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 (Substrates Products
Substrates Products on EC 3.4.14.10 - tripeptidyl-peptidase II
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SUBSTRATE 
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
Ala-Ala-Ala-p-nitroanilide + H2O
Ala-Ala-Ala + p-nitroaniline
-
24% of the activity with Ala-Ala-Phe-p-nitroanilide
-
-
?
Ala-Ala-Phe 2-naphthylamide + H2O
Ala-Ala-Phe + 2-naphthylamine
-
at 41% the rate of Ala-Ala-Phe 7-amido-4-methylcoumarin
-
?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
Arg-Ala-(dehydro)Ala-Val-Ala + H2O
?
-
inhibitor, at 0.05% the rate of Arg-Arg-Ala-(phospho)Ser-Val-Ala hydrolysis
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val + H2O
?
-
the Ala-(phospho)Ser bond is cleaved at the same rate as that of Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
-
?
Arg-Arg-Ala-Ser-Val-Ala + H2O
Arg-Arg-Ala + Ser-Val-Ala
-
better substrate than the phosphorylated peptide
-
-
?
cholecystokinin-8-sulfate + H2O
Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2
-
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
major cleavage site: L-Arg, followed by cleavage at Ala-(phospho)Ser
-
?
Gly-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-Ser-Val-Ala
-
-
-
-
?
His-Leu-His 2-naphthylamide + H2O
His-Leu-His + 2-naphthylamine
-
at 12% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
KKE-5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid-Q9K-4'-dimethylaminoazobenzene-4'-sulfonyl + H2O
?
-
-
-
?
L-Ala-L-Ala-L-Phe-p-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + p-nitroaniline
-
-
-
?
Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Leu-Arg-Arg + Ala-(phospho)Ser-Val-Ala
-
poor substrate
-
-
?
Leu-Leu-Glu-Ala + H2O
Leu-Leu-Glu + Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
at 6% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Pro-Pro-Ala-p-nitroanilide + H2O
Pro-Pro-Ala-p-nitroaniline
-
12% of the activity with Ala-Ala-Phe-p-nitroanilide
-
-
?
Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Leu-Glu-Arg + H2O
Val-Gly-Ala + His-Ala-Gly + Glu-Tyr-Gly + Ala-Glu-Ala + Leu-Glu-Arg
-
peptide derived from human hemoglobin alpha-chain, residues 17-31, sequential release of tripeptides from free N-terminus, cleaved into 5 tripeptides by human enzyme, cleavage of Gly25-Ala bond occurs at a lower rate than Ala19-His and Gly22-Glu
-
?
Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Val-Leu-Arg + Arg-Ala-Ser-Val-Ala
-
-
the latter product is cleaved at a higher rate than the substrate
?
Val-Tyr-Ser 2-naphthylamide + H2O
Val-Tyr-Ser + 2-naphthylamine
-
at 3% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
best chromogenic tripeptyl substrate
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Drosophila sp. (in: flies)
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
-
-
-
-
?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O
Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O
Gly-Ser-His + Leu-Leu-Glu-Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O
Gly-Ser-His + Leu-Leu-Glu-Ala
sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Phe-L-Pro-p-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + p-nitroaniline
-
-
-
-
?
L-Ala-L-Phe-L-Pro-p-nitroanilide + H2O
L-Ala-L-Phe-L-Pro + p-nitroaniline
-
-
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide, aminoacyl or dipeptidyl methylcoumarylamides
-
-
?
additional information
?
-
-
no substrates are peptides with proline residues around cleavage sites
-
-
?
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
?
-
no activity against Q20RRGRR and KKQ30KK
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
additional information
?
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
additional information
?
-
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
additional information
?
-
tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all
-
-
?
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
?
-
-
TPP II additionally has an endopeptidase activity and is able to attack longer disordered peptides up to 75 amino acid residues.Three cleavage sites after proline residues are noted, the endopeptidase activity is more promiscuous than expected, and certainly different from the specificity of the exopeptidase activity. No carboxypeptidase activity has been detected
-
-
?
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
?
-
-
no substrates are Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala, guanidovaleric acid-Arg-Arg-Ala-(phospho)Ser-Val, guanidovaleric acid-Arg-Arg-Ala-Ser-Val, epsilon-aminohexanoic acid-Arg-Arg-Ala-Ser-Val
-
-
?
additional information
?
-
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
