3.4.22.59: caspase-6
This is an abbreviated version!
For detailed information about caspase-6, go to the full flat file.
Word Map on EC 3.4.22.59
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3.4.22.59
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caspases
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bcl-2
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alzheimer
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neurodegenerative
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pro-apoptotic
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huntington
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lamins
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apoptosis-related
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parp
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executioner
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caspase-dependent
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anti-apoptotic
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polyadp-ribose
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tunel
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caspase-mediated
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casps
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jurkat
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bid
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pan-caspase
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zvad-fmk
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apaf-1
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medicine
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procaspase-3
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fadd
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diagnostics
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fas-associated
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drug development
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molecular biology
- 3.4.22.59
-
caspases
- bcl-2
- alzheimer
- neurodegenerative
-
pro-apoptotic
- huntington
- lamins
-
apoptosis-related
- parp
-
executioner
-
caspase-dependent
-
anti-apoptotic
-
polyadp-ribose
-
tunel
-
caspase-mediated
-
casps
-
jurkat
- bid
-
pan-caspase
- zvad-fmk
- apaf-1
- medicine
- procaspase-3
- fadd
- diagnostics
-
fas-associated
- drug development
- molecular biology
Reaction
strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-/- =
Synonyms
apoptotic protease Mch-2, C14.005, Cas6, Casp-6, Casp.6, Casp6, caspase 6, caspase-6, caspase-6A, caspase-6B, Csp-6, Csp6, HLcaspase-6, MCH2, Pfcasp-6, VEIDase
ECTree
3.4.22.59 caspase-6Advanced search results
results (
results (Engineering
Engineering on EC 3.4.22.59 - caspase-6
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A109T
missense rare variants with amino acid substitution located remotely from Casp6 active site. Activity with the substrate Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin is comparable to that of wild-type enzyme. No significant changes in kinetic parameters, KM, and kcat, for Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin
A34E
missense rare variants with amino acid substitution located remotely from Casp6 active site. Lower activity than wild-type enzyme with the substrate Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin. No significant changes in kinetic parameters, KM, and kcat, for Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin
C163A
C163S
D163A
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site-directed mutagenesis, uncleavable and catalytically inactive mutant of pro-caspase-6
D179A
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site-directed mutagenesis, the mutant of pro-caspase-6 is altered in one cleavage site residue, and is about half as catalytically active as the wild-type enzyme
D179A/D193A
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site-directed mutagenesis, the mutant of pro-caspase-6 is altered in two cleavage site residues, and is catalytically inactive
D193A
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site-directed mutagenesis, uncleavable and catalytically inactive mutant of pro-caspase-6
D23A
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site-directed mutagenesis, the mutant of pro-caspase-6 is altered in one cleavage site residue, but is still catalytically active similar to the wild-type enzyme
D23A/D179A
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site-directed mutagenesis, the mutant of pro-caspase-6 is altered in two cleavage site residues, and is only slightly to not catalytically active
D23A/D179A/D193A
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site-directed mutagenesis, the triple mutant of pro-caspase-6 is altered in three cleavage site residues becoming uncleavable for activation and thus is catalytically inactive or very poorly active
D23A/D193A
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site-directed mutagenesis, the mutant of pro-caspase-6 is altered in two cleavage site residues, and is catalytically inactive
D316A
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to prevent autocatalytic processing of the specific site of procaspase 6, Asp316 of rCaspase 6 is replaced with Ala
E244A
the function of the mutant is crippled by 2fold compared to the wild type enzyme
E244A/H287A
the function of the mutant is crippled by 47fold compared to the wild type enzyme
E35K
missense rare variants with amino acid substitution located remotely from Casp6 active site. Lower activity than wild-type enzyme with the substrate Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin. Slightly reduced kcat and about 2fold reduced catalytic efficiency kcat/KM
H287A
the function of the mutant is crippled by 14fold compared to the wild type enzyme
K36A
the function of the mutant is crippled by 2fold compared to the wild type enzyme
R42A/R43A/R44A
substitutions of the tri-arginine patch Arg-42-Arg-44 markedly alters rates of protein substrate hydrolysis. Turnover of protein substrates but not of short peptide substrates is affected. The mutant is unable to fully hydrolyze itself to the mature form
R44K
cancer-associated mutation markedly alters rates of protein substrate hydrolysis. Turnover of protein substrates but not of short peptide substrates is affected
S257A
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mutant caspase-6, not phosphorylated in the presence of active AMPK-related kinase 5
T182S
missense rare variants with amino acid substitution located remotely from Casp6 active site. Lower activity than wild-type enzyme with the substrate Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin. No significant changes in kinetic parameters, KM, and kcat, for Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin
additional information
C163S
the mutant is catalytically inactive and not capable of self-cleavage
additional information
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a flag-tagged dominant-negative caspase-6 point mutant is expressed in Saos-2 cells
additional information
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downregulation of caspase-6 by siRNA reduces bile acid-induced apoptosis and caspase-8 activation in Hep-G2-Ntcp cells
additional information
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generation of stable caspase-6 knockdown cell lines using K562 cells. Mutations at residues D442, D444, D516, D768, and D936 do not prevent cleavage in vitro
additional information
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proliferation and cell death are not enhanced in Casp6 KO B cells, immunoresponses, overview. B cells from Casp6 knockout mice examined ex vivo have more cells in G1 than wild-type B cells, and mitogen-induced G1 entry of Casp6 KO B cells is much faster than that of wild-type B cells. Even so, S phase entry and proliferation are not increased in Casp6 KO B cells. Rather than proliferating, activated Casp6 KO B cells preferentially differentiate into syndecan-1+ plasma cells and produce Abs. In Casp6 KO mice compared with wild-type mice, serum levels of IgG1, IgG2a, and IgG2b are increased and Ag-specific Ab responses are also enhanced along with increased percentages of syndecan-1+ plasma cells
additional information
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generation of knockout mice by using a construct for targeting the C57BL/6 caspase-6 locus in ES cells. lamin A/C degradation is markedly reduced in fibroblasts extracted from caspase-6 knock-out mice relative to fibroblasts from wild type mice
additional information
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generation of knockout mice by using a construct for targeting the C57BL/6 caspase-6 locus in ES cells. lamin A/C degradation is markedly reduced in fibroblasts extracted from caspase-6 knock-out mice relative to fibroblasts from wild type mice
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additional information
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proliferation and cell death are not enhanced in Casp6 KO B cells, immunoresponses, overview. B cells from Casp6 knockout mice examined ex vivo have more cells in G1 than wild-type B cells, and mitogen-induced G1 entry of Casp6 KO B cells is much faster than that of wild-type B cells. Even so, S phase entry and proliferation are not increased in Casp6 KO B cells. Rather than proliferating, activated Casp6 KO B cells preferentially differentiate into syndecan-1+ plasma cells and produce Abs. In Casp6 KO mice compared with wild-type mice, serum levels of IgG1, IgG2a, and IgG2b are increased and Ag-specific Ab responses are also enhanced along with increased percentages of syndecan-1+ plasma cells
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