EC                 Enzyme                                 

cathepsin X;
cathepsin B2;
cysteine-type carboxypeptidase;
cathepsin IV;
cathepsin Z;
acid carboxypeptidase;
lysosomal carboxypeptidase B
Acting on peptide bonds (peptidases);
Cysteine-type carboxypeptidases
BRITE hierarchy
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13.
EC created 1981, modified 2000
K08568  cathepsin X
HSA: 1522(CTSZ)
PTR: 736240(CTSZ)
PPS: 100978982(CTSZ)
GGO: 101135556(CTSZ)
PON: 100445547(CTSZ)
NLE: 100605843(CTSZ)
MCC: 694157(CTSZ)
MCF: 102118566(CTSZ)
CSAB: 103243445(CTSZ)
RRO: 104663800(CTSZ)
RBB: 108541622(CTSZ)
CJC: 100409242(CTSZ)
SBQ: 101044087(CTSZ)
MMU: 64138(Ctsz)
RNO: 252929(Ctsz)
CGE: 100689392(Ctsz)
NGI: 103741460(Ctsz)
HGL: 101720244(Ctsz)
CCAN: 109692783(Ctsz)
OCU: 100101623(CTSZ)
TUP: 102500911(CTSZ)
CFA: 611983(CTSZ)
AML: 100473166(CTSZ)
UMR: 103670963(CTSZ)
ORO: 101365974(CTSZ)
FCA: 101087983(CTSZ)
PTG: 102956771(CTSZ)
AJU: 106969919(CTSZ)
BTA: 404187(CTSZ)
BOM: 102265582(CTSZ)
BIU: 109567290(CTSZ)
PHD: 102340046(CTSZ)
CHX: 102175417(CTSZ)
OAS: 101101911(CTSZ)
SSC: 100141405(CTSZ)
CFR: 102515641(CTSZ)
CDK: 105095690(CTSZ)
BACU: 103013660(CTSZ)
LVE: 103085943(CTSZ)
OOR: 101287339(CTSZ)
ECB: 100056600(CTSZ)
EPZ: 103565404(CTSZ)
EAI: 106825078(CTSZ)
MYB: 102242643(CTSZ)
MYD: 102770003(CTSZ)
HAI: 109380091(CTSZ)
RSS: 109461159(CTSZ)
PALE: 102884357(CTSZ)
LAV: 100655776(CTSZ)
TMU: 101347887
MDO: 100027054(CTSZ)
SHR: 100927306(CTSZ)
OAA: 100080444(CTSZ)
GGA: 419311(CTSZ)
MGP: 100550055(CTSZ)
CJO: 107323052(CTSZ)
APLA: 101804246(CTSZ)
ACYG: 106040695(CTSZ)
TGU: 100222997(CTSZ) 100225523
GFR: 102041571(CTSZ)
FAB: 101818266(CTSZ)
PHI: 102103433(CTSZ)
PMAJ: 107213248(CTSZ)
CCW: 104687808(CTSZ)
FPG: 101921980(CTSZ)
FCH: 102059599(CTSZ)
CLV: 102084569(CTSZ)
EGZ: 104130672(CTSZ)
AAM: 106492788(CTSZ)
ASN: 102384346(CTSZ)
AMJ: 102561646(CTSZ)
PSS: 102447291(CTSZ)
CMY: 102934401(CTSZ)
CPIC: 101938312(CTSZ)
PVT: 110084725 110084731(CTSZ)
PBI: 103065322(CTSZ) 103065568
GJA: 107111924(CTSZ) 107111931
XLA: 432187 494800(ctsz.S)
XTR: 100127597(ctsz)
NPR: 108802340(CTSZ)
DRE: 450022(ctsz)
IPU: 108272968(ctsz) 108280169
TRU: 101077965(ctsz)
NCC: 104948760 104954748(ctsz)
OLA: 101156316(ctsz) 101171361
SASA: 106565426(CATZ) 106569716 106583261(CATZ)
ELS: 105016941(ctsz) 105030515
SFM: 108928420(ctsz) 108930071
LCM: 102354050(CTSZ)
CMK: 103171603(ctsz)
SKO: 102804623
CEL: CELE_F32B5.8(cpz-1) CELE_M04G12.2(cpz-2)
CBR: CBG04105(Cbr-cpz-1) CBG06727(Cbr-cpz-2)
TSP: Tsp_10493
CRG: 105327153
MYI: 110453406
OBI: 106881834
LAK: 106156390
ADF: 107348434
PPP: 112282901
DFA: DFA_10566 DFA_10571(ctsZ)
SMIN: v1.2.007800.t1(symbB.v1.2.007800.t1) v1.2.023187.t1(symbB.v1.2.023187.t1)
 » show all
1  [PMID:10504234]
Nagler DK, Zhang R, Tam W, Sulea T, Purisima EO, Menard R
Human cathepsin X: A cysteine protease with unique carboxypeptidase activity.
Biochemistry. 38 (1999) 12648-54.
2  [PMID:9738465]
Nagler DK, Menard R.
Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions.
FEBS. Lett. 434 (1998) 135-9.
3  [PMID:9642240]
Santamaria I, Velasco G, Pendas AM, Fueyo A, Lopez-Otin C.
Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location.
J. Biol. Chem. 273 (1998) 16816-23.
4  [PMID:577]
McDonald JK, Ellis S.
On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1.
Life. Sci. 17 (1975) 1269-76.
5  [PMID:1122298]
Otto K, Riesenkonig H.
Improved purification of cathepsin B1 and cathepsin B2.
Biochim. Biophys. Acta. 379 (1975) 462-75.
6  [PMID:4429705]
Ninjoor V, Taylor SL, Tappel AL.
Purification and characterization of rat liver lysosomal cathepsin B2.
Biochim. Biophys. Acta. 370 (1974) 308-21.
Other DBs
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CAS: 37217-21-3

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