EC                 Enzyme                                 

cathepsin B;
cathepsin B1 (obsolete);
cathepsin II
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg! bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides
An intracellular (lysosomal) enzyme in peptidase family C1 (papain family)
EC created 1972
K01363  cathepsin B
HSA: 1508(CTSB)
PTR: 463993(CTSB)
PPS: 100987583(CTSB)
GGO: 101152544(CTSB)
PON: 100173564(CTSB)
NLE: 100604807(CTSB)
MCC: 100424758(CTSB)
MCF: 101865017(CTSB)
CSAB: 103215319(CTSB)
RRO: 104679114(CTSB)
RBB: 108536689(CTSB)
CJC: 100389833(CTSB)
SBQ: 101047879(CTSB)
MMU: 13030(Ctsb)
RNO: 64529(Ctsb)
CGE: 100756995(Ctsb)
NGI: 103729973(Ctsb)
HGL: 101709008(Ctsb)
CCAN: 109682023(Ctsb)
OCU: 100101593(CTSB)
TUP: 102483590(CTSB)
CFA: 486077(CTSB)
AML: 100476830(CTSB)
UMR: 103675931(CTSB)
ORO: 101375531(CTSB)
FCA: 101084873(CTSB)
PTG: 102968829(CTSB)
AJU: 106975817(CTSB)
BTA: 281105(CTSB)
BOM: 102284921(CTSB)
BIU: 109562776(CTSB)
PHD: 102344297(CTSB)
CHX: 102173295(CTSB)
OAS: 780470(CTSB)
SSC: 100037961(CTSB)
CFR: 102522938(CTSB)
CDK: 105101888(CTSB)
BACU: 102999231(CTSB)
LVE: 103090468(CTSB)
OOR: 101283436(CTSB)
ECB: 100060963(CTSB)
EPZ: 103558180(CTSB)
EAI: 106822582(CTSB)
MYB: 102240887(CTSB)
MYD: 102761828 102771390(CTSB)
HAI: 109379548(CTSB)
RSS: 109448132(CTSB)
PALE: 102883622(CTSB)
LAV: 100663899(CTSB)
TMU: 101341172
MDO: 100032681(CTSB)
SHR: 100920513(CTSB)
OAA: 100082449(CTSB)
GGA: 396329(CTSB)
MGP: 100544902(CTSB)
CJO: 107312410(CTSB)
APLA: 101794268(CTSB)
ACYG: 106038130(CTSB)
TGU: 100190482(CTSB)
GFR: 102045641(CTSB)
FAB: 101815778(CTSB)
PHI: 102102206(CTSB)
PMAJ: 107202448(CTSB)
CCW: 104696872(CTSB)
FPG: 101920597(CTSB)
FCH: 102059814(CTSB)
CLV: 102084749(CTSB)
EGZ: 104127263(CTSB)
AAM: 106483924(CTSB)
ASN: 102378401(CTSB)
AMJ: 102573171(CTSB)
PSS: 102453723(CTSB)
CMY: 102930234(CTSB)
CPIC: 101943093(CTSB)
ACS: 100563878(ctsb)
PVT: 110070450(CTSB)
PBI: 103051970(CTSB)
GJA: 107112866(CTSB)
XLA: 379257(ctsb.S) 380102(ctsb.L)
XTR: 394833(ctsb)
NPR: 108797919(CTSB)
DRE: 406645(ctsba) 569298(ctsbb)
IPU: 108269890(ctsb)
TRU: 101070919(ctsb) 101076659
OLA: 101160638(ctsb) 101165526
NFU: 107377587(ctsb) 107381178
CSEM: 103379409 103380823(ctsb)
HCQ: 109528616(ctsb)
BPEC: 110172821(ctsb)
SASA: 100195493(catb) 106607936(ctsb) 106611360(CATB)
ELS: 105015425(ctsb)
LCM: 102351271(CTSB)
CMK: 103171629(ctsb)
CIN: 100176002
DME: Dmel_CG10992(CtsB1)
DSI: Dsimw501_GD15875(Dsim_GD15875)
MDE: 101887961
AAG: 5580010
NVL: 108557216
BMOR: 692390
PMAC: 106710142
PRAP: 111001540
PXY: 105390633
API: 100144775(Catb-348) 100144778(Catb-1852) 100144780(Catb-912) 100144781(Catb-2744) 100144782(Catb-1418) 100144784(Catb-1674) 100144785(Catb-16a) 100144787(Catb-84) 100144788(Catb-5880) 100144790(Catb-3098) 100144791(Catb-16d2) 100144792(Catb-16d1) 100144794(Catb-1874) 100144795(Catb-3483) 100144796(Catb-10270) 100159094 100159833 100159850 100159943 100160743 100161139 100162979 100164098 100164982 100169466 100568543 100569565 103307611 103309588
ZNE: 110830373
CEL: CELE_C25B8.3(cpr-6) CELE_C52E4.1(cpr-1) CELE_F32H5.1(F32H5.1) CELE_F36D3.9(cpr-2) CELE_F44C4.3(cpr-4) CELE_F57F5.1(F57F5.1) CELE_T10H4.12(cpr-3) CELE_W07B8.1(cpr-8) CELE_W07B8.4(W07B8.4) CELE_W07B8.5(cpr-5)
CBR: CBG01102 CBG01103(Cbr-cpr-5) CBG01104 CBG10849(Cbr-cpr-6) CBG17499 CBG18635(Cbr-cpr-3) CBG18654 CBG18978(Cbr-cpr-4) CBG23343(Cbr-cpr-1) CBG23351
BMY: Bm1_33735
CRG: 105328916
OBI: 106873643
LAK: 106173360
CPAP: 110814176
CIT: 102614215
TCC: 18613845
EGR: 104434154
VRA: 106757800
VAR: 108329369
CCAJ: 109797052
ADU: 107492262
LJA: Lj0g3v0055079.1(Lj0g3v0055079.1) Lj1g3v4819970.1(Lj1g3v4819970.1)
FVE: 101292935
PPER: 18788067
PMUM: 103327235
PAVI: 110764573
MDM: 103405978
PXB: 103933562
ZJU: 107426196
CSV: 101206928
CMO: 103502979
MCHA: 111025675
CMAX: 111470792
CMOS: 111439194
CPEP: 111800718
RCU: 8270811
JCU: 105642738
VVI: 100267480
INI: 109152432
SIND: 105162975
DCR: 108203066
BVG: 104908565
SOE: 110794569
NNU: 104590324
OSA: 9267789
ATS: 109739673(LOC109739673) 109773816(LOC109773816) 109780250(LOC109780250)
SBI: 110432844
ZMA: 100283781(cl31697_1)
PDA: 103696640
EGU: 105034333
AOF: 109831962
ATR: 18430031
SMIN: v1.2.004193.t1(symbB.v1.2.004193.t1) v1.2.011583.t1(symbB.v1.2.011583.t1) v1.2.027715.t1(symbB.v1.2.027715.t1) v1.2.034047.t1(symbB.v1.2.034047.t1)
 » show all
1  [PMID:7458901]
Bond JS, Barrett AJ.
Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B.
Biochem. J. 189 (1980) 17-25.
2  [PMID:7043200]
Barrett AJ, Kirschke H.
Cathepsin B, Cathepsin H, and cathepsin L.
Methods. Enzymol. 80 Pt C (1981) 535-61.
3  [PMID:3312190]
Polgar L, Csoma C.
Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B.
J. Biol. Chem. 262 (1987) 14448-53.
Barrett, A.J., Buttle, D.J. and Mason, R.W.
Lysosomal cysteine proteinases.
ISI Atlas of Science. Biochemistry 1 (1988) 256-260.
5  [PMID:3342870]
Kirschke H, Wikstrom P, Shaw E.
Active center differences between cathepsins L and B: the S1 binding region.
FEBS. Lett. 228 (1988) 128-30.
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 9047-22-7

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