Information on EC 3.4.22.55 - caspase-2

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The expected taxonomic range for this enzyme is: Tetrapoda

EC NUMBER
COMMENTARY hide
3.4.22.55
-
RECOMMENDED NAME
GeneOntology No.
caspase-2
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
strict requirement for an Asp residue at P1, with Asp316 being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-/-
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
182372-14-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
BALB/c
SwissProt
Manually annotated by BRENDA team
C3H/An
SwissProt
Manually annotated by BRENDA team
male C57BL/6
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
caspase-2 is synthesized as an inactive zymogen. The zymogen sequence includes a long prodomain containing a CARD followed by a large domain, a linker, and a small domain. Caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19 and the small subunit p12. This p19/p12 dimer self-associates to form the active caspase-2
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-DEVD-7-amino-4-trifluoromethyl coumarin + H2O
7-amino-4-trifluoromethyl coumarin + Ac-DEVD
show the reaction diagram
-
37°C, pH 7.0, 10 mM dithiothreitol
-
-
?
Ac-VDVAD-7-amido-4-trifluoromethylcoumarin + H2O
Ac-VDVAD + 7-amido-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
acetyl-DEHD-7-amido-4-methylcoumarin + H2O
acetyl-DEHD + 7-amino-4-methylcoumarin
show the reaction diagram
-
DEHD is the optimal tetrapeptide recognition motif
-
-
?
acetyl-Val-Asp-Val-Ala-Asp-4-nitroanilide + H2O
acetyl-Val-Asp-Val-Ala-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VDQQD-4-nitroanilide + H2O
acetyl-VDQQD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VDVAD-4-nitroanilide + H2O
acetyl-VDVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VDVADGW-amide + H2O
?
show the reaction diagram
-
preferred peptide substrate
-
-
?
all-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-all-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-II-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
BID + H2O
?
show the reaction diagram
Bid + H2O
tBid + ?
show the reaction diagram
caspase-2 + H2O
?
show the reaction diagram
catalytically inactive pro-caspase-2 + H2O
caspase-2
show the reaction diagram
-
37°C, pH 7.0, 10 mM dithiothreitol
-
-
?
CERT + H2O
?
show the reaction diagram
-
-
-
-
?
Cip1/p21 Bid + H2O
?
show the reaction diagram
-
-
-
-
?
CUX1 + H2O
?
show the reaction diagram
cyclophilin A + H2O
?
show the reaction diagram
-
-
-
-
?
DELTANp63 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoplakin + H2O
?
show the reaction diagram
-
-
-
-
?
DEVD-AFC + H2O
DEVD + AFC
show the reaction diagram
-
-
-
-
?
DNp63a + H2O
?
show the reaction diagram
-
-
-
-
?
elF4B + H2O
?
show the reaction diagram
-
-
-
-
?
eukaryotic translation initiation factor 4B + H2O
?
show the reaction diagram
-
Asp563 in eukaryotic translation initiation factor 4B is a caspase-2-preferred cleavage site
-
-
?
fatty acid binding protein 5 + H2O
?
show the reaction diagram
-
-
-
-
?
golgin-160 + H2O
?
show the reaction diagram
golgin-160 + H2O
p163 fragment + ?
show the reaction diagram
-
cleavage site is ESPD59G
-
-
?
HDAC4 + H2O
?
show the reaction diagram
huntingtin + H2O
?
show the reaction diagram
ICAD + H2O
?
show the reaction diagram
liposomes + H2O
permealized liposomes
show the reaction diagram
-
22°C
-
-
?
MDM-2 + H2O
?
show the reaction diagram
-
-
-
-
?
MDM2 + H2O
?
show the reaction diagram
-
-
-
-
?
MDM2 + H2O
MDM2 p60 + ?
show the reaction diagram
Mdm2 + H2O
processed Mdm2 + p60
show the reaction diagram
mouse double minute 2 homolog + H2O
?
show the reaction diagram
-
-
-
-
?
myotrophin + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-DEVD-4-nitroanilide + H2O
N-acetyl-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Val-Asp-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Val-Asp-Val-Ala-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-acetyl-VDVAD-7-amido-4-methylcoumarin + H2O
N-acetyl-VDVAD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
NF kappaB activator + H2O
?
show the reaction diagram
-
RIP1
proteolytic fragments of approximate 56 kDa and 20 kDa
-
?
pakin + H2O
?
show the reaction diagram
-
-
-
-
?
PARP + H2O
?
show the reaction diagram
PKC-delta + H2O
?
show the reaction diagram
-
in JURKAT cells
-
-
?
plakin + H2O
?
show the reaction diagram
-
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
show the reaction diagram
-
-
-
-
?
pro-caspase-7 + H2O
caspase-7
show the reaction diagram
-
37°C, pH 7.0, 10 mM dithiothreitol
-
-
?
procaspase-7 + H2O
caspase-7 + ?
show the reaction diagram
procaspase-8 + H2O
processed procaspase-8
show the reaction diagram
-
processing occurs between the large and small subunits
p43/41 form
-
?
profilin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
protein kinase Cdelta + H2O
?
show the reaction diagram
PRP31 pre-mRNA processing factor 31 homolog + H2O
?
show the reaction diagram
-
-
-
-
?
Rho kinase-2 + H2O
?
show the reaction diagram
-
-
-
-
?
ROCK1 + H2O
?
show the reaction diagram
-
-
-
-
?
ROCK2 + H2O
?
show the reaction diagram
-
-
-
-
?
soluble superoxide dismutase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
stathmin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
thioredoxin + H2O
?
show the reaction diagram
-
-
-
-
?
tropomyosin 2beta + H2O
?
show the reaction diagram
-
-
-
-
?
tropomyosin 3 + H2O
?
show the reaction diagram
-
-
-
-
?
Val-Asp-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
Val-Asp-Val-Ala-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Val-Asp-Val-Ala-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Val-Asp-Val-Ala-Asp + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
VDVAD + H2O
?
show the reaction diagram
-
-
-
-
?
VDVAD-4-nitroanilide + H2O
?
show the reaction diagram
-
37°C, pH 8.0, 1 mM DTT
-
-
?
VDVAD-7-amido-4-methylcoumarin + H2O
VDVAD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
VDVADAFC + H2O
VDVAD + AFC
show the reaction diagram
Z-VDVAD-7-amino-4-trifluoromethyl coumarin + H2O
7-amino-4-trifluoromethyl coumarin + Z-VDVAD
show the reaction diagram
-
37°C, pH 7.0, 10 mM dithiothreitol
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
all-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-all-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
BID + H2O
?
show the reaction diagram
Bid + H2O
tBid + ?
show the reaction diagram
caspase-2 + H2O
?
show the reaction diagram
CERT + H2O
?
show the reaction diagram
-
-
-
-
?
CUX1 + H2O
?
show the reaction diagram
cyclophilin A + H2O
?
show the reaction diagram
-
-
-
-
?
DELTANp63 + H2O
?
show the reaction diagram
-
-
-
-
?
desmoplakin + H2O
?
show the reaction diagram
-
-
-
-
?
DNp63a + H2O
?
show the reaction diagram
-
-
-
-
?
elF4B + H2O
?
show the reaction diagram
-
-
-
-
?
eukaryotic translation initiation factor 4B + H2O
?
show the reaction diagram
-
Asp563 in eukaryotic translation initiation factor 4B is a caspase-2-preferred cleavage site
-
-
?
fatty acid binding protein 5 + H2O
?
show the reaction diagram
-
-
-
-
?
golgin-160 + H2O
?
show the reaction diagram
HDAC4 + H2O
?
show the reaction diagram
huntingtin + H2O
?
show the reaction diagram
ICAD + H2O
?
show the reaction diagram
MDM-2 + H2O
?
show the reaction diagram
-
-
-
-
?
MDM2 + H2O
?
show the reaction diagram
-
-
-
-
?
MDM2 + H2O
MDM2 p60 + ?
show the reaction diagram
Mdm2 + H2O
processed Mdm2 + p60
show the reaction diagram
-
Mdm2 is a key negative regulator of p53
-
-
?
mouse double minute 2 homolog + H2O
?
show the reaction diagram
-
-
-
-
?
myotrophin + H2O
?
show the reaction diagram
-
-
-
-
?
pakin + H2O
?
show the reaction diagram
-
-
-
-
?
PARP + H2O
?
show the reaction diagram
plakin + H2O
?
show the reaction diagram
-
-
-
-
?
procaspase-7 + H2O
caspase-7 + ?
show the reaction diagram
-
activation
-
-
?
profilin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
protein kinase Cdelta + H2O
?
show the reaction diagram
PRP31 pre-mRNA processing factor 31 homolog + H2O
?
show the reaction diagram
-
-
-
-
?
Rho kinase-2 + H2O
?
show the reaction diagram
-
-
-
-
?
ROCK1 + H2O
?
show the reaction diagram
-
-
-
-
?
ROCK2 + H2O
?
show the reaction diagram
-
-
-
-
?
soluble superoxide dismutase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
stathmin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
thioredoxin + H2O
?
show the reaction diagram
-
-
-
-
?
tropomyosin 2beta + H2O
?
show the reaction diagram
-
-
-
-
?
tropomyosin 3 + H2O
?
show the reaction diagram
-
-
-
-
?
Val-Asp-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
Val-Asp-Val-Ala-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
activates at 50 mM, the enzyme is stable until 150 mM NaCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14-3-3 zeta
-
-
-
Ac-ADVAD-CHO
-
binding structure
Ac-DVAD-CHO
-
binding structure
Ac-VDVAD-CHO
-
binding structure
acetyl-DEVD-aldehyde
-
-
acetyl-IETD-aldehyde
-
-
amyloid beta
-
treatment of rat hippocampal neuron extracts with either 300 nM or 0.001 mM amyloid beta leads to activation of caspase-2
-
ankyrin
-
specific caspase-2 inhibitor
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
t1/2 at 0.001 mM is 40 min
benzyloxycarbonyl-Val-Asp-Val-Ala-Asp-fluoromethylketone
-
-
benzyloxycarbonyl-VDVAD-fluoromethylketone
-
-
biotinylated VAD-fluoromethylketone
-
irreversible pan-caspase inhibitor
-
bVAD-fmk
-
-
calcium/calmodulin regulated protein kinase II
-
phosphorylates caspase-2 at Ser-135
-
calcium/calmodulin-dependent kinase II
-
-
-
Cbzl-VDVAD-fluoromethylketone
-
caspase-2 cleaves BID in response 16 to endoplasmic reticulum stress. Resistance to endoplasmic reticulum stress-induced apoptosis can be conferred by inhibiting caspase-2 activity
coenzyme Q10
-
-
cyclin-dependent kinase 1
-
-
-
cyclin-dependent protein kinase1/cyclin B1
-
-
-
glucocorticoid modulatory element-binding protein 1
-
GMEB1, endogenous inhibitor of pro-caspase-2 activation
-
miR-708
-
-
-
pifithrin-alpha
-
-
protein kinase CK2
-
phosphorylates procaspase-2 directly at serine-157. When protein kinase CK2 activity is low, procaspase-2 is dephosphorylated, dimerized, and activated in a PIDDosome-independent manner
-
protein kinase KII
-
-
-
Q-VD-OPH
SP600125
-
inhibits caspase-2 partially
VAD-fmk
-
-
VDVAD
Z-Leu-Glu(OMe)-Thr-Asp(OMe)-CH2F
-
-
Z-Val-Ala-Asp-fluoromethylketone
Z-Val-Asp(OMe)-Val-Ala-Asp(OMe)-CH2F
Z-Val-Asp-Val-Ala-Asp-fluoromethylketone
z-VDVAD-fmk
zVAD-fmk
-
0.05 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloro-2'-deoxyadenosine
-
-
amyloid beta1-42
-
the levels of activated caspase-2 in cultured hippocampal neurons significantly increase within 30 min of treatment with 0.003 mM amyloid beta1-42
-
ATM/ATR
-
caspase-10
-
is required for effective processing of caspase-2
-
CD95-death-inducing signaling complex
-
-
-
cyclin D3
-
-
-
lovastatin
-
0.05 mM for 24 h, increases caspase-2 gene expression
p53-induced protein with a death domain
-
PIDD, caspase-2 is activated by the p53 target gene product PIDD, i.e. LRDD or leucine-rich repeats and death domain containing, in a complex called the caspase-2-PIDDosome
-
p53-inducible death domain-containing protein
-
PIDD
-
p73
-
-
-
palmitate
-
caspase-2 is activated by an overabundance of saturated long-chain fatty acids like palmitate. Inhibition of amino acid transamination by 10 mM aminooxyacetate blocks caspase activation
PIDD protein
-
-
-
PIDDosome
-
-
-
protein phosphatase 1
-
-
-
RAIDD
-
RAIDD protein
-
-
-
silibinin
-
caspase-2 and caspase-8 can activate each other in response to silibinin
sterol regulatory element binding protein 2
-
increases caspase-2 gene expression
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
Ac-VDVAD-7-amido-4-trifluoromethylcoumarin
-
pH 6.5, 22°C, wild-type enzyme
0.53
acetyl-VDQQD-4-nitroanilide
-
pH 6.2, 30°C
0.053
acetyl-VDVAD-4-nitroanilide
-
pH 6.2, 30°C
0.15
acetyl-VDVADGW-amide
-
pH 6.2, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
Ac-VDVAD-7-amido-4-trifluoromethylcoumarin
Homo sapiens
-
pH 6.5, 22°C, wild-type enzyme
additional information
additional information
Homo sapiens
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00171
acetyl-DEVD-aldehyde
-
pH 7.5, 25°C
0.0094
acetyl-IETD-aldehyde
-
pH 7.5, 25°C
additional information
additional information
-
KM-values above 0.01 mM are obtained with acetyl-WEHD-aldehyde, acetyl-YVAD-aldehyde, acetyl-AEVD-aldehyde and cowpox serpin CrmA
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
Ac-ADVAD-CHO
Homo sapiens
-
pH 6.5, 22°C, wild-type enzyme
0.00071
Ac-DVAD-CHO
Homo sapiens
-
pH 6.5, 22°C, wild-type enzyme
0.000025
Ac-VDVAD-CHO
Homo sapiens
-
pH 6.5, 22°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
treatment of melanoma cells with terfenadine induced DNA damage and caspases 2 activation. A selective inhibitor of caspase-2 (benzyloxycarbonyl-VDVAD-fluoromethylketone) protects melanoma cells from terfenadine-induced apoptosis
Manually annotated by BRENDA team
-
histone deacetylase inhibition leads to decreased protein kinase casein kinase 2 activity, which is followed by caspase-2 activation and partial cleavage of caspase-8 that sensitizes the tumor cell to TRAIL-induced apoptosis
Manually annotated by BRENDA team
-
PS-341 (bortezomib) induces a dose-dependent apoptosis in association with reactive oxygen species generation and cleavage of caspase-2 to its 33- and 14-kDa fragments. PS-341-induced caspase-2 activation is attenuated by a selective pharmacological inhibitor of cathepsin B (R-3032). Caspase-2 regulates mitochondrial permeability
Manually annotated by BRENDA team
at estrus, activity is 7.6fold greater in the old corpus luteum compared to new corpus luteum; immunostaining for caspase-2 increases as the luteal phase progresses
Manually annotated by BRENDA team
immunostaining for caspase-2 increases as the luteal phase progresses
Manually annotated by BRENDA team
-
human esophageal cancer cell line
Manually annotated by BRENDA team
-
human esophageal cancer cell line
Manually annotated by BRENDA team
-
hepatoma cell line
Manually annotated by BRENDA team
-
thrombin initiates EMP generation from the human microvascular endothelial cell line HMEC-1. Caspase-2 plays a role in release of endothelial microparticles by controlling the proteolytic activation of ROCK-II
Manually annotated by BRENDA team
-
human malignant glioma cell line
Manually annotated by BRENDA team
-
caspase 2 activation is required for release of cytochrome c and cell death
Manually annotated by BRENDA team
-
human colon cancer cell line
Manually annotated by BRENDA team
-
human pancreatic cancer cell
Manually annotated by BRENDA team
-
human esophageal cancer cell line
Manually annotated by BRENDA team
-
adult
Manually annotated by BRENDA team
additional information
-
isoform casp-2S is undetectable in the SKOV3, H-1299 and HCT-116 p53-deficient cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in mitotic primary mouse embryonic fibroblast
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13000
-
1 * 13000 + 1 * ?, active form, SDS-PAGE
18000
active form, 1 * 34000 + 1 * 18000, SDS-PAGE
34000
active form, 1 * 34000 + 1 * 18000, SDS-PAGE
48000
monomer, pro-caspase-2, inactive form, SDS-PAGE
51000
-
monomer, inactive form, pro-caspase-2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
oligomer
-
caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19, residues 170-333, and the small subunit p12, residues 348-452. This p19/p12 dimer self-associates to form the active caspase-2
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
sumoylation
-
-
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant caspase-2 enzymes complexed with peptide aldehyde inhibitors, incubation of 3 mg/ml protein with 1-5 mM peptide aldehyde inhibitor in DMSO at room temperature for 2 h, hanging drop vapour diffusion method, mixing of 0.002 ml of protein complex solution with 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.0, 15% PEG 3350, 3 mM DTT, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution, molecular replacement
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anti-FLAG affinity gel chromatography, and gel filtration
-
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant enzyme
-
recombinant procaspase-2 from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography to over 95%
-
recombinant protein from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Jurkat cells
-
caspase-2 maps to the q34-35 segment of human chromosome 7
-
commercial preparation of cDNA, in vitro transcription/translation
-
expressed as fusion protein in HeLa cell and HEK-293T cell
-
expressed in HEK-293T cells
-
expression in Saccharomyces cerevisiae and Escherichia coli
-
expression of procaspase-2 in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain Bl21 (DE3) pLysS
-
GST-fusion contruct expressed in Escherichia coli BL21
-
GST-fusion protein expressed in Escherichia coli BL21
-
in vitro translation, His6-tagged protein expressed in Escherichia coli BL21
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wild-type, mutants C303A and D316G are expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
caspase-2 enzyme activity in both Brucella abortus strain RB51- and S2308-infected bone marrow-derived dendritic cells is significantly up-regulated at 1 h, 4 h, and 24 h post infection
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caspase-2 induction by p53
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downregulated duiring the development of the central nervous system
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highly expressed in neural precursor cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D152A
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pro-caspase mutant, like the wild-type, this mutant is efficiently processed between the large and the small subunit, however, it is not further processed to seperate the prodomain from the large subunit
D316A
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fusion of the linker to the large subunit, toxic when expressed in yeast
D316A/D330A
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abolishes auto-processing and reduces enzymatic activity dramatically, 840fold decrease in activity
D316G
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uncleavable
D330A
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fusion of the linker to the small subunit, slightly greater deleterious effect on enzyme activity than fusion to the large subunit (D316A), toxic when expressed in yeast
S135A
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phosphorylation site
S157A/C320A
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nonphosphorylatable, dimerizes constitutively
S340A
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phosphorylation site, expression of mutant S340A more than doubles the sensitivity of cells to nocodazole-induced mitotic death compared with wild-type protein
T380A
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site-directed mutagenesis
T380A/Y420A
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site-directed mutagenesis
Y420A
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site-directed mutagenesis
C320A
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catalytically inactive
K152A
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mutant enzyme with strikingly altered caspase-2 localization. Whereas caspase-2 characteristically accumulates in the nucleus forming dots or filaments, the mutant enzyme is mostly localized outside and exclusively of the nucleus forming dot-like aggregates. K152A mutants can also kill transfected cells at comparable levels to the wild-type version
S139An
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expression of mutant S139A leads to significantly enhanced growth rate of cells
S135A
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phosphorylation site, suppressed equally compared with wild type protein during mitosis
S135A/S308A
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rapidly processed in mitosis compared with caspase-2 S308A mutant
S308A
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phosphorylation site, S308 phosphorylated in mitosis, abrogates mitotic suppression, processing of mutant S308A in mitosis does not occur immediately, but rather occurs with roughly the same kinetics as wild-type caspase-2 in interphase
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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high level of inactive, non-processed caspase-2 together with caspase-3 is used as a predictor of survival and complete remission in adults with acute myeloblastic or lymphoblastic leukemias