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Information on EC 3.4.14.10 - tripeptidyl-peptidase II
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3.4.14.10 tripeptidyl-peptidase IISpecify your search results
Word Map
- 3.4.14.10
-
exopeptidase
- tppii
-
ceroid
- butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
- cholecystokinin-8
-
gly-pro-x
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tripeptidyl peptidase, tripeptidyl-peptidase ii, ptp-a, tripeptidylpeptidase ii, dtpp ii, tripeptidyl aminopeptidase i, tpp-ii, tpp-2, ty-21 tpp, tripeptidyl-peptidase-ii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, tripeptidyl, II
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-
-
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cholecystokinin-inactivating peptidase
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-
-
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EC 3.4.14.8
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formerly, part transferred
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PTP-A
TPII
TPP
TPP II
TPPII
tripeptidyl aminopeptidase
tripeptidyl aminopeptidase II
tripeptidyl peptidase
tripeptidyl peptidase II
tripeptidylpeptidase II
TY-21 TPP
TPP II
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tripeptidyl aminopeptidase
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tripeptidyl aminopeptidase II
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tripeptidyl peptidase
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-
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tripeptidyl peptidase II
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal tripeptide from a polypeptide
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
101149-94-4
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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
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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
?
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the Ala-(phospho)Ser bond is cleaved at the same rate as that of Arg-Arg-Ala-(phospho)Ser-Val-Ala
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-
?
Arg-Arg-Ala-Ser-Val-Ala + H2O
Arg-Arg-Ala + Ser-Val-Ala
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better substrate than the phosphorylated peptide
-
-
?
cholecystokinin-8-sulfate + H2O
Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2
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-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
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-
-
?
Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-(phospho)Ser-Val-Ala
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major cleavage site: L-Arg, followed by cleavage at Ala-(phospho)Ser
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?
Gly-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Gly-Val-Leu + Arg-Arg-Ala-Ser-Val-Ala
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-
-
-
?
His-Leu-His 2-naphthylamide + H2O
His-Leu-His + 2-naphthylamine
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at 12% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
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?
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
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-
-
?
Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Leu-Arg-Arg + Ala-(phospho)Ser-Val-Ala
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poor substrate
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-
?
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
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-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
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at 6% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
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?
Pro-Pro-Ala-p-nitroanilide + H2O
Pro-Pro-Ala-p-nitroaniline
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12% of the activity with Ala-Ala-Phe-p-nitroanilide
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-
?
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
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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
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?
Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Val-Leu-Arg + Arg-Ala-Ser-Val-Ala
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the latter product is cleaved at a higher rate than the substrate
?
Val-Tyr-Ser 2-naphthylamide + H2O
Val-Tyr-Ser + 2-naphthylamine
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at 3% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
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?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
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-
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?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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best chromogenic tripeptyl substrate
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?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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-
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
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-
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
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-
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
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-
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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-
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Drosophila sp. (in: flies)
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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-
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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?
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
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-
-
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?
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
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-
?
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
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-
?
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
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-
?
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
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
-
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?
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
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-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
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?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
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-
-
?
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
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-
?
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
?
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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
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-
?
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
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-
?
additional information
?
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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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]butan-2-amine
-
IC50: 4 nM
(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]propan-2-amine
-
IC50: 6 nM
(2S)-1-[(2S)-2-(5-ethyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]-1-oxopropan-2-amine
-
IC50: 23 nM
2-amino-1-[2-(4-propyl-1H-imidazol-2-yl)-2,3-dihydroindol-1-yl]ethanone
-
IC50: 36 nM
Arg-Arg-Ala-(dehydro)Ala-Val-Ala
-
less effective than Arg-Ala-(dehydro)Ala-Val-Ala
Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
inhibits cleavage of Leu-Arg bond, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
diphenyl [1-([1-[(2S)-2-aminobutanoyl]-2,3-dihydro-1H-indole-2-carbonyl]amino)-3-methylbutyl]phosphonate
irreversible variant of butabindide. almost 60fold more potent than butabindide
Leu-Arg-Arg-Ala-(phospho)Ser-Val
-
weak, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
weak, Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala as substrate
Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
-
hydrolysis of Gly-Val-Leu-Arg-Arg-Ala-(phospho)Ser-Val-Ala
additional information
-
no inhibition by Val-Leu-Arg, isovaleryl-Val-Leu-Arg-Arg-Ala-Ser-Val-Ala, EDTA (with or without DTT)
-
additional information
no or poor inhibition by Streptomyces subtilisin inhibitor (SSI), API-2, 4-chloromercuribenzoate, 2,2'-dithiodipyridine, iodoacetate, talopeptin, Streptomyces pepsin inhibitor (S-PI), amastatin, bestatin, and arphamenine A
-
additional information
-
no or poor inhibition by Streptomyces subtilisin inhibitor (SSI), API-2, 4-chloromercuribenzoate, 2,2'-dithiodipyridine, iodoacetate, talopeptin, Streptomyces pepsin inhibitor (S-PI), amastatin, bestatin, and arphamenine A
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the subunits form an active complexwith a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassiciation is accompanied by a reactivation. At 30°C more than 7fold activation after 2 h. Arg-Arg-Ala and Ser-Val-Ala at 0.01 mM enhance reactivation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bone Resorption
Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen.
Bone Resorption
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption.
Burkitt Lymphoma
Down-regulation of proteolytic complexes following EBV activation in BL cells.
Burkitt Lymphoma
Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II.
Burkitt Lymphoma
The MAPK Signaling Cascade is a Central Hub in the Regulation of Cell Cycle, Apoptosis and Cytoskeleton Remodeling by Tripeptidyl-Peptidase II.
Neoplasms
Development, evaluation and application of tripeptidyl-peptidase II sequence signatures.
Neoplasms
Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle.
Neoplasms
MAP kinase-signaling controls nuclear translocation of tripeptidyl-peptidase II in response to DNA damage and oxidative stress.
Neoplasms
Retraction: Tripeptidyl-peptidase II controls DNA damage responses and in vivo ?-irradiation resistance of tumors. Cancer Research 2007;67:716574.
Neoplasms
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Neoplasms
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors.
Neurodegenerative Diseases
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
Tandem mass spectrometry assays of palmitoyl protein thioesterase 1 and tripeptidyl peptidase activity in dried blood spots for the detection of neuronal ceroid lipofuscinoses in newborns.
Neuronal Ceroid-Lipofuscinoses
Therapeutic landscape for Batten disease: current treatments and future prospects.
Sepsis
Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis.
tripeptidyl-peptidase ii deficiency
Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with tripeptidyl-peptidase II deficiency.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.88
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
0.44
Ala-Ala-Phe-7-amido-4-methylcoumarin
Drosophila sp. (in: flies)
-
pH 7.5, 30°C, recombinant enzyme
0.47
Ala-Ala-Phe-7-amido-4-methylcoumarin
Drosophila sp. (in: flies)
-
pH 7.5, 30°C, native enzyme
0.013
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
0.015
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
0.036
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
0.039
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
0.06
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
0.06
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
0.13
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 8.3, 37°C
0.058
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
0.074
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
0.11
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 8.3, 37°C
0.2
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.4, 37°C
0.25
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.6, 37°C
0.27
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.9, 37°C
0.3
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
0.013
L-Ala-L-Ala-L-Phe-p-nitroanilide
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
1
L-Ala-L-Ala-L-Phe-p-nitroanilide
mutant enzyme E331K, Km above 1.0 mM, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
1
L-Ala-L-Ala-L-Phe-p-nitroanilide
mutant enzyme E331Q, Km above 1.0 mM, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
43
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
0.74
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 8.3, 37°C
1.29
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
1.3
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
1.42
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
1.5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
7.2
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000006
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.000021
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant D387G
0.000021
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.000036
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant D387G
0.000006
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant D387G
0.000012
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant D387G
0.000022
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant D387G
0.000023
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant D387G
48.9
Ala-Ala-Phe-4-nitroanilide
pH 7.5, 37°C, recombinant enzyme
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.4, 37°C
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.9, 37°C
30
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 6.8, 37°C
36
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant D387G, pH 7.6, 37°C
12
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.9, 37°C
22
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.8, 37°C
23
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 7.6, 37°C
30
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant D387G, pH 6.4, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki-value above 5 mM: Met-Met-OH, Asp-Tyr-OH, PhCH2-Val-Nvl-OH, PhCH2OCO-Val-Nvl-OH, CH3-Nl2-Nle-OCH3. Ki-value above 3.0 mM: CH3-Nle-Nle-NHCH3, PhCH2-Nle-Nle-NHCH3, PhCH2OCO-Val-Nle-O(CH2)3CH3. Ki-value above 0.5 mM: CH3CO-Val-Nvl-OH
-
0.000011
butabindide
wild type enzyme, using 0.2 mM of substrate L-Ala-L-Ala-L-Phe-p-nitroanilide, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
0.000015
butabindide
wild type enzyme, using 0.02 mM of substrate L-Ala-L-Ala-L-Phe-p-nitroanilide, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
0.14
butabindide
mutant enzyme E331Q, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
0.001
L-Val-L-Leu-L-Arg-L-Arg-L-Ala-L-Ser-L-Val-L-Ala
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
2
L-Val-L-Leu-L-Arg-L-Arg-L-Ala-L-Ser-L-Val-L-Ala
mutant enzyme E331Q, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000004
(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]butan-2-amine
Rattus norvegicus
-
IC50: 4 nM
0.000006
(2S)-1-oxo-1-[(2S)-2-(5-propyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]propan-2-amine
Rattus norvegicus
-
IC50: 6 nM
0.000023
(2S)-1-[(2S)-2-(5-ethyl-1H-imidazol-2-yl)-2,3-dihydro-1H-indol-1-yl]-1-oxopropan-2-amine
Rattus norvegicus
-
IC50: 23 nM
0.000036
2-amino-1-[2-(4-propyl-1H-imidazol-2-yl)-2,3-dihydroindol-1-yl]ethanone
Rattus norvegicus
-
IC50: 36 nM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15.7
pH 7.5, 37°C, purified recombinant enzyme, substrate Ala-Ala-Phe-4-nitroanilide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
additional information
additional information
-
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
additional information
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
additional information
-
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
additional information
-
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
additional information
isoform TPP II has a bell-shaped pH dependence of kcat app/KM probably due to deprotonation of the N-terminal amino group of the substrate at higher pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
647140, 647141, 647142, 647143, 647144, 647145, 647147, 647148, 647149, 647150, 647152, 647153, 647158
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high amounts of TPPII mRNA are detected in neocortex, especially in the frontal region and the hippocampus
brenda
-
high amounts of TPPII mRNA are detected in neocortex, especially in the frontal region and the hippocampus
brenda
the extracellular enzyme is produced by the bacterium Streptomyces herbaricolor strain TY-21 during the late stationary growth phase
brenda
-
the extracellular enzyme is produced by the bacterium Streptomyces herbaricolor strain TY-21 during the late stationary growth phase
-
brenda
-
higher specific activity in extracts from embryos as compared with adult
brenda
-
-
brenda
-
CD8 T cell lines specific are generated from spleen cells from Listeria monocytogenes-infected BALB/c mice 2 weeks after infection
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
radiation does not lead to nuclear translocation of TPPII
-
brenda
-
-
brenda
-
PTP-A is secreted to the surface of the outer membrane
brenda
-
PTP-A is secreted to the surface of the outer membrane
-
brenda
-
cholecystokinin-8-inactivating peptidase is a membrane bound isoform
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
the enzyme belongs to the peptidase S8 family. TY-21 TPP shows no homology with mammalian TPPII, but shows relatively higher homology with TPP S (49%). Alignment of the protein sequences of TY-21 TPP with TPP S and subtilisin reveal three conserved regions around the catalytic triad in the active site in these enzymes that are specific for subtilisin
evolution
-
the enzyme belongs to the peptidase S8 family. TY-21 TPP shows no homology with mammalian TPPII, but shows relatively higher homology with TPP S (49%). Alignment of the protein sequences of TY-21 TPP with TPP S and subtilisin reveal three conserved regions around the catalytic triad in the active site in these enzymes that are specific for subtilisin
-
malfunction
cell lines from primary fibroblasts are generated having conditional (floxed) TPPII alleles, transformed with both the c-myc and H-ras oncogenes. TPPII is deleted using retroviral self-deleting Cre recombinase. Clonally derived TPPIIflox/flox and TPPII-/- transformed fibroblasts show no influences of TPPII expression on basal cell survival and proliferation, nor on radiation-induced p53 activation, p21 induction, cell cycle arrest, apoptosis, or clonogenic cell death
malfunction
suppression of TPP2 expression with shRNA significantly inhibits cellular proliferation compared with the control cells
physiological function
-
it is demonstrated that both, the proteasome and TPPII play a role in the processing of Listeria monocytogenes-derived antigenic peptides
physiological function
isoform TPPII can regulate sperm maturation by modulating intracellular Ca2+ stores via the type 3 ryanodine receptor. Tripeptidyl peptidase II antagonists strongly activate the cAMP/PKA signaling pathway that drives sperm capacitation-associated protein tyrosine phosphorylation. In the absence of Ca2+, TPPII antagonists elevate the intracellular Ca2+ levels in sperm, resulting in a marked improvement in sperm movement, capacitation, acrosome reaction, and the in vitro fertilizing ability. This antagonist-induced release of intracellular Ca2+ can be blocked by the inhibitors of ryanodine receptors which are the main intracellular Ca2+ channels responsible for releasing stored Ca2+
physiological function
-
isoform TPPII physically interacts with the tumor suppressor MYBBP1A and the cell cycle regulator protein CDK2. HEK-293 cells overexpressing TPPII form highly enzymatically active oligomeric complexes, and the cytoplasmic interaction frequency of TPPII with MYBBP1A increases with the protein expression of TPPII in serum-free cell growth conditions. A specific reversible inhibitor of TPPII, butabindide, suppresses the cytoplasmic interactions of TPPII and MYBBP1A both in control HEK-293 and cells overexpressing murine TPPII. A gene expression study during anoikis shows that overexpression of TPP II decreases mRNA expression level of MYBBP1A at the cell detachment conditions
physiological function
TPP II is involved in the fertilization process. The increased intercellular Ca2+ level induced by TPPII antagonists via RyR3 (ryanodine receptor) represents a mechanism of activation of sperm
physiological function
-
in the absence of proteasome inhibitor BSc2118, TPPII is diffusely dispersed within the cytoplasm of C-26 colon adenocarcinoma cells. The proteasome and ubiquitin-rich perinuclear region do not display enhanced TPPII staining. When proteasome function is impaired by the inhibitor, TPPII associates more closely with both the proteasome and polyubiquitinated. TPPII is dynamically recruited into the developing aggresome: TPPII in the early aggresome is dispersed within the central part but subsequently aggregated on the surface of this structure
physiological function
TPP2 inhibition indirectlybut rapidly decreases the levels of active, diphosphorylated extracellular signal-regulated kinase ERK1 and ERK2 in the nucleus, thereby down-regulating signal transduction downstream of growth factors and mitogenic stimuli. TPP2 inhibition of neurons in the hippocampus leads to an excessive strengthening of synapses
physiological function
TPPII, assembles to form a spindle-shaped complex of about 6 MDa. Dependent on protein concentration, TPPII has a distinct tendency for polymorphism. Two different assembly states (36-mers and 32-mers) coexist as well as occasional extended forms with longer strands. TPPII and 26S proteasomes spatially associate in agreement with TPPII's role in postproteasomal degradation
physiological function
tripeptidyl peptidases (TPPs) are unique exopeptidases that cleave tripeptide units from oligopeptides or polypeptides. It is required to degrade unnecessary proteins in cells for sustaining life. In this process, TPP plays an important role and is present in lysosomes and the cytosol. There are two kinds of TPPs in mammals, TPPI (EC 3.4.14.9) and TPPII (EC 3.4.14.10)
physiological function
-
tripeptidyl peptidases (TPPs) are unique exopeptidases that cleave tripeptide units from oligopeptides or polypeptides. It is required to degrade unnecessary proteins in cells for sustaining life. In this process, TPP plays an important role and is present in lysosomes and the cytosol. There are two kinds of TPPs in mammals, TPPI (EC 3.4.14.9) and TPPII (EC 3.4.14.10)
-
Show AA Sequence and Transmembrane Helices (2690 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000000
138000
additional information
138000
-
x * 138000, the subunits form an active complex with a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation is accompanied by a reactivation
additional information
-
two TPPII species of 53000 Da and 142000 Da are detected by SDS-PAGE. The subunits assemble into higher order complexes of 5 to 9 MD
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
?
-
x * 138000, the subunits form an active complex with a MW of 1000000 Da, the complex can sponateously dissociate in vitro into dimers which retain 1/10th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation is accompanied by a reactivation
?
x * 100000-140000, SDS-PAGE of recombinant protein, full-length TPP II and shortened versions thereof
additional information
-
two TPPII species of 53000 Da and 142000 Da are detected by SDS-PAGE. The subunits assemble into higher order complexes of 5 to 9 MD
additional information
Drosophila sp. (in: flies)
-
the 150000 Da subunits of Drosophila TPPII assemble into a giant proteolytic complex of 6 MDa, consisting of two segmented and twisted strands that form a spindle-shaped structure. The building blocks of this complex are apparently dimers, within which the 150-kDa monomers are oriented head to head. Stacking of these dimers leads to the formation of twisted single strands, two of which comprise the fully assembled spindle. This spindle also forms when TPPII is heterologously expressed in Escherichia coli, demonstrating that no scaffolding protein is required for complex formation and length determination
additional information
Drosophila sp. (in: flies)
-
TPP II is a large homooligomeric complex of about 6 MDa. Spindle formation (at TPP II concentrations above 0.03 mg/ml) by strand paring causes both significant thermodynamic and kinetic stabilization
additional information
-
conformation of the native complex, transmission electron microscopy, the complex dissociates into MW 270000 dimers upon dialysis against Tris-HCl buffer
additional information
-
compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex
additional information
-
compared with other subtilases, TPP II has a 200 amino-acid insertion between the catalytic Asp44 and His264 residues and is active as an oligomeric complex. The insert is important for the formation of the active high-molecular mass complex
additional information
-
enzyme from an alternatively spliced cDNA variant contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein forms a larger complex. The C-terminal 13 amino acids are important for aggregation of subunits
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryoelectron microscopy and single-particle analysis show that the complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. The dimensions of the TPP2 spindle are 55 x 28 nm and the strands are built of nine stacked dimers. The interior of each strand is permeated by a cavity system that features a suite of chambers at each dimer-dimer interface
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D387G
D44A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
H264A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
N362A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da
S449A
-
inactive mutant enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da
D387G
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
E331K
the catalytic efficiency is reduced 20000fold for the E331K variant compared to the wild type enzyme
E331Q
G375D
H267A
additional information
D387G
the pKa values of mutant D387G for kcat (app) increase when Asp-387 is changed to glycine. Mutant shows a bell-shaped pH-dependence of kcat(app), possibly due to an impaired protonation of the leaving group. Mutant shows a decresed kcat for all substrates and a highly decreased kcat/Km compared to wild-type. In contrast to wild-type at higher pH the kcat (app) value decreases
E331Q
the catalytic efficiency is reduced 400fold for the E331Q variant compared to the wild type enzyme
E331Q
mutant has a 2-3 orders of magnitude decreased kcat app/KM compared to wild-type, mostly dependent on an increase in KM
G375D
mutant has only 0.1% activity of wild-type at pH 7.5. Mutant shows a marked decrease in pH optimum compared to wild-type
H267A
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
H267A
mutant shows mostly a decresed kcat for all substrates and a highly decreased kcat/Km between 2 to fold orders of magnitude compared to wild-type. kcat shows a higher rise with pH in mutant H267A than in wild-type with substrate Ala-Ala-Phe-4-nitroanilide but at pH more than 7.6 kcat (app) decreases for substrate Ala-Ala-Phe-4-nitroanilide, resulting in a significantly better fit for a bell-shaped curve than for a sigmoidal
additional information
-
the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human
additional information
-
enzyme from an alternatively spliced cDNA variant contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein forms a larger complex. The C-terminal 13 amino acids are important for aggregation of subunits
additional information
-
the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 2 mM Tris-HCl dissociation buffer, 0.5 mM 2-mercaptoethanol, 3% w/v glycerol, pH 8, gradually decreases activity, 30% glycerol stabilizes
-
purified enzyme undergos a spontaneous dissociation upon storage, the dissociated enzyme has a specific activity which is 1/10th of that of the normal high MW complex
-
spindle formation (at TPP II concentrations above 0.03 mg/ml) by strand paring causes both significant thermodynamic and kinetic stabilization
Drosophila sp. (in: flies)
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, frozen in liquid nitrogen, stable
4°C, in microsomal extract, at least 3 days, less stable in phosphate buffer diluted extracts
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography and Resource RPC hydrophobic column chromatography
DEAE Sephacel column chromatography and hydroxyapatite column chromatography
-
recombinant enzyme from Escherichia coli 790fold by ammonium sulfate fractionation, anion exchange chromatography, ultrafiltration, and gel filtration
using polyethyleneimine precipitation, (NH4)2SO4 precipitation, dialysis, anion-exchange chromatography, hydrophobic interaction chromatography
using polyethyleneimine precipitation, (NH4)2SO4 precipitation, dialysis, anion-exchange chromatography, hydrophobic interaction chromatography
using polyethyleneimine precipitation, (NH4)2SO4 precipitation, dialysis, anion-exchange chromatography, hydrophobic interaction chromatography
using polyethyleneimine precipitation, (NH4)2SO4 precipitation, dialysis, anion-exchange chromatography, hydrophobic interaction chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
an 8 kb NcoI fragment covering the 5'-flanking region of the TPP2 gene, including the initiation codon, is cloned into a luciferase-containing reporter vector. HEK-293 cells and NIH3T3 cells are transiently transfected with the construct. Through sequential deletions and analysis of short PCR-fragments, the promoter can be localized to a 215 bp fragment upstream of the initiation codon
-
expressed in Escherichia coli
expression in Escherichia coli
expression of murine TPP2 gene optimized for high-level expression in Escherichia coli
gene tpp, DNA and amino acid sequence determination and analysis, recombinant expression of extracellular enzyme in Escherichia coli strains JM109 and XL-1 Blue
normal and alternatively spliced cDNA variant which contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein, expression in human kidney 293 cells
-
overexpression in 293-cells, enzyme i mainly in a nonassociated, inactive state
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TPP2 mRNA and protein are significantly up-regulated in oral squamous cell carcinoma-derived cells compared with human normal oral keratinocytes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
isoform TPPII can regulate sperm maturation by modulating intracellular Ca2+ stores via the type 3 ryanodine receptor. Tripeptidyl peptidase II antagonists strongly activate the cAMP/PKA signaling pathway that drives sperm capacitation-associated protein tyrosine phosphorylation. In the absence of Ca2+, TPPII antagonists elevate the intracellular Ca2+ levels in sperm, resulting in a marked improvement in sperm movement, capacitation, acrosome reaction, and the in vitro fertilizing ability. This antagonist-induced release of intracellular Ca2+ can be blocked by the inhibitors of ryanodine receptors which are the main intracellular Ca2+ channels responsible for releasing stored Ca2+
medicine
TPP2 mRNA and protein are significantly up-regulated in oral squamous cell carcinoma-derived cells compared with human normal oral keratinocytes. Suppression of TPP2 expression with shRNA significantly inhibit cellular proliferation compared with the control cells. In addition, appropriate localization of cellular proliferation and spindle assembly checkpoint molecules MAD2 and upregulation of CCNB1 are observed in TPP2 knockdown oral squamous cell carcinoma cells. TPP2 expression in primary oral squamous cell carcinomas is significantly greater than that in the normal oral counterparts, and the TPP2-positive cases are significantly correlated with tumor size
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Balw, R.M.; Ragnarsson, U.; Zetterquist, .
Tripeptidyl aminopeptidase in the extralysosomal fraction of rat liver
J. Biol. Chem.
258
11622-11628
1983
Rattus norvegicus
brenda
Tomkinson, B.; Wernstedt, C.; Hellman, U.; Zetterquist, .
Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type
Proc. Natl. Acad. Sci. USA
84
7508-7512
1987
Homo sapiens
brenda
Balw, R.M.; Tomkinson, B.; Ragnarsson, U.; Zetterquist, .
Purification, substrate specificity, and classification of tripeptidyl peptidase II
J. Biol. Chem.
261
2409-2417
1986
Homo sapiens, Rattus norvegicus
brenda
Macpherson, E.; Tomkinson, B.; Balw, R.M.; Hglund, S.; Zetterquist, .
Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity
Biochem. J.
248
259-263
1987
Homo sapiens
brenda
Balw, R.M.; Eriksson, I.
Tripeptidyl peptidase II in haemolysates and liver homogenates of various species
Biochem. J.
241
75-80
1987
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Platyrrhini, no activity in Escherichia coli, Rattus norvegicus, Sus scrofa
brenda
Tomkinson, B.; Zetterquist, .
Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin
Biochem. J.
267
149-154
1990
Homo sapiens
brenda
Tomkinson, B.; Grehn, L.; Fransson, B.; Zetterquist, ?.
Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II
Arch. Biochem. Biophys.
314
276-279
1994
Homo sapiens
brenda
Tomkinson, B.; Nyberg, F.
Distribution of tripeptidyl-peptidase II in the central nervous system of rat
Neurochem. Res.
20
1443-1447
1995
Rattus norvegicus
brenda
Matrinsson, T.; Vujic, M.; Tomkinson, B.
Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids
Genomics
17
493-495
1993
Homo sapiens
brenda
Wilson, C.; Gibosn, A.M.; McDermott, J.R.
Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain
Neurochem. Res.
18
743-749
1993
Homo sapiens
brenda
Tomkinson, B.
Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II
Biomed. Biochim. Acta
50
727-729
1991
Homo sapiens
brenda
Harris, J.; Tomkinson, B.
Electron microscopical and biochemical studies on the oligomeric states of human erythrocyte tripeptidyl peptidase-II
Micron Microsc. Acta
21
77-89
1990
Homo sapiens
-
brenda
Tomkinson, B.
Characterization of cDNA for murine tripeptidyl-peptidase II reveals alternative splicing [published erratum appears in Biochem J 1995 Mar 15;306(Pt 3):880]
Biochem. J.
304
517-523
1994
Mus musculus
brenda
Tomkinson, B.
Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity
Arch. Biochem. Biophys.
376
275-280
2000
Homo sapiens
brenda
Tomkinson, B.; Ni Laoi, B.; Wellington, K.
The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex
Eur. J. Biochem.
269
1438-1443
2002
Homo sapiens, Mus musculus
brenda
Tomkinson, B.; Hansen, M.; Cheung, W.F.
Structure-function studies of recombinant murine tripeptidyl-peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation
FEBS Lett.
405
277-280
1997
Mus musculus
brenda
Renn, S.C.; Tomkinson, B.; Taghert, P.H.
Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster
J. Biol. Chem.
273
19173-19182
1998
Drosophila melanogaster, Rattus norvegicus
brenda
Ganellin, C.R.; Bishop, P.B.; Bambal, R.B.; Chan, S.M.; Law, J.K.; Marabout, B.; Luthra, P.M.; Moore, A.N.; Peschard, O.; Bourgeat, P.; Rose, C.; Vargas, F.; Schwartz, J.C.
Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors
J. Med. Chem.
43
664-674
2000
Rattus norvegicus
brenda
Breslin, H.J.; Miskowski, T.A.; Kukla, M.J.; Leister, W.H.; De Winter, H.L.; Gauthier, D.A.; Somers, M.V.; Peeters, D.C.; Roevens, P.W.
Design, synthesis, and tripeptidyl peptidase II inhibitory activity of a novel series of (S)-2,3-dihydro-2-(4-alkyl-1H-imidazol-2-yl)-1H-indoles
J. Med. Chem.
45
5303-5310
2002
Rattus norvegicus
brenda
Hilbi, H.; Jozsa, E.; Tomkinson, B.
Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis
Biochim. Biophys. Acta
1601
149-154
2002
Homo sapiens
brenda
Radu, D.; Tomkinson, B.; Zachrisson, O.; Weber, G.; de Belleroche, J.; Hirsch, S.; Lindefors, N.
Overlapping regional distribution of CCK and TPPII mRNAs in Cynomolgus monkey brain and correlated levels in human cerebral cortex (BA 10)
Brain Res.
1104
175-182
2006
Macaca fascicularis, Rattus norvegicus, Homo sapiens (P29144)
brenda
Chand, A.; Wyke, S.M.; Tisdale, M.J.
Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle
Cancer Lett.
218
215-222
2005
Mus musculus
brenda
Lindas, A.C.; Tomkinson, B.
Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II
Gene
345
249-257
2005
Homo sapiens
brenda
Reits, E.; Neijssen, J.; Herberts, C.; Benckhuijsen, W.; Janssen, L.; Drijfhout, J.W.; Neefjes, J.
A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
Immunity
20
495-506
2004
Homo sapiens
brenda
Tomkinson, B.; Lindas, A.C.
Tripeptidyl-peptidase II: a multi-purpose peptidase
Int. J. Biochem. Cell Biol.
37
1933-1937
2005
Homo sapiens
brenda
Seyit, G.; Rockel, B.; Baumeister, W.; Peters, J.
Size matters: the spindle form of the 6 MDA tripeptidylpeptidase II from drosophila melanogaster stabilizes the activated state
J. Biol. Chem.
281
25723-25733
2006
Drosophila sp. (in: flies)
brenda
Ganellin, C.R.; Bishop, P.B.; Bambal, R.B.; Chan, S.M.; Leblond, B.; Moore, A.N.; Zhao, L.; Bourgeat, P.; Rose, C.; Vargas, F.; Schwartz, J.C.
Inhibitors of tripeptidyl peptidase II. 3. Derivation of butabindide by successive structure optimizations leading to a potential general approach to designing exopeptidase inhibitors
J. Med. Chem.
48
7333-7342
2005
Rattus norvegicus
brenda
Book, A.J.; Yang, P.; Scalf, M.; Smith, L.M.; Vierstra, R.D.
Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis
Plant Physiol.
138
1046-1057
2005
Arabidopsis sp.
brenda
Rockel, B.; Peters, J.; Mueller, S.A.; Seyit, G.; Ringler, P.; Hegerl, R.; Glaeser, R.M.; Baumeister, W.
Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II
Proc. Natl. Acad. Sci. USA
102
10135-10140
2005
Drosophila sp. (in: flies)
brenda
Naujokat, C.; Fuchs, D.; Berges, C.
Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition
Biochim. Biophys. Acta
1773
1389-1397
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Levengood, M.R.; van der Donk, W.A.
Use of lantibiotic synthetases for the preparation of bioactive constrained peptides
Bioorg. Med. Chem. Lett.
18
3025-3028
2008
Homo sapiens
brenda
Hong, X.; Lei, L.; Kuenert, B.; Naredla, R.; Applequist, S.E.; Grandien, A.; Glas, R.
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors
Cancer Res.
67
7165-7174
2007
Homo sapiens
brenda
Bhutani, N.; Venkatraman, P.; Goldberg, A.L.
Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
EMBO J.
26
1385-1396
2007
Homo sapiens (P29144)
brenda
Basler, M.; Groettrup, M.
No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes
Eur. J. Immunol.
37
896-904
2007
Homo sapiens
brenda
Endert, P.
Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?
Eur. J. Immunol.
38
609-613
2008
Homo sapiens
brenda
Marcilla, M.; Villasevil, E.M.; de Castro, J.A.
Tripeptidyl peptidase II is dispensable for the generation of both proteasome-dependent and proteasome-independent ligands of HLA-B27 and other class I molecules
Eur. J. Immunol.
38
631-639
2008
Homo sapiens
brenda
Lindas, A.C.; Tomkinson, B.
Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements
Gene
393
62-69
2007
Homo sapiens
brenda
Preuss, K.D.; Held, G.; Kubuschok, B.; Hung, C.Z.; Malatsidze, N.; Wagner, M.; Pfreundschuh, M.
Identification of antigenic targets of paraproteins by expression cloning does not support a causal role of chronic antigenic stimulation in the pathogenesis of multiple myeloma and MGUS
Int. J. Cancer
121
459-461
2007
Homo sapiens
brenda
Guil, S.; Rodriguez-Castro, M.; Aguilar, F.; Villasevil, E.M.; Anton, L.C.; Del Val, M.
Need for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental
J. Biol. Chem.
281
39925-39934
2006
Homo sapiens
brenda
Huai, J.; Firat, E.; Nil, A.; Million, D.; Gaedicke, S.; Kanzler, B.; Freudenberg, M.; van Endert, P.; Kohler, G.; Pahl, H.L.; Aichele, P.; Eichmann, K.; Niedermann, G.
Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice
Proc. Natl. Acad. Sci. USA
105
5177-5182
2008
Mus musculus
brenda
Anton, L.C.; Villasevil, E.M.
Is there an alternative to the proteasome in cytosolic protein degradation?
Biochem. Soc. Trans.
36
839-842
2008
Homo sapiens
brenda
Lindas, A.C.; Eriksson, S.; Jozsa, E.; Tomkinson, B.
Investigation of a role for Glu-331 and Glu-305 in substrate binding of tripeptidyl-peptidase II
Biochim. Biophys. Acta
1784
1899-1907
2008
Mus musculus (Q64514)
brenda
Firat, E.; Tsurumi, C.; Gaedicke, S.; Huai, J.; Niedermann, G.
Tripeptidyl peptidase II plays a role in the radiation response of selected primary cell types but not based on nuclear translocation and p53 Sstabilization
Cancer Res.
69
3325-3331
2009
Mus musculus
brenda
Tye, C.E.; Lorenz, R.L.; Bartlett, J.D.
Lysosomal protease expression in mature enamel
Cells Tissues Organs
189
111-114
2009
Mus musculus
brenda
Schnurr, M.; Orban, M.; Robson, N.C.; Shin, A.; Braley, H.; Airey, D.; Cebon, J.; Maraskovsky, E.; Endres, S.
ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II
J. Immunol.
182
1253-1259
2009
Homo sapiens
brenda
Oda, H.; Saiki, K.; Tonosaki, M.; Yajima, A.; Konishi, K.
Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis
J. Periodont. Res.
44
362-267
2008
Porphyromonas gingivalis, Porphyromonas gingivalis W83
brenda
Tsurumi, C.; Firat, E.; Gaedicke, S.; Huai, J.; Mandal, P.K.; Niedermann, G.
Viability and DNA damage responses of TPPII-deficient Myc- and Ras-transformed fibroblasts
Biochem. Biophys. Res. Commun.
386
563-568
2009
Mus musculus (Q64514)
brenda
Grauling-Halama, S.; Bahr, U.; Schenk, S.; Geginat, G.
Role of tripeptidyl peptidase II in the processing of Listeria monocytogenes-derived MHC class I-presented antigenic peptides
Microbes Infect.
11
795-802
2009
Mus musculus
brenda
Nahalkova, J.; Tomkinson, B.
TPPII, MYBBP1A and CDK2 form a protein-protein interaction network
Arch. Biochem. Biophys.
564
128-135
2014
Homo sapiens
brenda
Eklund, S.; Dogan, J.; Jemth, P.; Kalbacher, H.; Tomkinson, B.
Characterization of the endopeptidase activity of tripeptidyl-peptidase II
Biochem. Biophys. Res. Commun.
424
503-507
2012
Mus musculus
brenda
Eklund, S.; Lindas, A.C.; Hamnevik, E.; Widersten, M.; Tomkinson, B.
Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics
Biochim. Biophys. Acta
1824
561-570
2012
Drosophila melanogaster, Drosophila melanogaster (Q9V6K1), Homo sapiens, Mus musculus, Mus musculus (Q64514)
brenda
Usukura, K.; Kasamatsu, A.; Okamoto, A.; Kouzu, Y.; Higo, M.; Koike, H.; Sakamoto, Y.; Ogawara, K.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Tripeptidyl peptidase II in human oral squamous cell carcinoma
J. Cancer Res. Clin. Oncol.
139
123-130
2013
Homo sapiens, Homo sapiens (P29144)
brenda
Zhou, Y.; Ru, Y.; Wang, C.; Wang, S.; Zhou, Z.; Zhang, Y.
Tripeptidyl peptidase II regulates sperm function by modulating intracellular Ca(2+) stores via the ryanodine receptor
PLoS ONE
8
e66634
2013
Mus musculus, Mus musculus (Q64514)
brenda
Schoenegge, A.M.; Villa, E.; Foerster, F.; Hegerl, R.; Peters, J.; Baumeister, W.; Rockel, B.
The structure of human tripeptidyl peptidase II as determined by a hybrid approach
Structure
20
593-603
2012
Homo sapiens (P29144), Homo sapiens
brenda
Ekino, K.; Yonei, S.; Oyama, H.; Oka, T.; Nomura, Y.; Shin, T.
Cloning, purification, and characterization of tripeptidyl peptidase from Streptomyces herbaricolor TY-21
Appl. Biochem. Biotechnol.
184
239-252
2018
Kitasatospora herbaricolor (D1MVE1), Kitasatospora herbaricolor, Kitasatospora herbaricolor TY-21 (D1MVE1)
brenda
Bialy, L.P.; Kuckelkorn, U.; Henklein, P.; Fayet, J.; Wilczynski, G.M.; Kaminski, A.; Mlynarczuk-Bialy, I.
Changes in spatio-temporal localization of tripeptidyl peptidase II (TPPII) in murine colon adenocarcinoma cells during aggresome formation a microscopy study based on a novel fluorescent proteasome inhibitor
Histol. Histopathol.
34
359-372
2019
Mus musculus
brenda
Wiemhoefer, A.; Stargardt, A.; van der Linden, W.A.; Renner, M.C.; van Kesteren, R.E.; Stap, J.; Raspe, M.A.; Tomkinson, B.; Kessels, H.W.; Ovaa, H.; Overkleeft, H.S.; Florea, B.; Reits, E.A.
Tripeptidyl peptidase II mediates levels of nuclear phosphorylated ERK1 and ERK2
Mol. Cell. Proteomics
14
2177-2193
2015
Homo sapiens (P29144)
brenda
Fukuda, Y.; Beck, F.; Plitzko, J.M.; Baumeister, W.
In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes
Proc. Natl. Acad. Sci. USA
114
4412-4417
2017
Rattus norvegicus (Q64560)
brenda
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