3.4.22.60: caspase-7
This is an abbreviated version!
For detailed information about caspase-7, go to the full flat file.
Word Map on EC 3.4.22.60
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3.4.22.60
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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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executioner
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necrosis
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polyadp-ribose
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caspase-dependent
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annexin
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tunel
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survivin
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cyclin
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apoptosis-inducing
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adp-ribose
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apoptosis-related
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bid
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xiap
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calpains
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pan-caspase
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jnk
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cdk2
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hoechst
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caspase-mediated
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antiproliferative
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apaf-1
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z-vad-fmk
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caspase-3-like
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pyroptosis
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ac-devd-cho
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apoptosome
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template-based
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puma
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trail-induced
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devd
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caspase-3-deficient
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mitochondria-dependent
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procaspase
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apoptosis-associated
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molecular biology
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casp10
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spinocerebellar
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sub-g1
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medicine
- 3.4.22.60
- caspase-3
- bcl-2
- parp
-
anti-apoptotic
-
pro-apoptotic
-
executioner
- necrosis
-
polyadp-ribose
-
caspase-dependent
-
annexin
-
tunel
- survivin
- cyclin
-
apoptosis-inducing
- adp-ribose
-
apoptosis-related
- bid
- xiap
- calpains
-
pan-caspase
- jnk
- cdk2
-
hoechst
-
caspase-mediated
-
antiproliferative
- apaf-1
- z-vad-fmk
-
caspase-3-like
-
pyroptosis
- ac-devd-cho
- apoptosome
-
template-based
- puma
-
trail-induced
- devd
-
caspase-3-deficient
-
mitochondria-dependent
-
procaspase
-
apoptosis-associated
- molecular biology
- casp10
-
spinocerebellar
-
sub-g1
- medicine
Reaction
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/- =
Synonyms
apoptotic protease Mch-3, C14.004, Casp-7, Casp7, caspase 7, caspase-7, CMH-1, cystein aspartic-specific protease-7, DEVDase, ICE-LAP3, ICE-like apoptotic protease 3, LICE2 cysteine protease, More, SCA-2, SREBP cleavage activity 2
ECTree
3.4.22.60 caspase-7Advanced search results
results (
results (Engineering
Engineering on EC 3.4.22.60 - caspase-7
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C290N
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
D198A
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additionally, amino acid residues 20-25 are replaced with a thrombin cleavage site (LVPRGS) and a thrombin cleavage site (LVPRGS) is inserted between Asp-203 and Thr-204
D23A
the mutation shows increased catalytic activity but is unable to cleave PARP
D628A
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site-directed mutagenesis, caspase-7 resistant mutant, retains telomerase activity
G188L
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
G188P
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
R187M
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
Y223A
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
Y230V/W232Y/S234V/Q276D
variant closely micks the substrate specificty of caspase 6, but does not cleave lamin C, a known caspase-6-specific substrate
additional information
additional information
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engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-7, activities in different mutant cell lines, overview
additional information
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comparison of phenotypes of caspase-7 with caspase-3 deficient cells, overview
additional information
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construction of two truncated mutant isozymes 24casp7 and 57casp7, which lack the first 24 and 57 amino acid residues, respectively, and thus the cleavage site at Asp23
additional information
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knockdown of caspase-7 by using siRNAs results in the inhibition of Hep-G2 cell proliferation, but knockdown of other caspases does not show a significant effect on cell growth. The expression of His-tagged shRNA directed against caspase-7 induce the cell cycle arrest at mitosis, which is rescued by the re-expression of caspase-7 containing silent mutations at the target site for the shRNA
additional information
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caspase cleavage site is substituted and a thrombin cleavage site inserted: amino acid residues 20-25 are replaced with a thrombin cleavage site (LVPRGS) and a thrombin cleavage site (LVPRGS) is inserted between Asp-203 and Thr-204
additional information
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caspase cleavage sites are substituted: amino acid residues 20-25 and 195-200 are replaced with thrombin cleavage sites (LVPRGS)
additional information
caspase-7 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7 activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
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caspase-7 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7 activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
mutational analysis to introduce the specificity of caspase-6 into caspase-7. Substitution of substrate-contacting residues from caspase-6 into caspase-7 is ineffective, yielding an inactive enzyme, whereas saturation mutagenesis at these positions and selection by directed evolution produces active caspases. The structures of the evolved-specificity caspase-7 reveal alternate binding modes for the substrate, including reorganization of an active site loop
additional information
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mutational analysis to introduce the specificity of caspase-6 into caspase-7. Substitution of substrate-contacting residues from caspase-6 into caspase-7 is ineffective, yielding an inactive enzyme, whereas saturation mutagenesis at these positions and selection by directed evolution produces active caspases. The structures of the evolved-specificity caspase-7 reveal alternate binding modes for the substrate, including reorganization of an active site loop
additional information
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comparison of phenotypes of caspase-7 with caspase-3 deficient cells, overview
additional information
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contsruction of caspase-7-deficient mice, that show protection from endotoxin-induced lymphocyte apoptosis and improved survival, phenotype, overview
additional information
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mice lacking caspase-7 and its macrophages allow substantial Legionella pneumophila replication, while wild-type mouse strains are restrictive to Legionella pneumophila infection
additional information
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mice lacking caspase-7 and its macrophages allow substantial Legionella pneumophila replication, while wild-type mouse strains are restrictive to Legionella pneumophila infection
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