Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 18.104.22.168
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|Apoptotic protease Mch-3.|
|ICE-like apoptotic protease 3.|
|Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-|
- Caspase-7 is an effector/executioner caspase, as are caspase-3
(EC 22.214.171.124) and caspase-6 (EC 126.96.36.199).
- These caspases are responsible for the proteolysis of the majority of
cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)),
which lead to the apoptotic phenotype.
- Although a hydrophobic residue at P5 of caspase-2 (EC 188.8.131.52) and
caspase-3 leads to more efficient hydrolysis, the amino-acid residue
at this location in caspase-7 has no effect.
- Caspase-7 is activated by the initiator caspases (caspase-8
(EC 184.108.40.206), caspase-9 (EC 220.127.116.11) and caspase-10
- Removal of the N-terminal prodomain occurs before cleavage in the
linker region between the large and small subunits.
- Belongs to peptidase family C14.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
, with possibility to download in different formats, align etc.
entries corresponding to 3.4.22.-
entries corresponding to 3.4.-.-
entries corresponding to 3.-.-.-