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)
CSAB: 103236614(CASP3)
RRO: 104666783 104673791(CASP3)
RBB: 108512689
CJC: 100387570(CASP3)
SBQ: 101029697(CASP3)
MMU: 12367(Casp3)
RNO: 25402(Casp3)
CGE: 100689061(Casp3)
NGI: 103744668 103750475(Casp3)
OCU: 100008840(CASP3)
TUP: 102472926(CASP3) 102487119
CFA: 403567(CASP3)
AML: 100469056(CASP3)
UMR: 103680991(CASP3)
ORO: 101371336(CASP3)
FCA: 493932(CASP3)
PTG: 102954729(CASP3)
AJU: 106979326(CASP3)
BTA: 408016(CASP3)
BOM: 102287348(CASP3)
BIU: 109553316(CASP3)
PHD: 102334771(CASP3)
CHX: 102177031(CASP3)
OAS: 443031(CASP3)
SSC: 397244(CASP3)
CFR: 102520133(CASP3)
CDK: 105084433(CASP3)
BACU: 103019939(CASP3)
LVE: 103073819(CASP3)
OOR: 101289847(CASP3)
ECB: 100034083(CASP3)
EPZ: 103549132(CASP3)
EAI: 106830081(CASP3)
MYB: 102258599(CASP3)
MYD: 102760961(CASP3)
HAI: 109395706(CASP3)
RSS: 109449637(CASP3)
PALE: 102897289(CASP3)
LAV: 100672256(CASP3)
TMU: 101354307
MDO: 654273(CASP3) 654275
SHR: 100922500(CASP3) 100922757
OAA: 100087105(CASP3)
GGA: 395476(CASP3)
MGP: 100548182(CASP3)
CJO: 107313280(CASP3)
APLA: 101805296(CASP3)
ACYG: 106035172(CASP3)
TGU: 100230799
GFR: 102035830(CASP3)
FAB: 101808212(CASP3)
PHI: 102104322(CASP3)
PMAJ: 107203069(CASP3)
CCW: 104690575(CASP3)
FPG: 101913355(CASP3)
FCH: 102056397(CASP3)
CLV: 102089427(CASP3)
EGZ: 104129473(CASP3)
AAM: 106484082(CASP3)
ASN: 102383553(CASP3)
AMJ: 102572621(CASP3) 102576234(CASP14)
PSS: 102463828(CASP3)
CMY: 102942062(CASP3)
CPIC: 101948246(CASP3)
ACS: 100563931(casp3)
PVT: 110083865(CASP3)
PBI: 103049711(CASP3)
GJA: 107115654(CASP3)
XLA: 100036910(casp3.L) 397720(casp3.S)
XTR: 100151728(casp3)
DRE: 140621(casp3a) 566604(casp3b)
IPU: 100528811(casp3) 108260860
TRU: 446083(casp3)
LCO: 104928227 104936945(caspase-3)
NCC: 104959742 104967108(casp3)
OLA: 100049215(casp3) 100049265
NFU: 107390752(casp3) 107397381
CSEM: 103383467 103391460(casp3)
SASA: 100194892(casp3) 106602722(CASP3) 106612018
ELS: 105006735(casp3) 105029385(casp3)
SFM: 108924572(casp3)
LCM: 106705928(CASP3)
CMK: 103187405(casp3)
SKO: 102802674
CRG: 105326608
MYI: 110452312
SHX: MS3_07622
EPA: 110247107
 » 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 39:16056-63 (2000)
DOI:10.1021/bi001007w
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 272:21010-7 (1997)
DOI:10.1074/jbc.272.34.21010
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 360:654-66 (2006)
DOI:10.1016/j.jmb.2006.05.041
Reference
5  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol Mol Biol Rev 64:821-46 (2000)
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 15:2407-16 (1996)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.56
IUBMB Enzyme Nomenclature: 3.4.22.56
ExPASy - ENZYME nomenclature database: 3.4.22.56
BRENDA, the Enzyme Database: 3.4.22.56
CAS: 169592-56-7

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