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Information on EC 3.4.22.60 - caspase-7 and Organism(s) Mus musculus and UniProt Accession P97864
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3.4.22.60 caspase-7Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/-
Synonyms
caspase-7, caspase 7, casp7, sca-2, cmh-1, casp-7, ice-lap3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apoptotic protease Mch-3
-
-
-
-
C14.004
-
-
-
-
caspase 7
-
-
-
-
CMH-1
-
-
-
-
ICE-LAP3
-
-
-
-
ICE-like apoptotic protease 3
-
-
-
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LICE2 cysteine protease
-
-
-
-
SCA-2
-
-
-
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SREBP cleavage activity 2
-
-
-
-
additional information
-
caspase-7 is a members of the caspase family of cysteine proteases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
189258-14-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-ASTD-7-amido-4-methylcoumarin + H2O
acetyl-ASTD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
inhibitor of caspase-actived DNase + H2O
?
-
mouse caspase-7 and caspase-3 are equally efficient at cleaving
-
-
?
pro-endothelial monocyte-activating polypeptide II + H2O
?
-
caspase-7-mediated generation and release of mature endothelial monocyte-activating polypeptide II may provide a mechanism for leukocyte recruitment to sites of programmed cell death, and thus may link apoptosis to inflammation
-
-
?
pro-endothelial monocyte-activating polypeptide II + H2O
endothelial monocyte-activating polypeptide II + ?
-
pro-endothelial monocyte-activating polypeptide II in which the ASTD cleavage site is changed to the sequence ASTA, is not processed by caspase-7
-
-
?
additional information
?
-
-
intracellular pathogen Legionella pneumophila strain Lp02 infection of murine macrophages leads to caspase-7 activation downstream of the Nlrc4 inflammasome requiring activation by caspase-1, overview. Caspase-1-dependent caspase-7 activation contributes to Legionella pneumophila phagosome maturation in macrophages
-
-
?
additional information
?
-
-
members of the caspase family of cysteine proteases play central roles in coordinating the stereotypical events that occur during apoptosis, the major executioner caspases are caspase-3 and caspase-7, which show overlapping substrate specificities, overview
-
-
?
additional information
?
-
-
the apoptotic executioner caspase-7 is activated in the splenocytes of lipopolysaccharide-injected mice, suggesting a role for caspase-7 in lymphocyte apoptosis. Caspase-7 deficiency and caspase inhibition protect from endotoxin-induced lymphocyte apoptosis and improve survival
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-endothelial monocyte-activating polypeptide II + H2O
?
-
caspase-7-mediated generation and release of mature endothelial monocyte-activating polypeptide II may provide a mechanism for leukocyte recruitment to sites of programmed cell death, and thus may link apoptosis to inflammation
-
-
?
additional information
?
-
-
intracellular pathogen Legionella pneumophila strain Lp02 infection of murine macrophages leads to caspase-7 activation downstream of the Nlrc4 inflammasome requiring activation by caspase-1, overview. Caspase-1-dependent caspase-7 activation contributes to Legionella pneumophila phagosome maturation in macrophages
-
-
?
additional information
?
-
-
members of the caspase family of cysteine proteases play central roles in coordinating the stereotypical events that occur during apoptosis, the major executioner caspases are caspase-3 and caspase-7, which show overlapping substrate specificities, overview
-
-
?
additional information
?
-
-
the apoptotic executioner caspase-7 is activated in the splenocytes of lipopolysaccharide-injected mice, suggesting a role for caspase-7 in lymphocyte apoptosis. Caspase-7 deficiency and caspase inhibition protect from endotoxin-induced lymphocyte apoptosis and improve survival
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzyloxycarbonyl-ASTD-fluoromethylketone
-
0.01 mM, complete inhibition of cleavage of pro-endothelial monocyte-activating polypeptide II
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
caspase 1
-
caspase-7 is cleaved and activated by caspase-1. This is mediated by flagellin and requires the host receptors Nlrc4 and Naip5
-
additional information
-
activation of caspase-7 in macrophages by cleavage through caspase-1 is mediated by bacterial flagellin and absolutely requires a functional host proteins Nlrc4 and Naip5
-
additional information
-
cordycepin induces caspase-7 protein expression, and apoptosis in MA-10 mouse Leydig tumor cells through a caspase-7 dependent pathway, overview
-
additional information
-
Escherichia coli lipopolysaccharides induce the enzyme in splenocytes
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the activated form of caspase-7 is detected from the beginning of ossification during embryonic development and persists postnatally in alveolar and mandibular bones as well as long bones of limbs
-
bone marrow macrophages prepared from femurs of five to eight-week-old mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
caspase-7-deficient MEF cells are not resistance to intrinsic cell death, but remain attached to the extracellular matrix
malfunction
-
caspase-7-deficient mice still possesses apoptotic cells in the primary enamel knot in a similar distribution to the wild type
malfunction
-
enzyme-deficient mice show a significant decrease in mineral density of endochondral bones
malfunction
-
mice lacking caspase-7 and its macrophages allow substantial Legionella pneumophila replication. This permissiveness of caspase-7-deficient macrophages to the intracellular pathogen is due to defective delivery of the organism to the lysosome and to delayed cell death during early stages of infection
malfunction
-
there is a significant decrease in the amount of mineralized tissue in caspase-7 knockout mice
physiological function
-
caspase-7 influences intramembranous and endochondral bone development
physiological function
-
caspase-7 is directly involved in functional cell differentiation and regulation of the mineralization of dental matrices
physiological function
-
caspase-7 is not essential for apoptosis in the primary enamel knot but possibly fulfills non-apoptotic functions in tooth development
physiological function
-
caspase-7 is required for apoptotic cell detachment and contributes to reactive oxygen species production
physiological function
-
caspase-7 plays a role in host defense against Legionella pneumophila. Caspase-7 activation during Legionella pneumophila infection restricts growth by promoting early macrophage death and efficient delivery of the organism to the lysosome
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CASP7_MOUSE
303
0
34061
Swiss-Prot
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
procaspase-7 is activated by caspase-1 cleavage to caspase-7
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison of phenotypes of caspase-7 with caspase-3 deficient cells, overview
additional information
-
contsruction of caspase-7-deficient mice, that show protection from endotoxin-induced lymphocyte apoptosis and improved survival, phenotype, overview
additional information
-
mice lacking caspase-7 and its macrophages allow substantial Legionella pneumophila replication, while wild-type mouse strains are restrictive to Legionella pneumophila infection
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the NcoI site of the pET11d vector and expression in Escherichia coli BL21codon+
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
strong correlation between caspase-7 activity, normal brain development, and apoptotic DNA fragmenation in Casp3-/-mice, caspase-7 is a caspase-3 surrogate in Casp3-/-mice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strausberg R.L.; Feingold E.A.; Grouse L.H.; Derge J.G.; et al.
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
Proc. Natl. Acad. Sci. USA
99
16899-16903
2002
Homo sapiens (P55210), Mus musculus (P97864)
van de Craen, M.; Vandenabeele, P.; Declercq, W.; van den Brande, I.; van Loo, G.; Molemans, F.; Schotte, P.; van Criekinge, W.; Beyaert, R.; Fiers, W.
Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus (P97864)
Juan, T.S.C.; McNiece, I.K.; Argento, J.M.; Jenkins, N.A.; Gilbert, D.J.; Copeland, N.G.; Fletcher, F.A.
Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3
Genomics
40
86-93
1997
Homo sapiens (P55210), Homo sapiens, Mus musculus (P97864), Mus musculus
Behrensdorf, H.A.; van de Craen, M.; Knies, U.E.; Vandenabeele, P.; Clauss, M.
The endothelial monocyte-activating polypeptide II (EMAP II) is a substrate for caspase-7
FEBS Lett.
466
143-147
2000
Mus musculus
Houde, C.; Banks, K.G.; Coulombe, N.; Rasper, D.; Grimm, E.; Roy, S.; Simpson, E.M.; Nicholson, D.W.
Caspase-7 expanded function and intrinsic expression level underlies strain-specific brain phenotype of caspase-3-null mice
J. Neurosci.
24
9977-9984
2004
Homo sapiens, Mus musculus
Lamkanfi, M.; Moreira, L.O.; Makena, P.; Spierings, D.C.; Boyd, K.; Murray, P.J.; Green, D.R.; Kanneganti, T.D.
Caspase-7 deficiency protects from endotoxin-induced lymphocyte apoptosis and improves survival
Blood
113
2742-2745
2009
Mus musculus
Jen, C.Y.; Lin, C.Y.; Leu, S.F.; Huang, B.M.
Cordycepin induced MA-10 mouse Leydig tumor cell apoptosis through caspase-9 pathway
Evid. Based. Complement Alternat. Med.
2009
1-10
2009
Mus musculus
Akhter, A.; Gavrilin, M.A.; Frantz, L.; Washington, S.; Ditty, C.; Limoli, D.; Day, C.; Sarkar, A.; Newland, C.; Butchar, J.; Marsh, C.B.; Wewers, M.D.; Tridandapani, S.; Kanneganti, T.D.; Amer, A.O.
Caspase-7 activation by the Nlrc4/Ipaf inflammasome restricts Legionella pneumophila infection
PLoS Pathog.
5
e1000361
2009
Mus musculus, Mus musculus C57BL/6
Walsh, J.G.; Cullen, S.P.; Sheridan, C.; Luethi, A.U.; Gerner, C.; Martin, S.J.
Executioner caspase-3 and caspase-7 are functionally distinct proteases
Proc. Natl. Acad. Sci. USA
105
12815-12819
2008
Homo sapiens, Mus musculus
Matalova, E.; Vanden Berghe, T.; Svandova, E.; Vandenabeele, P.; Healy, C.; Sharpe, P.T.; Tucker, A.S.
Caspase-7 in molar tooth development
Arch. Oral Biol.
57
1474-1481
2012
Mus musculus
Brentnall, M.; Rodriguez-Menocal, L.; De Guevara, R.L.; Cepero, E.; Boise, L.H.
Caspase-9, caspase-3 and caspase-7 have distinct roles during intrinsic apoptosis
BMC Cell Biol.
14
32
2013
Mus musculus
Svandova, E.; Lesot, H.; Vanden Berghe, T.; Tucker, A.S.; Sharpe, P.T.; Vandenabeele, P.; Matalova, E.
Non-apoptotic functions of caspase-7 during osteogenesis
Cell Death Dis.
5
e1366
2014
Mus musculus
Matalova, E.; Lesot, H.; Svandova, E.; Vanden Berghe, T.; Sharpe, P.T.; Healy, C.; Vandenabeele, P.; Tucker, A.S.
Caspase-7 participates in differentiation of cells forming dental hard tissues
Dev. Growth Differ.
55
615-621
2013
Mus musculus
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