KEGG ENZYME: 3.4.22.62

ENZYME: 3.4.22.62

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

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)

ORO:	101362812(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)

OOR:	101271677(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)

TMU:

101355103

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)

PMAJ:

107213687(CASP9)

CCW:	104697549(CASP9)

FPG:	101914844(CASP9)

FCH:	102054465(CASP9)

CLV:	102093506(CASP9)

EGZ:	104133155(CASP9)

AAM:	106493414(CASP9)

ASN:	102384999(CASP9)

AMJ:	102573968(CASP9)

PSS:	102443524(CASP9)

CMY:	102939753(CASP9)

CPIC:

101944555(CASP9)

ACS:	100560103(casp9)

PVT:	110072690(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:	107579230 107591141(casp9) 107593914

CCAR:

109048790 109103852

IPU:	108276164(casp9)

AMEX:

103034324

TRU:	101075121(casp9)

TNG:	GSTEN00020648G001

LCO:	104939007(casp9)

NCC:

104954971

MZE:	101487562(casp9)

OLA:	101157857(casp9)

XMA:	102226741(casp9)

PRET:

103467149(casp9)

NFU:	107386824 107390653

CSEM:

103385017(casp9)

LCF:	108882570(casp9)

HCQ:	109511699(casp9)

BPEC:

110167143(casp9)

SASA:

106567147 106572551(casp9)

ELS:	105028691(casp9)

SFM:	108939364(casp9)

LCM:	102362720(CASP9)

CMK:	103187647(casp9)

SPU:	586121 592436

APLC:

110979123 110979155

SKO:

100376094

CRG:

105325340

MYI:	110446169 110446170 110466239

LAK:	106168747 106170245 106171849

EPA:

ADF:

HMG:

AQU:

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

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:

3.4.22.62

IUBMB Enzyme Nomenclature:

3.4.22.62

ExPASy - ENZYME nomenclature database:

3.4.22.62

BRENDA, the Enzyme Database:

3.4.22.62

CAS:	180189-96-2

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Pathway (1)   
   KEGG MODULE (1)   
Gene (305)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (130)   
   KEGG MGENES (8)   
   RefGene (154)   
   EGENES (12)   
Protein sequence (63)   
   UniProt (3)   
   SWISS-PROT (2)   
   RefSeq(pep) (14)   
   PDBSTR (44)   
DNA sequence (18)   
   RefSeq(nuc) (15)   
   GenBank (2)   
   EMBL (1)   
3D Structure (4)   
   PDB (4)   
All databases (391)   

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