KEGG   ENZYME: 3.4.14.9Help
Entry
EC 3.4.14.9                 Enzyme                                 

Name
tripeptidyl-peptidase I;
tripeptidyl aminopeptidase;
tripeptidyl peptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Dipeptidyl-peptidases and tripeptidyl-peptidases
BRITE hierarchy
Reaction(IUBMB)
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
Comment
A lysosomal enzyme that is active at acidic pH. Deficient in classical late-infantile neuronal ceroid lipofuscinosis brain tissue. Belongs in peptidase family S53. Formerly included in EC 3.4.14.8.
History
EC 3.4.14.9 created 1992 (part of EC 3.4.14.8 created 1989, incorporated 1992), modified 2000, modified 2001, modified 2003
Orthology
K01279  
tripeptidyl-peptidase I
Genes
HSA: 
1200(TPP1)
PTR: 
450999(TPP1)
PPS: 
100969179(TPP1)
GGO: 
101149790(TPP1)
PON: 
100440001(TPP1)
MCC: 
MCF: 
101867272(TPP1)
MMU: 
12751(Tpp1)
RNO: 
83534(Tpp1)
CGE: 
100759190(Tpp1)
HGL: 
101707185(Tpp1)
TUP: 
102474485(TPP1)
CFA: 
485337(TPP1)
AML: 
FCA: 
101093296(TPP1)
PTG: 
102968271(TPP1)
BTA: 
515575(TPP1)
BOM: 
102279785(TPP1)
PHD: 
102332223(TPP1)
CHX: 
102176981(TPP1)
SSC: 
100623352(TPP1)
CFR: 
102512212(TPP1)
BACU: 
103017792(TPP1)
LVE: 
103084335(TPP1)
ECB: 
100070095(TPP1)
MYB: 
102249131(TPP1)
MYD: 
102763994(TPP1)
PALE: 
102887010(TPP1)
MDO: 
100030970(TPP1)
SHR: 
100918462(TPP1)
OAA: 
GGA: 
425576(TPP1)
TGU: 
100232321(TPP1)
FAB: 
101810332(TPP1)
PHI: 
102114063(TPP1)
APLA: 
101792345(TPP1)
FPG: 
101920803(TPP1)
FCH: 
102051334(TPP1)
CLV: 
102094093(TPP1)
ASN: 
102377067(TPP1)
AMJ: 
102560569(TPP1)
PSS: 
CMY: 
102933063(TPP1)
ACS: 
PBI: 
103059366(TPP1)
XLA: 
414505(tpp1)
XTR: 
100124868(tpp1)
DRE: 
798347(tpp1)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103185353(tpp1)
BFO: 
NVE: 
HMG: 
AQU: 
GSL: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_122124(AO090166000084) AOR_1_2392174(AO090005001380) AOR_1_386054(AO090011000235)
ANG: 
ANI_1_368124(An14g02470) ANI_1_676074(An08g04640)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
ZTR: 
PFJ: 
BCOM: 
PPL: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
PGR: 
MBR: 
DDI: 
DPP: 
DFA: 
ACAN: 
PIF: 
NGD: 
EHX: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:10349869]
  Authors
Ezaki J, Tanida I, Kanehagi N, Kominami E.
  Title
A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase.
  Journal
J. Neurochem. 72 (1999) 2573-82.
  Organism
Homo sapiens
Reference
2  [PMID:9989235]
  Authors
Rawlings ND, Barrett AJ.
  Title
Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis.
  Journal
Biochim. Biophys. Acta. 1429 (1999) 496-500.
  Organism
Homo sapiens, Rattus norvegicus
Reference
3  [PMID:10679303]
  Authors
Ezaki J, Takeda-Ezaki M, Oda K, Kominami E.
  Title
Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis.
  Journal
Biochem. Biophys. Res. Commun. 268 (2000) 904-8.
  Organism
Rattus norvegicus
Reference
4  [PMID:10617131]
  Authors
Junaid MA, Wu G, Pullarkat RK.
  Title
Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis.
  Journal
J. Neurochem. 74 (2000) 287-94.
  Organism
Bos taurus
Reference
5  [PMID:11054422]
  Authors
Lin L, Sohar I, Lackland H, Lobel P.
  Title
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.
  Journal
J. Biol. Chem. 276 (2001) 2249-55.
  Organism
Homo sapiens
  Sequence
[hsa:1200]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
151662-36-1

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