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
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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
Advanced search results
Engineering
Engineering on EC 3.4.22.62 - caspase-9
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analysis
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optical sensor for the detection of caspase-9 in a single cell. LEHD-7-amido-4-methylcoumarin covalently attached on the nanoprobe tip of the optical sensor is cleaved during apoptosis by caspase-9 generating free 7-amino-4-methylcoumarin
C172A
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the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C239S
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the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C272A
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the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C272A/C287A
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the mutant enzyme shows highly reduced zinc binding compared to the wild-type enzyme
C287A
C287A/C239S
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the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
C403S
point mutation at C403 of caspase-9 impairs its activation mediated by H2O2, interaction with APAF-1 diminished through the abolition of disulfide formation, weaker association between cytochrome c and the C403S mutant than that between cytochrome c and wild-type caspase-9
DELTA1-111
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a truncated form of procaspase-9 missing the first 111 amino acids, and a variety of mutants derived therefrom are expressed in Echerichia coli inclusion bodies. Upon refolding to active enzyme, DELTA1-111 procaspase-9 and mutants are recovered at purity greater than 95% with a final yield of 20-35 mg/L cell culture. the active procaspaseretains its prosegment, while undergoing major auto processing at ASp315 and a minor cleavage at Glu306
DELTA1-111/DELTAA316-D330
DELTA1-111/E306A/D315A
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E306A/D315A mutation blocks autoprocessing and shifts pH optimum from pH 6.2 for DELTA1-111 to pH 7.2. Activity with acetyl-LEHD-7-amido-4-trifluoromethyl coumarin is identical to the activity of mutant DELTA1-111
DELTA1-111/E306D/D315A
DELTA1-111/E306D/DELTAA316-D330
H237A
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the active site mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
T125A/C287A
site-directed mutagenesis, immunofluorescence staining of cells transiently transfected with vectors encoding caspase-9 double mutant
C299G
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site-directed mutagenesis, the mutant displays significantly decreased proteolytic activity compared to the wild-type enzyme
H249D
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site-directed mutagenesis, the mutant displays significantly decreased proteolytic activity compared to the wild-type enzyme
S348A
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S348G
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S348V
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
S350A
introduction of point mutants into full-length murine caspase-9 (mC-9) cDNA, generated by a two-step PCR method, efficiently cleaved by the active initiator caspase
additional information
immunofluorescence staining of cells transiently transfected with vectors encoding caspase-9 point mutation
C287A
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the active site mutant enzyme shows reduced zinc binding compared to the wild-type enzyme
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activity with acetyl-LEHD-7-amido-4-trifluoromethylcoumarin is 6fold higher than the activity of mutant DELTA1-111
DELTA1-111/DELTAA316-D330
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activity with acetyl-LEHD-7-amido-4-trifluoromethyl coumarin is 6fold higher than the activity of mutant DELTA1-111
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activity with acetyl-LEHD-7-amido-4-trifluoromethylcoumarin is 90% of the activity of mutant DELTA1-111
DELTA1-111/E306D/D315A
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activity with acetyl-LEHD-7-amido-4-trifluoromethyl coumarin is 90% of the activity of mutant DELTA1-111
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activity with acetyl-LEHD-7-amido-4-trifluoromethylcoumarin is 7.6fold higher than the activity of mutant DELTA1-111
DELTA1-111/E306D/DELTAA316-D330
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activity with acetyl-LEHD-7-amido-4-trifluoromethyl coumarin is 7.6fold higher than the activity of mutant DELTA1-111
caspase-9S is a naturally occuring variant of caspase-9 that is missing most of the large subunit of caspase-9, including the catalytic site, but has the intact prodomain and small subunit. Caspase-9S does not show apoptotic activity in transfection analysis. Overexpression of caspase 9S inhibits apoptosis induced by caspase-9. Caspase-9S inhibits apoptosis induced by tumor necrosis factor alpha, TNF factor-related apoptosis-inducing ligand, Bax, or fas-associated death domain-containing protein as well as the combination of Apaf-1 and caspase-9
additional information
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caspase-9S is a naturally occuring variant of caspase-9 that is missing most of the large subunit of caspase-9, including the catalytic site, but has the intact prodomain and small subunit. Caspase-9S does not show apoptotic activity in transfection analysis. Overexpression of caspase 9S inhibits apoptosis induced by caspase-9. Caspase-9S inhibits apoptosis induced by tumor necrosis factor alpha, TNF factor-related apoptosis-inducing ligand, Bax, or fas-associated death domain-containing protein as well as the combination of Apaf-1 and caspase-9
additional information
engineering of a leucine-zipper-linked dimeric caspase-9 (LZ-C9). Removal of the caspase recruitment domain of procaspase-9 and replacement with the leucine-zipper dimerization domain of the transcriptional factor GCN4. A six residue linker is added in between the leucine zipper and the beginning of the catalytic domain of caspase-9. LZ-C9 is more active than the caspase-9 holoenzyme for acetyl-LEHD-7-amido-4-trifluoromethylcoumarin but much less active the the caspase-9 holoenzyme for the physiological substrate procaspase-3
additional information
engineering of a leucine-zipper-linked dimeric caspase-9 (LZ-C9). Removal of the caspase recruitment domain of procaspase-9 and replacement with the leucine-zipper dimerization domain of the transcriptional factor GCN4. A six residue linker is added in between the leucine zipper and the beginning of the catalytic domain of caspase-9. LZ-C9 is more active than the caspase-9 holoenzyme for acetyl-LEHD-7-amido-4-trifluoromethyl coumarin but much less active the the caspase-9 holoenzyme for the physiological substrate procaspase-3
additional information
plasmids pGFP-CASP9 WT/C287/T125 and pGST-CASP9 WT/T125 generated by site-directed mutagenesis
additional information
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plasmids pGFP-CASP9 WT/C287/T125 and pGST-CASP9 WT/T125 generated by site-directed mutagenesis