KEGG   ENZYME: 3.4.22.56Help
Entry
EC 3.4.22.56                Enzyme                                 

Name
caspase-3;
CPP32;
apopain;
yama protein
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp! with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Comment
Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60) [5]. 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 [3,5]. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B [1]. Caspase-3 can activate procaspase-2 (EC 3.4.22.55) [2]. Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain [6]. Although Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate [4]. Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp! is a better substrate than Asp-Val-Ala-Asp! . This is not the case for caspase-7 [4]. Belongs in peptidase family C14.
History
EC 3.4.22.56 created 2007
Orthology
K02187  
caspase 3
Genes
HSA: 
836(CASP3)
PTR: 
461669(CASP3)
PPS: 
100974934(CASP3)
GGO: 
101126742(CASP3)
PON: 
100435491(CASP3)
NLE: 
100585064(CASP3)
MCC: 
694473(CASP3)
MCF: 
102144182(CASP3)
CJC: 
100387570(CASP3)
MMU: 
12367(Casp3)
RNO: 
25402(Casp3)
CGE: 
100689061(Casp3)
HGL: 
101712867(Casp3)
TUP: 
102472926(CASP3)
CFA: 
403567(CASP3)
AML: 
FCA: 
493932(CASP3)
PTG: 
102954729(CASP3)
BTA: 
408016(CASP3)
BOM: 
102287348(CASP3)
PHD: 
102334771(CASP3)
CHX: 
102177031(CASP3)
OAS: 
443031(CASP3)
SSC: 
397244(CASP3)
CFR: 
102520133(CASP3)
BACU: 
103019939(CASP3)
LVE: 
103073819(CASP3)
ECB: 
100034083(CASP3)
MYB: 
102258599(CASP3)
MYD: 
102760961(CASP3)
PALE: 
102897289(CASP3)
MDO: 
SHR: 
OAA: 
100087105(CASP3)
GGA: 
395476(CASP3)
MGP: 
APLA: 
101805296(CASP3)
TGU: 
FAB: 
101808212(CASP3)
PHI: 
102104322(CASP3)
FPG: 
101913355(CASP3)
FCH: 
102056397(CASP3)
CLV: 
102089427(CASP3)
ASN: 
AMJ: 
PSS: 
102463828(CASP3)
CMY: 
102942062(CASP3)
ACS: 
PBI: 
103049711(CASP3)
XLA: 
XTR: 
100151728(casp3)
DRE: 
140621(casp3a) 566604(casp3b)
TRU: 
446083(casp3)
MZE: 
OLA: 
XMA: 
CMK: 
ISC: 
SMM: 
AQU: 
 » show all
Taxonomy
Reference
1  [PMID:11123933]
  Authors
Krebs JF, Srinivasan A, Wong AM, Tomaselli KJ, Fritz LC, Wu JC.
  Title
Heavy membrane-associated caspase 3: identification, isolation, and characterization.
  Journal
Biochemistry. 39 (2000) 16056-63.
Reference
2  [PMID:9261102]
  Authors
Li H, Bergeron L, Cryns V, Pasternack MS, Zhu H, Shi L, Greenberg A, Yuan J.
  Title
Activation of caspase-2 in apoptosis.
  Journal
J. Biol. Chem. 272 (1997) 21010-7.
Reference
3
  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
4  [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
5  [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
6  [PMID:8665848]
  Authors
Martin SJ, Amarante-Mendes GP, Shi L, Chuang TH, Casiano CA, O'Brien GA, Fitzgerald P, Tan EM, Bokoch GM, Greenberg AH, Green DR.
  Title
The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism.
  Journal
EMBO. J. 15 (1996) 2407-16.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
169592-56-7

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