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
-
annexin
-
extrinsic
- cyclin
- leukemia
- bid
-
neuroprotective
-
depolarization
-
polyadp-ribose
- survivin
-
hoechst
- z-vad-fmk
-
antiproliferative
- adp-ribose
- xiap
- iodide
-
deoxynucleotidyl
-
mitochondria-dependent
-
mitochondria-mediated
- cisplatin
- dutp
- fadd
- procaspase-3
-
caspase-mediated
-
pan-caspase
-
fas-mediated
-
trail
-
fas-associated
-
trail-induced
-
bcl-2-associated
-
apoptogenic
- pharmacology
- cdc25c
- puma
-
transferase-mediated
-
executioner
-
factor-related
-
deltapsim
- medicine
-
tunel-positive
-
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 (Subunits
Subunits on EC 3.4.22.62 - caspase-9
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
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gel filtration and SDS-PAGE, caspases are functional as homodimers of monomeric units that comprise an N-terminal prodomain and a catalytic large and small subunit connected by an intersubunit linker. The zymogen (uncleaved) caspase-9 as a monomer has very low activity, which is increased upon dimerization
additional information
?
x * 68000, observed molecular weight of caspase-9 by tandem mass spectrometry in cell lysates with and without cytochrome c/dATP treatment
?
x * 69200, calculated molecular weight of caspase-9 by tandem mass spectrometry in cell lysates with and without cytochrome c/dATP treatment
dimer
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dimerisation of caspase-9 results in rapid autocatalytic cleavage, yielding caspase-9 (p35/p12)
dimer
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processed caspase-9 can be displaced from the apoptosome by additional molecules of procaspase-9, resulting in release of cleaved caspase-9, which can form active dimers
additional information
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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
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. Caspase-9 does not require intersubunit cleavage for activation
additional information
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the caspase family signature histidine active-site H236SQYDCCVVIMLSHG250, the cysteine active-site K290PKLFFIQACGG301 and the caspase 9 characteristic pentapeptide active-site QACGG are located in the p20 domain
