3.4.14.10: tripeptidyl-peptidase II
This is an abbreviated version!
For detailed information about tripeptidyl-peptidase II, go to the full flat file.
Word Map on EC 3.4.14.10
-
3.4.14.10
-
exopeptidase
-
tppii
-
ceroid
-
butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
-
cholecystokinin-8
-
gly-pro-x
-
medicine
- 3.4.14.10
-
exopeptidase
- tppii
-
ceroid
- butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
- cholecystokinin-8
-
gly-pro-x
- medicine
Reaction
Release of an N-terminal tripeptide from a polypeptide =
Synonyms
aminopeptidase, tripeptidyl, II, cholecystokinin-inactivating peptidase, dTPP II, EC 3.4.14.8, hTPP II, mTPP II, PTP-A, TPII, TPP, TPP II, TPP-2, TPP-II, TPP2, TPPII, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl aminopeptidase I I, tripeptidyl aminopeptidase II, tripeptidyl peptidase, tripeptidyl peptidase II, tripeptidyl-peptidase-II, tripeptidylpeptidase II, TY-21 TPP
ECTree
3.4.14.10 tripeptidyl-peptidase IIAdvanced search results
results (
results (Natural Substrates Products
Natural Substrates Products on EC 3.4.14.10 - tripeptidyl-peptidase II
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
-
-
?
additional information
?
-
-
the enzyme is important for the degradation of some specific substrates, e.g. the neuropeptide cholecystokinin. It is likely that the main biological function of tripeptidyl-peptidase II is to participate in a general intracellular protein turnover. This peptidase may act on oligopeptides generated by the proteasome, or other endopeptidases, and the tripeptides formed would subsequently be good substrates for other exopeptidases. Tripeptidyl-peptidase II activity is increased in sepsis-induced muscle wasting, a situation of enhanced protein turnover
-
-
?
additional information
?
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
-
TPPII plays an important role in antigen processing, as most proteasomal products require further processing by TPPII for MHC class I presentation. As a consequence, peptide generation for MHCclass I is severely hampered when TPPII activitis inhibited
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
additional information
?
-
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
-
the activities of both the proteasome and PTTII are regulated in a parallel manner in cancer cachexia, and both are induced by the same factor and probably have the same intracellular signalling pathways and transcription factors
-
-
?
additional information
?
-
-
PTP-A cleaves Xaa-Xaa-Pro-Yaa-(Xaa)n between Pro and Yaa, where Yaa represents any residue except proline, and Zaa represents any residue except glycine, proline, or a charged residue
-
-
?
additional information
?
-
-
PTP-A cleaves Xaa-Xaa-Pro-Yaa-(Xaa)n between Pro and Yaa, where Yaa represents any residue except proline, and Zaa represents any residue except glycine, proline, or a charged residue
-
-
?
additional information
?
-
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
