3.4.22.36: caspase-1
This is an abbreviated version!
For detailed information about caspase-1, go to the full flat file.
Word Map on EC 3.4.22.36
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3.4.22.36
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inflammasome
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pyroptosis
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pyrin
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caspases
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nod-like
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lps
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necrosis
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tnf
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apoptosis-associated
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speck-like
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lipopolysaccharide
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adaptor
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pro-il-1
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toll-like
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card
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domain-containing
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nucleotide-binding
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neuroinflammation
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autoinflammatory
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lps-induced
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bcl-2
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domain-like
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thp-1
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multiprotein
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tunel
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microglia
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gasdermin
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danger
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marrow-derived
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interleukin-18
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leucine-rich
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cpp32
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urate
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nod2
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damage-associated
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nigericin
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medicine
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txnip
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il-1ra
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bmdms
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pan-caspase
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hmgb1
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gouty
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lymphopoietin
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monosodium
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fas-mediated
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z-vad-fmk
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fas-associated
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caspase-3-like
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pathogen-associated
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z-devd-fmk
- 3.4.22.36
- inflammasome
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pyroptosis
- pyrin
-
caspases
-
nod-like
- lps
- necrosis
- tnf
-
apoptosis-associated
-
speck-like
- lipopolysaccharide
- adaptor
-
pro-il-1
-
toll-like
-
card
-
domain-containing
-
nucleotide-binding
-
neuroinflammation
-
autoinflammatory
-
lps-induced
- bcl-2
-
domain-like
- thp-1
-
multiprotein
-
tunel
- microglia
-
gasdermin
-
danger
-
marrow-derived
- interleukin-18
-
leucine-rich
- cpp32
- urate
- nod2
-
damage-associated
- nigericin
- medicine
-
txnip
-
il-1ra
-
bmdms
-
pan-caspase
- hmgb1
-
gouty
- lymphopoietin
-
monosodium
-
fas-mediated
- z-vad-fmk
-
fas-associated
-
caspase-3-like
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pathogen-associated
- z-devd-fmk
Reaction
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/- =
Synonyms
apoptosis-related cysteine protease, C14.001, CASP-1, Casp1, caspase 1, caspase-1, Csp-1, cysteine aspartyl protease-1, effector caspase, H.a.CASP1, hearm caspase-1, ICE, IL-1 beta converting enzyme, IL-1 converting enzyme, IL-1-converting enzyme, IL-1B converting enzyme, IL-1BC, IL-1beta-converting enzyme, IL-1beta–-converting enzyme, IL1beta-converting enzyme, interleukin 1, beta, convertase, interleukin converting enzyme, interleukin-1 beta converting enzyme, interleukin-1 converting enzyme, interleukin-1-converting enzyme, interleukin-1B converting enzyme, interleukin-1beta converting enzyme, interleukin-1beta-converting enzyme, interleukin-converting enzyme, p45, procaspase-1
ECTree
3.4.22.36 caspase-1Advanced search results
results (
results (Engineering
Engineering on EC 3.4.22.36 - caspase-1
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A329T
C136S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C169S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C244S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C270S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C285A
C285S
C331S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C362S
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the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C362S/C397S
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the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C364S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C397S
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the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C69S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C72S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C77S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
D297A
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site-directed mutagenesis, mutation at the D297 residue abolishes the effect of caspase-1 on RIG-I
D316A
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site-directed mutagenesis, mutation at the D316 residue does not abolish the effect of caspase-1 on RIG-I
D336A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
E390A
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site-directed mutagenesis, the mutant shows an about 130fold loss of catalytic efficiency compared to the wild-type enzyme
K319R
L265S
N263S
N337A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
R221C
R240Q
R286A
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site-directed mutagenesis, the mutant shows an about 230fold loss of catalytic efficiency compared to the wild-type enzyme
R286K
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site-directed mutagenesis, the mutant shows an about 150fold loss of catalytic efficiency compared to the wild-type enzyme
R286K/E390D
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site-directed mutagenesis, the mutant shows an about 37fold loss of catalytic efficiency compared to the wild-type enzyme
S332A
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site-directed mutagenesis, the mutant shows an about 4fold loss of catalytic efficiency compared to the wild-type enzyme
S333A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
S339A
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site-directed mutagenesis, the mutant shows an about 7fold loss of catalytic efficiency compared to the wild-type enzyme
T267I
T334A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
T388A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
additional information
A329T
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
C285A
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a procaspase-1 variant with decreased enzymatic activity showing about 3.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
C285S
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site-directed mutagenesis, in comparison to wild type procaspase-1, expression of the C285S mutant does not alter the cellular levels of the RIG-I protein
C285S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
K319R
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a procaspase-1 variant with decreased enzymatic activity showing about 1.6fold increased nuclear factor-kappaB activation compared to the wild type enzyme
K319R
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
L265S
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a procaspase-1 variant with decreased enzymatic activity showing about 6.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
L265S
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
N263S
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a procaspase-1 variant with decreased enzymatic activity showing about 1.8fold increased nuclear factor-kappaB activation compared to the wild type enzyme
N263S
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
R221C
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
R240Q
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a procaspase-1 variant with decreased enzymatic activity showing about 5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
R240Q
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
T267I
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
additional information
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caspase-1-/- bone marrow-derived macrophages exhibit strong caspase-3 expression and reduced cell damage compared to wild-type cells during early Burkholderia pseudomallei infection, indicating classical apoptosis, whereas wild-type bone marrow-derived macrophages show signs of rapid caspase-1-dependent cell death. Caspase-1-/- bone marrow-derived macrophages exhibit impaired bactericidal activity compared to wild-type bone marrow-derived macrophages
additional information
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caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
additional information
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caspase-1-deficient mice have unimpaired inflammatory responses to necrotic cells
additional information
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defective Anthrax-induced interleukin-1beta secretion in Nod2-/- or caspase-1-/- macrophages, not due to decreased pro-interleukin-1beta expression, caspase-1 or NOD2 deficiencies do not exert a major effect on TNF-alpha secretion
additional information
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genetic disruption of cryopyrin or the adaptor apoptosis associated speck-like protein, ASC, abrogates caspase-1 activation in poly(I:C), dsRNA, or viral RNA-stimulated macrophages
additional information
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Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
additional information
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secretion of interleukin-1beta following KIM5 infection is reduced in caspase-1-deficient macrophages compared to wild-type macrophages
additional information
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caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
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additional information
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Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
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