KEGG   ENZYME: 3.4.22.62Help
Entry
EC 3.4.22.62                Enzyme                                 

Name
caspase-9;
CASP-9;
ICE-like apoptotic protease 6;
ICE-LAP6;
apoptotic protease Mch-6;
apoptotic protease-activating factor 3;
APAF-3
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp!Xaa
Comment
Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63) [1]. Caspase-9 contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [1]. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2 [1]. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo [1]. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage [2,3]. Procaspase-3 is the enzyme's physiological substrate [2]. Belongs in peptidase family C14.
History
EC 3.4.22.62 created 2007
Orthology
K04399  
caspase 9
Genes
HSA: 
842(CASP9)
PTR: 
456457(CASP9)
PPS: 
100992567(CASP9)
GGO: 
101130414(CASP9)
PON: 
100460459(CASP9)
NLE: 
100597173(CASP9)
MCC: 
694544(CASP9)
MCF: 
102126830(CASP9)
CSAB: 
103225550(CASP9)
RRO: 
104677696(CASP9)
RBB: 
108524269(CASP9)
CJC: 
100409028(CASP9)
SBQ: 
101051525(CASP9)
MMU: 
12371(Casp9)
RNO: 
58918(Casp9)
CGE: 
100689370 103160479
NGI: 
103725336(Casp9)
HGL: 
101702898(Casp9)
CCAN: 
109692548(Casp9)
OCU: 
100101592(CASP9)
TUP: 
102470940(CASP9)
CFA: 
487432(CASP9)
AML: 
100483760(CASP9)
UMR: 
103666628(CASP9)
FCA: 
768260(CASP9)
PTG: 
102967404(CASP9)
AJU: 
106975594(CASP9)
BTA: 
100140945(CASP9)
BOM: 
102268660(CASP9)
BIU: 
109570433(CASP9)
PHD: 
102336217(CASP9)
CHX: 
102174681(CASP9)
OAS: 
101110953(CASP9)
SSC: 
100518913(CASP9)
CFR: 
102519816(CASP9)
CDK: 
105107056(CASP9)
BACU: 
103010071(CASP9)
LVE: 
103086745(CASP9)
ECB: 
100054331(CASP9)
EPZ: 
103565016(CASP9)
EAI: 
106828005(CASP9)
MYB: 
102254877(CASP9)
MYD: 
102759481(CASP9)
HAI: 
109381302(CASP9)
RSS: 
109459000(CASP9)
PALE: 
102878565(CASP9)
LAV: 
100656597(CASP9)
MDO: 
100027338(CASP9)
SHR: 
100931481(CASP9)
OAA: 
100092345(CASP9)
GGA: 
426970(CASP9)
MGP: 
100550410(CASP9)
CJO: 
107323418(CASP9)
APLA: 
101795386(CASP9)
ACYG: 
106040238(CASP9)
TGU: 
100227981(CASP9)
GFR: 
102039030(CASP9)
FAB: 
101808292(CASP9)
PHI: 
102108950(CASP9)
CCW: 
104697549(CASP9)
FPG: 
101914844(CASP9)
FCH: 
102054465(CASP9)
CLV: 
102093506(CASP9)
AAM: 
106493414(CASP9)
ASN: 
102384999(CASP9)
AMJ: 
102573968(CASP9)
PSS: 
102443524(CASP9)
CMY: 
102939753(CASP9)
CPIC: 
101944555(CASP9)
ACS: 
100560103(casp9)
PBI: 
103063403(CASP9)
GJA: 
107124463(CASP9)
XLA: 
373560(casp9.S)
XTR: 
100144708(casp9)
NPR: 
108797190(CASP9)
DRE: 
492763(casp9)
SRX: 
107716147 107737696
SANH: 
107673102 107687452
SGH: 
107591141(casp9) 107593914
IPU: 
108276164(casp9)
TRU: 
101075121(casp9)
TNG: 
GSTEN00020648G001
LCO: 
104939007(casp9)
NCC: 
104954971
MZE: 
101487562(casp9)
OLA: 
101157857(casp9)
XMA: 
102226741(casp9)
CSEM: 
103385017(casp9)
LCF: 
108882570(casp9)
SASA: 
106567147 106572551(casp9)
ELS: 
105028691(casp9)
SFM: 
108939364(casp9)
LCM: 
102362720(CASP9)
CMK: 
103187647(casp9)
SPU: 
586121 592436
SKO: 
100376094
CRG: 
105325340
LAK: 
106168207 106168747 106170245 106171849 106173374
ADF: 
107343798
HMG: 
101235218
AQU: 
100633941
 » 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  [PMID:16630893]
  Authors
Yin Q, Park HH, Chung JY, Lin SC, Lo YC, da Graca LS, Jiang X, Wu H.
  Title
Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.
  Journal
Mol. Cell. 22 (2006) 259-68.
Reference
3  [PMID:12620239]
  Authors
Boatright KM, Renatus M, Scott FL, Sperandio S, Shin H, Pedersen IM, Ricci JE, Edris WA, Sutherlin DP, Green DR, Salvesen GS.
  Title
A unified model for apical caspase activation.
  Journal
Mol. Cell. 11 (2003) 529-41.
Reference
4
  Authors
Salvesen, G.S. and Boatright, K.M.
  Title
Caspase-9.
  Journal
In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p. 1296-1298.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
180189-96-2
DBGET integrated database retrieval system