KEGG   ENZYME: 3.4.22.60Help
Entry
EC 3.4.22.60                Enzyme                                 

Name
caspase-7;
CASP-7;
ICE-like apoptotic protease 3;
ICE-LAP3;
apoptotic protease Mch-3;
Mch3;
CMH-1
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp!
Comment
Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59) [1]. These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype [2]. Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect [3]. Caspase-7 is activated by the initiator caspases [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits [4]. Belongs in peptidase family C14.
History
EC 3.4.22.60 created 2007
Orthology
K04397  
caspase 7
Genes
HSA: 
840(CASP7)
PTR: 
450745(CASP7)
PPS: 
100985952(CASP7)
GGO: 
101147760(CASP7)
PON: 
100435918(CASP7)
NLE: 
100591910(CASP7)
MCC: 
697633(CASP7)
MCF: 
102127213(CASP7)
CJC: 
100386577(CASP7)
MMU: 
12369(Casp7)
RNO: 
64026(Casp7)
CGE: 
100766857(Casp7)
HGL: 
101709568(Casp7)
TUP: 
102470949(CASP7)
CFA: 
486896(CASP7)
AML: 
UMR: 
103657312(CASP7)
FCA: 
768262(CASP7)
PTG: 
102951959(CASP7)
BTA: 
526279(CASP7)
BOM: 
102271384(CASP7)
PHD: 
102324332(CASP7)
CHX: 
100861343(CASP7)
OAS: 
101122741(CASP7)
CFR: 
102509752(CASP7)
BACU: 
103013605(CASP7)
LVE: 
103083104(CASP7)
ECB: 
100068258(CASP7)
MYB: 
102243767(CASP7)
MYD: 
102768516(CASP7)
PALE: 
102879606(CASP7)
MDO: 
100027500(CASP7)
SHR: 
100927801(CASP7)
OAA: 
100082745(CASP7)
GGA: 
423901(CASP7)
MGP: 
APLA: 
101799962(CASP7)
TGU: 
FAB: 
101807080(CASP7)
PHI: 
102112480(CASP7)
FPG: 
101911113(CASP7)
FCH: 
102047023(CASP7)
CLV: 
102084230(CASP7)
ASN: 
102375360(CASP7)
AMJ: 
102566884(CASP7)
PSS: 
CMY: 
102934687(CASP7)
ACS: 
100563813(casp7)
PBI: 
103054928(CASP7)
XLA: 
100037079(casp7) 397819(xcaspase-7)
XTR: 
549053(casp7) 733553
DRE: 
553634(casp7) 798445
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102357990(CASP7)
CMK: 
103172118(caspase-7) 103172119 103186582(casp7) 103187405(casp3)
BFO: 
ISC: 
HRO: 
LGI: 
SMM: 
HMG: 
TAD: 
 » show all
Taxonomy
Reference
1  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
Reference
2
  Authors
Nicholson, D. and Thornberry, N.A.
  Title
Caspase-3 and caspase-7.
  Journal
In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p. 1298-1302.
Reference
3  [PMID:16781734]
  Authors
Fang B, Boross PI, Tozser J, Weber IT.
  Title
Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition.
  Journal
J. Mol. Biol. 360 (2006) 654-66.
Reference
4  [PMID:12824163]
  Authors
Denault JB, Salvesen GS.
  Title
Human caspase-7 activity and regulation by its N-terminal peptide.
  Journal
J. Biol. Chem. 278 (2003) 34042-50.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
189258-14-8

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