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3.4.22.56: caspase-3

This is an abbreviated version!
For detailed information about caspase-3, go to the full flat file.

Word Map on EC 3.4.22.56

Reaction

strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position =

Synonyms

apopain, C14.003, Cas-3, CASP-3, CASP3, caspase 3, caspase-3, CgCaspase-3, CPP-32, CPP32, CPP32/apopain, cystein aspartic-specific protease-3, cysteine aspartic acid-specific protease, cysteine protease CPP32, DEVDase, IRP, Lyccasp3, Mncaspase-3c, More, SBTc-3, SCA-1, SREBP cleavage activity 1, Yama protein, Yama/CPP32, ZCASP3

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.56 caspase-3

Engineering

Engineering on EC 3.4.22.56 - caspase-3

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C143A
-
inactive enzyme. Catalytically inactive p17 polypeptide is expressed in a stable manner, while wild-type p17 is rapidly degraded
D179A
increase both in kcat- and KM-value. D179 is involved in substrate recognition
DELTA176-181
decrease both in kcat- and KM-value
R207E/C163S
-
site-directed mutagenesis, the mutant resides in the cytoplasm
R64E
-
site-directed mutagenesis, the mutant existed in the nuclear fraction, the subcellular localization signal in the rev-caspase-3 is not disrupted by the R64E mutation
R64E/C163S
-
site-directed mutagenesis, the mutant resides in the cytoplasm
R64E/R207E
-
site-directed mutagenesis, the mutant resides in the cytoplasm
C163G
-
transfection of human breast cancer cells lacking enzyme with wild-type or mutant cDNA. Expression of wild-type, but not the inactive mutants C163G or C163S, is associated with increased enzyme activity and susceptibility to staurosporine-induced apoptosis. Wild-type and mutant transfection results in inhibition of cell growth and decrease in phosphorylation of the Akt protein compared to control
C163S
-
transfection of human breast cancer cells lacking enzyme with wild-type or mutant cDNA. Expression of wild-type, but not the inactive mutants C163G or C163S, is associated with increased enzyme activity and susceptibility to staurosporine-induced apoptosis. Wild-type and mutant transfection results in inhibition of cell growth and decrease in phosphorylation of the Akt protein compared to control
additional information