activator U0126 (10 microM)
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