KEGG   ENZYME: 3.4.22.1Help
Entry
EC 3.4.22.1                 Enzyme                                 

Name
cathepsin B;
cathepsin B1 (obsolete);
cathepsin II
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
An intracellular (lysosomal) enzyme in peptidase family C1 (papain family)
History
EC 3.4.22.1 created 1972
Orthology
K01363  
cathepsin B
Genes
HSA: 
1508(CTSB)
PTR: 
463993(CTSB)
PPS: 
100987583(CTSB)
GGO: 
101152544(CTSB)
PON: 
100173564(CTSB)
MCC: 
100424758(CTSB)
MCF: 
101865017(CTSB)
MMU: 
13030(Ctsb)
RNO: 
64529(Ctsb)
CGE: 
HGL: 
101709008(Ctsb)
TUP: 
102483590(CTSB)
CFA: 
486077(CTSB)
AML: 
FCA: 
101084873(CTSB)
PTG: 
102968829(CTSB)
BTA: 
281105(CTSB)
BOM: 
102284921(CTSB)
PHD: 
102344297(CTSB)
CHX: 
102173295(CTSB)
SSC: 
100037961(CTSB)
CFR: 
102522938(CTSB)
ECB: 
100060963(CTSB)
MYB: 
102240887(CTSB)
MYD: 
102771390(CTSB)
PALE: 
102883622(CTSB)
MDO: 
SHR: 
100920513(CTSB)
OAA: 
GGA: 
396329(CTSB)
MGP: 
TGU: 
FAB: 
101815778(CTSB)
PHI: 
102102206(CTSB)
APLA: 
101794268(CTSB)
FPG: 
101920597(CTSB)
FCH: 
102059814(CTSB)
CLV: 
102084749(CTSB)
ASN: 
102378401(CTSB)
PSS: 
102453723(CTSB)
CMY: 
102930234(CTSB)
ACS: 
XLA: 
379257(ctsb) 380102(cg10992)
XTR: 
394833(ctsb)
DRE: 
406645(ctsba) 569298(ctsbb)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102351271(CTSB)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
TCA: 
BMOR: 
API: 
100144775(Catb-348)
ISC: 
CEL: 
CELE_C52E4.1(cpr-1) CELE_F32H5.1(F32H5.1) CELE_F44C4.3(cpr-4) CELE_T10H4.12(cpr-3) CELE_W07B8.1(W07B8.1) 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: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
MTR: 
CAM: 
FVE: 
CSV: 
RCU: 
POP: 
POPTR_0002s18500g(POPTRDRAFT_644702) POPTR_0002s18510g(POPTRDRAFT_552399)
VVI: 
SLY: 
SOT: 
OSA: 
OBR: 
BDI: 
ZMA: 
100283781(cl31697_1)
SITA: 
ATR: 
s00045p00036790(AMTR_s00045p00036790)
SMO: 
OLU: 
OTA: 
MIS: 
MPP: 
MBR: 
DDI: 
DPP: 
DFA: 
ACAN: 
TGO: 
TET: 
PTM: 
EHX: 
GTT: 
NGR: 
GLA: 
 » show all
Taxonomy
Reference
1  [PMID:7458901]
  Authors
Bond JS, Barrett AJ.
  Title
Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B.
  Journal
Biochem. J. 189 (1980) 17-25.
  Organism
Oryctolagus cuniculus
Reference
2  [PMID:7043200]
  Authors
Barrett AJ, Kirschke H.
  Title
Cathepsin B, Cathepsin H, and cathepsin L.
  Journal
Methods. Enzymol. 80 Pt C (1981) 535-61.
Reference
3  [PMID:3312190]
  Authors
Polgar L, Csoma C.
  Title
Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B.
  Journal
J. Biol. Chem. 262 (1987) 14448-53.
  Organism
Sus scofa
Reference
4
  Authors
Barrett, A.J., Buttle, D.J. and Mason, R.W.
  Title
Lysosomal cysteine proteinases.
  Journal
ISI Atlas of Science. Biochemistry 1 (1988) 256-260.
Reference
5  [PMID:3342870]
  Authors
Kirschke H, Wikstrom P, Shaw E.
  Title
Active center differences between cathepsins L and B: the S1 binding region.
  Journal
FEBS. Lett. 228 (1988) 128-30.
  Organism
Rattus norvegicus
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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