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Information on EC 3.4.14.9 - tripeptidyl-peptidase I
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3.4.14.9 tripeptidyl-peptidase ISpecify your search results
Word Map
- 3.4.14.9
-
ceroid
- lipofuscinosis
-
infantile
- neurodegenerative
-
lincl
-
late-infantile
- tripeptides
- palmitoyl-protein
-
curvilinear
- batten
-
serine-carboxyl
-
exopeptidase
-
pepstatin-insensitive
- molecular biology
- medicine
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
Synonyms
aminopeptidase, tripeptidyl, I, AO090166000084, CLN2, CLN2 protein, LPIC, lysosomal pepstatin insensitive protease, SedB, SedC, SedD, sedolisin B, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, tripeptidyl, I
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-
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AO090166000084
LPIC
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-
-
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lysosomal pepstatin insensitive protease
-
-
-
-
SedD
TPP I
TPP-I
Tpp1
TPPI
tripeptidyl aminopeptidase
-
-
-
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tripeptidyl aminopeptidase I
tripeptidyl peptidase
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-
-
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tripeptidyl peptidase 1
tripeptidyl peptidase I
tripeptidyl-peptidase 1
TPP I
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prefers Leu, Phe and Nle at the P1 position, whereas Asn, His, Lys, Arg, Ser, Val, Ile, Thr, Gly and Pro are highly unfavored in this position, showing less than 1% of the activity of the best substrates
Tpp1
TPP1 is a serine protease that possesses two catalytic functions, a primary tripeptidyl exopeptidase activity with a pH optimum of about 5.0 that catalyzes the sequential release of tripeptides from the unsubstituted N termini of substrates and a much weaker endoproteolytic activity with a pH optimum of about 3.0
tripeptidyl aminopeptidase I
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-
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tripeptidyl peptidase I
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tripeptidyl peptidase I
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shows tripeptidyl peptidase activity and pepstatin insensitive carboxyl endopeptidase activity
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
151662-36-1
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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
(pGlu)LYENKPRRRPYIL + H2O
(pGlu)L + YENKPRRRPYIL
-
i.e. neurotensin, 15.0% degradation after 16 h
-
?
Ala-Ala-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Ala-Pro-4-nitroanilide + H2O
Ala-Ala-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Arg-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Asp-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Asp-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-His-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-His-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Nle-Leu-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nle-Leu + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Nle-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nle-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Nva-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nva-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Phe-Pro-4-nitroanilide + H2O
Ala-Phe-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe + H2O
Ala-Pro-Gly + Asp-Arg-Ile + Tyr-Val-His-Pro-Phe
SedB
-
-
?
Ala-Ser-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Ser-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Arg-Ala-Phe-7-amido-4-methylcoumarin + H2O
Arg-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Arg-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
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-
-
-
?
Arg-Pro-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Arg-Pro-Phe + 7-amino-4-carbamoylmethylcoumarin
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-
-
-
?
Asp-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Asp-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
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-
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-
?
DRVYIHPFHL + H2O
DRV + YIHPFHL
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i.e. angiotensin I, 11.3% degradation after 16 h
-
?
GKPIPFFRLK + H2O
GKPIP + FFRLK
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endo-type substrate, 24.5% degradation after 16 h
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?
Gly-L-Pro-L-Met-2-anthraquinonyl hydrazide + H2O
Gly-L-Pro-L-Met + 2-anthraquinonyl hydrazine
-
-
-
-
?
Gly-Lys-Pro-Ile-Pro-Phe-Phe-Arg-Leu-Lys + H2O
Gly-Lys-Pro-Ile-Pro-Phe + Phe-Arg-Leu-Lys
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-
-
-
?
Gly-Pro-Ala 4-nitroanilide + H2O
Gly-Pro-Ala + 4-nitroaniline
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at 20% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
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-
?
Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
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at 10% the rate of Gly-Pro-Met 4-methylcoumarin 7-amide hydrolysis
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?
Gly-Pro-Met-7-amido-4-methylcoumarin + H2O
Gly-Pro-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
GNLWATGHFM-NH2 + H2O
GNL + WATGHFM-NH2
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i.e. neuromedin B, complete degradation after 16 h
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?
His-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
His-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
L-Arg-L-Nle-L-Nle-7-amido-4-methylcoumarin + H2O
L-Arg-L-Nle-L-Nle + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
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synthetic peptide modeled after NH2-terminal tripeptide sequence of the phenylalanyl monomer of bovine or rat growth hormone, fluorogenic substrate
-
?
phenylalanyl monomer of bovine growth hormone + H2O
?
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cleaves 11 tripeptides sequentially from the NH2-terminus
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-
?
RVYIHPF + H2O
RVY + IHPF
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i.e. angiotensin III, 95.0% degradation after 15 min
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?
Ser-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ser-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
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-
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?
synthetic collagen-like polypetides + H2O
Gly-Pro-Xaa tripeptides
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-
-
?
Val-Pro-Arg 4-nitroanilide + H2O
Val-Pro-Arg + 4-nitroaniline
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at 11% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
-
-
?
YGGFLRKYP + H2O
YGG + FLRKYP
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i.e. beta-neo-endorphin, 28% degradation after 16 h
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?
[Ala-Ala-Phe]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
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specific substrate for determining TPP-I activity and intracellular localization in living cells
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-
?
[Arg-Nle-Nle]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
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specific substrate for determining TPP-I activity and intracellular localization in living cells
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-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedB
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedC
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?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedD
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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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?
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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33.8% degradation within 60 min
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-
?
DRVYIHPF + H2O
DRV + YIHPF
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i.e. angiotensin II, 18.2% degradation after 16 h
-
?
Gly-Pro-Leu 2-naphthylamide + H2O
Gly-Pro-Leu + 2-naphthylamine
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25% of the activity with Gly-Pro-Met 2-naphthylamide, Ala-Ala-Phe-4-nitroanilide or Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O
Gly-Pro-Leu + 2-naphthylamine
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at 30% the rate of Gly-Pro-Met 2-naphthylamide hydrolysis
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-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
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-
-
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?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
SedB
-
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
SedC
-
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
SedD
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-
?
glucagon + H2O
additional information
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-
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all nine tripeptides and the C-terminal pentapeptide are identified
?
additional information
?
-
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no substrates are Ala-Phe-Pro-beta-naphthylamide (modeled after NH2-terminal tripeptide sequence of the alanyl monomer of bovine growth hormone), alanyl monomer of bovine growth hormone
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-
-
additional information
?
-
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no significant aminopeptidase activity
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-
-
additional information
?
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succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, succinyl-Gly-Pro-Leu 4-methylcoumarin 7-amide, Gly-Pro-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, Pro-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin, Ala 7-amido-4-methylcoumarin, Phe-7-amido-4-methylcoumarin, or Leu-7-amido-4-methylcoumarin
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-
-
additional information
?
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the enzyme removes tripeptides from the free N-termini of small polypeptides and also shows a minor endoprotease activity
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-
additional information
?
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absolute requirement for unsubstituted amino-terminus
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additional information
?
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classical late infantile neuronal ceroid lipofuscinosis is an autosomal recessive disease caused by mutations in the CLN2 gene resulting in functional defects of the gene product tripeptidyl-peptidase I. This disease is associated with a progressive neurodegenerative course beginning at the age of two years with developmental stagnation, finally leading to a complete loss of motor function, vision and speech by the age of 10 years
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-
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additional information
?
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elevated enzyme activity of tripeptidyl peptidase I and other lysosomal enzymes in Sjoegren's syndrome patients may play a role in tissue damage by accelerated breakdown of glycoproteins in lysosomes
-
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-
additional information
?
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TPP I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B. The inability of cells from patients with late-infantile neuronal ceroid lipofuscinosis (CNL2) to degrade neuromedin B and other neuropeptides may contribute to the pathogenesis of the disease
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-
additional information
?
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determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates
-
-
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additional information
?
-
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prefers Leu, Phe and Nle at the P1 position, whereas Asn, His, Lys, Arg, Ser, Val, Ile, Thr, Gly and Pro are highly unfavored in this position, showing less than 1% of the activity of the best substrates
-
-
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additional information
?
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TPP I acts preferentially on small, unstructured oligopeptides of less than 5 kDa
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-
-
additional information
?
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dipeptidyl-peptidase I cannot functionally compensate for the loss of tripeptidyl-peptidase I
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additional information
?
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substrates not cleaved after 24 h of digestion: dynorphin, beta-casomorphin-7, Leu-enkephalin, Met-enkephalin, neurokinin-A, LVV-hemorphin, bradykinin
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-
-
additional information
?
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the enzymne cleaves tripeptides from synthetic substrates provided that the N-terminus is unsubstituted and the amino acid in the P1 position is not charged. The enzyme also cleaves small peptides, angiotensin II and glucagon, releasing tripeptides but does not appear to demonstrate any preference for amino acids on either side of the cleavage site. Substrates with a charged amino acid in the P1 position appear to be resistant to hydrolysis
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-
-
additional information
?
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an inherited deficiency of tripeptidyl peptidase I activity causes a fatal lysosomal storage disorder, classic late infantile neuronal ceroid lipofuscinosis, CLN2
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-
-
additional information
?
-
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N-terminal exopeptidase that removes tripeptide units provided the P3 residue is unsubstituted
-
-
-
additional information
?
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Met-2-naphthylamide, succinyl-Gly-Pro-Met 2-naphthylamide, Pro-Met-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin, methoxysuccinyl-Gly-Pro-Met-7-amido-4-methylcoumarin, benzyloxy-Arg-Arg-7-amido-4-methylcoumarin, Arg-7-amido-4-methylcoumarin, Pro-Ala-4-nitroanilide, Ala 4-nitroanilide, tert-butyloxycarbonyl-Gly-Pro-Ala 4-nitroanilide, benzoyl-Val-Pro-Arg 4-nitroanilide
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-
-
additional information
?
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exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils
-
-
-
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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
?
-
-
classical late infantile neuronal ceroid lipofuscinosis is an autosomal recessive disease caused by mutations in the CLN2 gene resulting in functional defects of the gene product tripeptidyl-peptidase I. This disease is associated with a progressive neurodegenerative course beginning at the age of two years with developmental stagnation, finally leading to a complete loss of motor function, vision and speech by the age of 10 years
-
-
-
additional information
?
-
-
elevated enzyme activity of tripeptidyl peptidase I and other lysosomal enzymes in Sjoegren's syndrome patients may play a role in tissue damage by accelerated breakdown of glycoproteins in lysosomes
-
-
-
additional information
?
-
-
TPP I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B. The inability of cells from patients with late-infantile neuronal ceroid lipofuscinosis (CNL2) to degrade neuromedin B and other neuropeptides may contribute to the pathogenesis of the disease
-
-
-
additional information
?
-
-
dipeptidyl-peptidase I cannot functionally compensate for the loss of tripeptidyl-peptidase I
-
-
-
additional information
?
-
-
an inherited deficiency of tripeptidyl peptidase I activity causes a fatal lysosomal storage disorder, classic late infantile neuronal ceroid lipofuscinosis, CLN2
-
-
-
additional information
?
-
-
exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dextran sulfate
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initially, as the glycosaminoglycan concentration progressed from 0 to about 100 ng/ml, the activity of TPP I falls down rapidly to reach a plateau with saturable inhibition at about 100 ng-0.1 mg/ml and then it gradually increases with increased glycosaminoglycan concentration. The maximal percent inhibition is 50%
-
heparin
-
initially, as the glycosaminoglycan concentration progressed from 0 to about 100 ng/ml, the activity of TPP I falls down rapidly to reach a plateau with saturable inhibition at about 100 ng-0.1 mg/ml and then it gradually increases with increased glycosaminoglycan concentration. The maximal percent inhibition is 50%
prosegment of tripeptidyl peptidase I
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wild type prosegment of tripeptidyl peptidase I (176 amino acid residues) is a potent, slow-binding inhibitor of its parent enzyme with an overall inhibition constant in the low nanomolar range, in the presence of the prosegment (at 0.001 mM) leads from a significant to complete inhibition of TPP I activity at pH between 3.5 and 5.5 with IC 50 ranging from more than 0.016 mM to 0.000043 mM at pH from 3.5 to 5.5
-
additional information
-
no inhibition by pepstatin; no inhibition: EDTA; no inhibition: Phe-Pro-Arg chloromethylketone, inhibitors of cysteine proteinases or metalloproteinases, iodoacetamide, trans-epoxysuccinyl-L-leucinamido(4-guanidino)butane (i.e. E-64), mercaptoethanol, bestatin, soybean trypsin inhibitor, phenylchloromethyl ketone
-
additional information
-
resistant to inhibition by diisopropylfluorophosphate
-
additional information
-
no inhibition: alkali-inactivated diisopropylfluoride, leupeptin; no inhibition by pepstatin; no inhibition: EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
neonatally treated mice display high levels of TPP-I activity in the CNS 1 year after administration of AAVrh.10hCLN2 vector directly to the neonatal brain of CLN2 knockout mice at 2 days, 3 weeks, and 7 weeks of age, the AAVrh.10hCLN2 vector contains an expression cassette consisting of the human CLN2 cDNA driven by a CMV/beta-actin hybrid promoter consisting of the enhancer from the cytomegalovirus immediate early gene, the promoter, splice donor and intron from the chicken beta-actin gene, the splice acceptor from the rabbit beta-globin gene followed by a CLN2 cDNA with an optimized Kozak translation initiation sequence, the cDNA is followed by the polyadenylation sequence from rabbit beta-globin, the expression cassette is surrounded by the inverted terminal repeats of adeno-associated virus 2
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00509
Ala-Asp-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.0625
Phe-Pro-Ala-4-nitroanilide
pH 6.0, 20°C, SedB
0.00402
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.123
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, mutant enzyme E77A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04 - 1.97
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D276A
0.0124
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 378°C, mutant enzyme E77A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001581
prosegment of tripeptidyl peptidase I
-
in sodium acetate buffer (50 mM, pH 5.0), 0.05% Triton X-100
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001292
prosegment of tripeptidyl peptidase I
Homo sapiens
-
in sodium acetate buffer (50 mM, pH 5.0), 0.05% Triton X-100
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
-
hydrolysis of Gly-Pro-Met 2-naphthylamide or Ala-Ala-Phe 4-methylcoumarin 7-amide
5.9
-
and a second optimum at pH 4.5, at pH 5.9 70% of the activity at pH 4.5
additional information
-
the optimum pH of TPP 1 is dependent on the substrate used
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
active between pH 3 and pH 7, SedB; active between pH 3 and pH 7, SedC
3 - 4.8
-
pH 3.0: about 30% of maximal activity, pH 4.8: about 50% of maximal activity
3 - 8
-
about half-maximal activity at pH 3 and 8, hydrolysis of Gly-Pro-Met 2-naphthylamide
3.5 - 6.5
-
about half-maximal activity at pH 3.5 and 6.5, hydrolysis of Ala-Ala-Phe 4-methylcoumarin 7-amide
3.5 - 5
-
pH 3.5: about 25% of maximal activity, pH 5.0: about 45% of maximal activity, hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin
4 - 5.5
-
about 55% of maximal activity at pH 4.0 and at pH 5.5, hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.12
calculated from sequence, mature domain, SedD
5.17
calculated from sequence, mature domain, SedB
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme histochemistry show high activity of TPP I in carotid body glomeruli. The glomus cells contain many TPP I-positive granules, while the glial-like sustentacular cells display a slightly fainter reaction
brenda
-
activity in neuroglia cells, no activity in small granule cells, Purkinje cells, remified dendrites and myelinated fibers
brenda
-
activity in ducts, no activity in acinar cells and islets of Langerhans
brenda
-
activity in excretory duct and stereocilia, no activity in glandular acinus and intercalated portion
brenda
-
activity in spermatogonia, spermatozoa, Sertoli cells and Leygig cells, no activity in basement cells
brenda
-
TPPI is expressed ubiquitously throughout the body but disease appears restricted to the brain
brenda
presence of recombinant fusion protein with enhanced green fluorescent protein
brenda
-
presence of recombinant fusion protein with enhanced green fluorescent protein
-
brenda
presence of recombinant fusion protein with enhanced green fluorescent protein
brenda
-
presence of recombinant fusion protein with enhanced green fluorescent protein
-
brenda
-
activity in proximal tubules, distal tubules, collecting tubules and transitional cells, no activity in glomerulus and Bowman‘s capsule
brenda
-
enzyme activity is elevated during the first 5 years of Sjoegren's syndrome, and it increases further between 5 and 10 years after diagnosis
brenda
-
activity in corpus luteum and corpus albicus, no activity in follicles
brenda
-
heterogenous distribution of TPP I positive macrophages, leukocytes and reticular fibroblasts in the red and white pulp
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
presence of recombinant fusion protein with enhanced green fluorescent protein
brenda
-
presence of recombinant fusion protein with enhanced green fluorescent protein
-
brenda
-
the conversion of the proenzyme into the mature form takes place in lysosomal compartment
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
TPP1 knockout mice which serve as a mouse model for classical late-infantile neuronal ceroid lipofuscinosis (LINCL) are analysed in terms of storage material present in the brain of the mouse model. It is shown that a number of protein constituents including glial fibrillary acidic protein are elevated
malfunction
-
TPP1 knockout mice providing a mouse model for late-infantile neuronal ceroid lipofuscinosis (LINCL) generated that either lack the pro-apoptotic p53 or have increased levels of anti-apoptotic Bcl-2. Neither modification affects the shortened life-span of the LINCL mouse. These findings suggest that targeting pathways of cell death involving p53 or Bcl-2 do not represent useful directions for developing effective treatment
physiological function
both the total protease and tripeptidyl peptidase activities in the culture medium of a gene disruptant strain are decreased as compared to those of the control strain. The maximum yields of recombinant bovine chymosin and human lysozyme produced by the disruptants show approximately 2.9- and 1.7fold increases, respectively, as compared to their control strains. Tripeptidyl peptidase activity in the culture medium of the disruptant is decreased
physiological function
-
both the total protease and tripeptidyl peptidase activities in the culture medium of a gene disruptant strain are decreased as compared to those of the control strain. The maximum yields of recombinant bovine chymosin and human lysozyme produced by the disruptants show approximately 2.9- and 1.7fold increases, respectively, as compared to their control strains. Tripeptidyl peptidase activity in the culture medium of the disruptant is decreased
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A2N9MBI9_9BACT
1009
0
103751
TrEMBL
K8YZE9_NANGC
Nannochloropsis gaditana (strain CCMP526)
256
0
27157
TrEMBL
A2QVE4_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
639
0
69641
TrEMBL
A2R746_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
573
0
62348
TrEMBL
A0A2U3KUD1_9FIRM
895
0
93726
TrEMBL
M5BJS7_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
507
0
55603
TrEMBL
A0A2U3LID1_9FIRM
811
1
84341
TrEMBL
C3MLH7_SULIL
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
605
1
67240
TrEMBL
A0A0B7FM04_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
593
0
62927
TrEMBL
A0A2U3KXD0_9BACT
1901
1
194796
TrEMBL
M5C9U2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
368
0
39938
TrEMBL
A0A0B7G433_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
584
0
62964
TrEMBL
SED2_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
602
0
65839
Swiss-Prot
SED3_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
596
1
65276
Swiss-Prot
Q2U9N2_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
594
0
63572
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
48000
68000
89000
x * 89000, fusion protein with enhanced green fluorescent protein, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 40600, SedD, calculated from sequence; x * 43000, SedB, calculated from sequence
?
x * 89000, fusion protein with enhanced green fluorescent protein, SDS-PAGE
?
-
x * 89000, fusion protein with enhanced green fluorescent protein, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
all five potential N-glycosylation sites in the enzyme are utilized, some of its N-linked oligosaccharides are of the complex/hybrid type
glycoprotein
-
TPP I in vivo utilizes all five N-glycosylation sites (Asn210, Asn222, Asn286, Asn313 and Asn443). Mutation of N286Q dramatically affects the folding of the enzyme and partially arrests TPP I in the endoplasmic reticulum. N-glycans at Asn210, Asn222, Asn313, and Asn443 contribute slightly to the specific activity of the enzyme
glycoprotein
-
TPP 1 is glycosylatd at most or all of five asparagin-linked glycosylation sites
glycoprotein
-
TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity
proteolytic modification
the preproprotein SedB is composed of 602 amino acids, the signal peptide contains 24 amino acids; the preproprotein SedC is composed of 596 amino acids, the signal peptide contains 24 amino acids; the preproprotein SedD is composed of 568 amino acids, the signal peptide contains 20 amino acids
proteolytic modification
-
the 68000 Da precursor polypeptide is converted to the mature enzyme of 48000 Da. Although tripeptidyl-peptidase I zymogen is capable of autoactivation in vitro, a serine protease that is sensitive to 4-(2-aminoethyl)-benzene-sulfonamide participates in processing of the proenzyme to the mature, active form in vivo
proteolytic modification
-
the protein is synthesized as an inactive zymogen that is autocatalytically converted to an active serine protease at acidic pH, removal of a 19-residue signal peptide
proteolytic modification
-
TPP-I is synthesized as a 66000 Da inactive precursor consisting of a 195 residue prepro-peptide and 368 residue mature enzyme. Most of the precursor proteins are converted to a 46000 Da form by post-translational proteolysis
proteolytic modification
-
proenzyme, the N-linked glycan at Asn286 is involved in maturation of the enzyme
proteolytic modification
-
TPP I activity is not involved in the major proteolytic step leading to generation of the mature enzyme, indicating that autoactivation of human pro-TTP I in vitro occurs by intramolecular mechanisms
proteolytic modification
-
autoactivation of pro-TPP I is fully activated at pH 3.5 after only 15 min of activation in 50 mM sodium acetate buffer, independent of NaCl concentration. In presence of 1 M NaCl (but not 150 mM NaCl) significant activation also is observed at pH 4.0. Ionic strength affects the yield but not the rates or the mechanism of pro-TPP I activation in vitro
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
deglycosylated inactive proenzyme pro-TPP1, hanging drop vapour diffusion method, using 0.1 M citrate, 4-7% polyethylene glycol 6000, at pH 5.0
-
fully-glycosylated TPP1 precursor, hanging drop vapour diffusion method, using 7% PEG4000, 0.02 M zinc sulfate, 0.1 M sodium acetate, pH 5.0, and 0.1 M ammonium sulfate
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C365R
D360A
E343K
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
G284V
G473R
-
the mutation probably compromises the active center and results in loss of proteolytic activity
G77R
I287N
K428N
-
no apparent conformational destabilization is observed for the missense mutation
N286Q
-
the secreted proenzyme formes non-native, interchain disulfide bridges and displays only residual TPP I activity upon acidification. A small portion of the mutant enzyme reaches the lysosome and is processed to an active species, however, it shows low thermal and pH stability
N286S
P202L
P544S
Q248P
-
the mutation probably compromises the active center and results in loss of proteolytic activity
Q422H
Q442H
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
R127Q
R206C
R208X
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, no detection of any translational product for the mutant
R266Q
-
no apparent conformational destabilization is observed for the missense mutation
R447H
S475L
T353P
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, enzyme shows 5.5% of wild-type enzyme when expressed in HEK cells, blocked processing to mature size peptidase leads to protein retention in the endoplasmic reticulum and rapid degradation in non-lysosomal compartments
V216M
-
no apparent conformational destabilization is observed for the missense mutation
V227M
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
V277M
C365R
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
G284V
-
the mutation probably compromises the active center and results in loss of proteolytic activity
G284V
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
G77R
-
the mutation is associated with classic late infantile neuronal ceroid lipofuscinosis
G77R
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, 1% of wild-type activity
I287N
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, enzyme shows 4.1% of wild-type enzyme when expressed in HEK cells, blocked processing to mature size peptidase leads to protein retention in the endoplasmic reticulum and rapid degradation in non-lysosomal compartments
I287N
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
N286S
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, enzyme shows 5.8% of wild-type enzyme when expressed in HEK cells, blocked processing to mature size peptidase leads to protein retention in the endoplasmic reticulum and rapid degradation in non-lysosomal compartments
N286S
-
the substitution results in loss of one glycosylation site, which leads to almost complete loss of protease activity
N286S
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
P202L
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, no enzymatic activity
P544S
-
decreased activity; demonstrates a normal polypeptide pattern on Western blots, enzyme activity, and lysosomal localization
P544S
-
protein processing similar to wild-type, lysosomal localisation, 32.8% of wild-type activity
Q422H
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, enzyme shows 4.7% of wild-type enzyme when expressed in HEK cells, blocked processing to mature size peptidase leads to protein retention in the endoplasmic reticulum and rapid degradation in non-lysosomal compartments
R127Q
-
mutation is identified in patients with late infantile ceroid lipofuscinosis, enzyme shows 74.3% of wild-type enzyme when expressed in HEK cells
R127Q
-
decreased activity; demonstrates a normal polypeptide pattern on Western blots, enzyme activity, and lysosomal localization
R127Q
-
protein processing similar to wild-type,lysosomal localization, 43% of wild-type activity
R206C
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, 0.7% of wild-type activity
R447H
-
protein processing different from wild-type, mutant is not localized in lysosomes, intracellular trafficking of mutant is altered compared to wild-type, 1.8% of wild-type activity
S475L
-
the mutation probably compromises the active center and results in loss of proteolytic activity
S475L
-
protein processing similar to wild-type, lysosomal localization, no enzymatic activity
V277M
-
the mutation probably compromises the active center and results in loss of proteolytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 5
-
optimal activation occurs in the range pH 3.0-4.0, the proteolytic processing takes place in a wider pH range (2.0-5.0), at pH 3.0 and lower, TPP I is quickly inactivated, whereas the polypeptide generated at higher pH (4.5-5.0) possesses 6- and 13-aa N-terminal extensions and is inactive, the enzyme is unstable at alkaline and neutral pH
678513
3 - 6
-
at pH 3.0 the activity of TPP I is less than 75% of its maximal activity at pH 4.5, most stable at pH 3-4, no activity at pH above 6.0
679200
3.5
-
TPP I is an acidic protease that is quickly inactivated under alkaline pH conditions, in the absence of prosegment, the enzyme is quickly denatured with a rate constant of around 0.107/min, amounting to a half-life of 6.472 min, whereas in the presence of the prosegment, the inactivation rate is reduced to about 0.035/min, and approximately 84% of the activity is preserved after over 2 h of incubation
698756
7.4
-
37°C, half-life: of mature enzyme in absence of heparin is 2.5 min, of mature enzyme in presence of heparin is 21.5 min
665697
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
binding to glycosaminoglycans improves the thermal stability of TPP I
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
butyl-Sepharose 4 column chromatography, Mono Q12 column chromatography, and Superdex 75 gel filtration
-
Ni2+ affinity resin chromatography and heparin agarose affinity chromatography
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
C-terminal hexahistidine-tagged human CLN2p/tripeptidyl-peptidase I produced from insect cells transfected with a baculovirus vector
-
expression as fusion protein with enhanced green fluorescent protein, in Aspergillus oryzae
expression in Chinese hamster ovary cells under the control of the cytomegalovirus promoter
-
expression of mutant enzymes N210Q, N222Q, N286Q, N313Q and N443N in Chinese hamster overy cells and human embryonic kidney 293 cells
-
expression of SedB in Pichia pastoris; expression of SedC in Pichia pastoris; expression of SedD in Pichia pastoris
expression of wild-type and mutant enzymes (E272A, D276A, D327A, D360A and S475L) in CHO cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
molecular biology
-
fluorescent method for the histochemical detection of tripeptidyl peptidase I using glycyl-L-prolyl-L-Met-2-anthraquinonyl hydrazide as substrate
diagnostics
-
saliva is a reliable and non-invasive source for the diagnosis of infantile (CLN1) and late infantile (CLN2) neuronal ceroid lipofuscinoses
medicine
-
adeno-associated virus 2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for late infantile neuronal ceroid lipofuscinosis
medicine
-
[Ala-Ala-Phe]2-rhodamine 110 and [Arg-Nle-Nle]2-rhodamine 110 are specific substrate for determining TPP-I activity and intracellular localization in living cells. These substrates can be a valuable tool for studying the neuronal pathology underlying classical late-infantile neuronal ceroid lipofuscinosis
medicine
-
mutations in tripeptidyl-peptidase I underlie the classic late-infantile form of neuronal ceroid lipofuscinoses (CLN2), the most common neurodegenerative disorders of childhood
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doebber, T.W.; Divor, A.R.; Ellis, S.
Identification of a tripeptidyl aminopeptidase in the anterior pituitary gland: effect on the chemical and biological properties of rat and bovine growth hormones
Endocrinology
103
1794-1804
1978
Bos taurus
brenda
McDonald, J.K.; Hoisington, A.R.; Eisenhauer, D.A.
Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets
Biochem. Biophys. Res. Commun.
126
63-71
1985
Sus scrofa
brenda
Page, A.E.; Fuller, K.; Chambers, T.J.; Warburton, M.J.
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption
Arch. Biochem. Biophys.
306
354-359
1993
Homo sapiens
brenda
Krimper, R.P.; Jones, T.H.
Purification and characterization of tripeptidyl peptidase I from Dictyostelium discoideum
Biochem. Mol. Biol. Int.
47
1079-1088
1999
Dictyostelium discoideum
brenda
Du, P.G.; Kato, S.; Li, Y.H.; Maeda, T.; Yamane, T.; Yamamoto, S.; Fujiwara, M.; Yamamoto, Y.; Nishi, K.; Ohkubo, I.
Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization
Biol. Chem.
382
1715-1725
2001
Rattus norvegicus
brenda
Golabek, A.A.; Kida, E.; Walus, M.; Wujek, P.; Mehta, P.; Wisniewski, K.E.
Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I
J. Biol. Chem.
278
7135-7145
2003
Homo sapiens
brenda
Lin, L.; Sohar, I.; Lackland, H.; Lobel, P.
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH
J. Biol. Chem.
276
2249-2255
2001
Homo sapiens, Homo sapiens (O14773)
brenda
Vines, D.; Warburton, M.J.
Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen
Biochim. Biophys. Acta
1384
233-242
1998
Rattus norvegicus
brenda
Reichard, U.; Lechenne, B.; Asif, A.R.; Streit, F.; Grouzmann, E.; Jousson, O.; Monod, M.
Sedolisins, a new class of secreted proteases from Aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs
Appl. Environ. Microbiol.
72
1739-1748
2006
Aspergillus fumigatus (Q70GH4), Aspergillus fumigatus (Q70J58), Aspergillus fumigatus (Q70J59)
brenda
Kopan, S.; Sivasubramaniam, U.; Warburton, M.J.
The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis
Biochem. Biophys. Res. Commun.
319
58-65
2004
Homo sapiens
brenda
Dikov, A.; Dimitrova, M.; Krieg, R.; Halbhuber, K.
New fluorescent method for the histochemical detection of tripeptidyl peptidase I using glycyl-L-prolyl-L-Met-2-anthraquinonyl hydrazide as substrate
Cell. Mol. Biol.
50
OL565-OL568
2004
Rattus norvegicus
brenda
Sohar, N.; Sohar, I.; Hammer, H.
Lysosomal enzyme activities: new potential markers for Sjoegrens syndrome
Clin. Biochem.
38
1120-1126
2005
Homo sapiens
brenda
Kohan, R.; Noher de Halac, I.; Anzolini, V.T.; Cismondi, A.; Oller Ramirez, A.M.; Capra, A.P.; Dodelson de Kremer, R.
Palmitoyl protein thioesterase 1 (PPT1) and tripeptidyl peptidase-I (TPP-I) are expressed in the human saliva. A reliable and non-invasive source for the diagnosis of infantile (CLN1) and late infantile (CLN2) neuronal ceroid lipofuscinoses
Clin. Biochem.
38
492-494
2005
Homo sapiens
brenda
Walus, M.; Kida, E.; Wisniewski, K.E.; Golabek, A.A.
Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I
FEBS Lett.
579
1383-1388
2005
Homo sapiens, Homo sapiens (O14773)
brenda
Sondhi, D.; Peterson, D.A.; Giannaris, E.L.; Sanders, C.T.; Mendez, B.S.; De, B.; Rostkowski, A.B.; Blanchard, B.; Bjugstad, K.; Sladek, J.R.; Redmond, D.E.; Leopold, P.L.; Kaminsky, S.M.; Hackett, N.R.; Crystal, R.G.
AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL
Gene Ther.
12
1618-1632
2005
Chlorocebus sabaeus
brenda
Steinfeld, R.; Steinke, H.B.; Isbrandt, D.; Kohlschuetter, A.; Gaertner, J.
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes
Hum. Mol. Genet.
13
2483-2491
2004
Homo sapiens
brenda
Oyama, H.; Fujisawa, T.; Suzuki, T.; Dunn, B.M.; Wlodawer, A.; Oda, K.
Catalytic residues and substrate specificity of recombinant human tripeptidyl peptidase I (CLN2)
J. Biochem.
138
127-134
2005
Homo sapiens
brenda
Wujek, P.; Kida, E.; Walus, M.; Wisniewski, K.E.; Golabek, A.A.
N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I
J. Biol. Chem.
279
12827-12839
2004
Homo sapiens
brenda
Golabek, A.A.; Wujek, P.; Walus, M.; Bieler, S.; Soto, C.; Wisniewski, K.E.; Kida, E.
Maturation of human tripeptidyl-peptidase I in vitro
J. Biol. Chem.
279
31058-31067
2004
Homo sapiens
brenda
Golabek, A.A.; Walus, M.; Wisniewski, K.E.; Kida, E.
Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo
J. Biol. Chem.
280
7550-7561
2005
Homo sapiens
brenda
Tian, Y.; Sohar, I.; Taylor, J.W.; Lobel, P.
Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates
J. Biol. Chem.
281
6559-6572
2006
Homo sapiens
brenda
Steinfeld, R.; Fuhrmann, J.C.; Gaertner, J.
Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates
J. Histochem. Cytochem.
54
991-996
2006
Homo sapiens
brenda
Kyttaelae, A.; Lahtinen, U.; Braulke, T.; Hofmann, S.L.
Functional biology of the neuronal ceroid lipofuscinoses (NCL) proteins
Biochim. Biophys. Acta
1762
920-933
2006
Homo sapiens
brenda
Golabek, A.A.; Kida, E.
Tripeptidyl-peptidase I in health and disease
Biol. Chem.
387
1091-1099
2006
Homo sapiens
brenda
Du, P.; An, L.; Qiu, F.; Lu, G.
Peptidase activities of tripeptidyl peptidase I (TPP I): exopeptidase and endopeptidase
Chem. Res. Chin. Univ.
22
65-67
2006
Rattus norvegicus
-
brenda
Guo, X.; Deng, Y.; Lin, Y.; Cosme-Blanco, W.; Chan, S.; He, H.; Yuan, G.; Brown, E.J.; Chang, S.
Dysfunctional telomeres activate an ATM-ATR-dependent DNA damage response to suppress tumorigenesis
EMBO J.
26
4709-4719
2007
Mus musculus
brenda
Schroeder, B.; Elsaesser, H.P.; Schmidt, B.; Hasilik, A.
Characterisation of lipofuscin-like lysosomal inclusion bodies from human placenta
FEBS Lett.
581
102-108
2007
Homo sapiens, Homo sapiens (O14773)
brenda
Leman, A.R.; Polochock, S.; Mole, S.E.; Pearce, D.A.; Rothberg, P.G.
Homogeneous PCR nucleobase quenching assays to detect four mutations that cause neuronal ceroid lipofuscinosis: T75P and R151X in CLN1, and IVS5-1G>C and R208X in CLN2
J. Neurosci. Methods
157
124-131
2006
Homo sapiens
brenda
Qian, M.; Sleat, D.E.; Zheng, H.; Moore, D.; Lobel, P.
Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors
Mol. Cell. Proteomics
7
58-70
2008
Mus musculus
brenda
Bessa, C.; Teixeira, C.A.; Dias, A.; Alves, M.; Rocha, S.; Lacerda, L.; Loureiro, L.; Guimaraes, A.; Ribeiro, M.G.
CLN2/TPP1 deficiency: the novel mutation IVS7-10A>G causes intron retention and is associated with a mild disease phenotype
Mol. Genet. Metab.
93
66-73
2008
Homo sapiens
brenda
Sleat, D.E.; El-Banna, M.; Sohar, I.; Kim, K.H.; Dobrenis, K.; Walkley, S.U.; Lobel, P.
Residual levels of tripeptidyl-peptidase I activity dramatically ameliorate disease in late-infantile neuronal ceroid lipofuscinosis
Mol. Genet. Metab.
94
222-233
2008
Mus musculus
brenda
Cabrera-Salazar, M.A.; Roskelley, E.M.; Bu, J.; Hodges, B.L.; Yew, N.; Dodge, J.C.; Shihabuddin, L.S.; Sohar, I.; Sleat, D.E.; Scheule, R.K.; Davidson, B.L.; Cheng, S.H.; Lobel, P.; Passini, M.A.
Timing of therapeutic intervention determines functional and survival outcomes in a mouse model of late infantile batten disease
Mol. Ther.
15
1782-1788
2007
Homo sapiens, Homo sapiens (O14773)
brenda
Sondhi, D.; Hackett, N.R.; Peterson, D.A.; Stratton, J.; Baad, M.; Travis, K.M.; Wilson, J.M.; Crystal, R.G.
Enhanced survival of the LINCL mouse following CLN2 gene transfer using the rh.10 rhesus macaque-derived adeno-associated virus vector
Mol. Ther.
15
481-491
2007
Homo sapiens
brenda
Chang, M.; Cooper, J.D.; Sleat, D.E.; Cheng, S.H.; Dodge, J.C.; Passini, M.A.; Lobel, P.; Davidson, B.L.
Intraventricular enzyme replacement improves disease phenotypes in a mouse model of late infantile neuronal ceroid lipofuscinosis
Mol. Ther.
16
649-656
2008
Homo sapiens
brenda
Kim, K.H.; Pham, C.T.; Sleat, D.E.; Lobel, P.
Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis
Biochem. J.
415
225-232
2008
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
Ivanov, I.; Tasheva, D.; Todorova, R.; Dimitrova, M.
Synthesis and use of 4-peptidylhydrazido-N-hexyl-1,8-naphthalimides as fluorogenic histochemical substrates for dipeptidyl peptidase IV and tripeptidyl peptidase I
Eur. J. Med. Chem.
44
384-392
2009
Mus musculus, Rattus norvegicus
brenda
Sondhi, D.; Peterson, D.A.; Edelstein, A.M.; del Fierro, K.; Hackett, N.R.; Crystal, R.G.
Survival advantage of neonatal CNS gene transfer for late infantile neuronal ceroid lipofuscinosis
Exp. Neurol.
213
18-27
2008
Mus musculus
brenda
Golabek, A.A.; Dolzhanskaya, N.; Walus, M.; Wisniewski, K.E.; Kida, E.
Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme
J. Biol. Chem.
283
16497-16504
2008
Homo sapiens
brenda
Pal, A.; Kraetzner, R.; Gruene, T.; Grapp, M.; Schreiber, K.; Gronborg, M.; Urlaub, H.; Becker, S.; Asif, A.R.; Gaertner, J.; Sheldrick, G.M.; Steinfeld, R.
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis
J. Biol. Chem.
284
3976-3984
2009
Homo sapiens (O14773)
brenda
Guhaniyogi, J.; Sohar, I.; Das, K.; Stock, A.M.; Lobel, P.
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis
J. Biol. Chem.
284
3985-3997
2009
Homo sapiens, Homo sapiens (O14773)
brenda
Xu, S.; Sleat, D.E.; Jadot, M.; Lobel, P.
Glial fibrillary acidic protein is elevated in the lysosomal storage disease classical late-infantile neuronal ceroid lipofuscinosis, but is not a component of the storage material
Biochem. J.
428
355-362
2010
Mus musculus
brenda
Walus, M.; Kida, E.; Golabek, A.A.
Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I
Hum. Mutat.
31
710-721
2010
Homo sapiens, Homo sapiens (O14773)
brenda
Kim, K.H.; Sleat, D.E.; Bernard, O.; Lobel, P.
Genetic modulation of apoptotic pathways fails to alter disease course in tripeptidyl-peptidase 1 deficient mice
Neurosci. Lett.
453
27-30
2009
Mus musculus
brenda
Atanasova, D.; Lazarov, N.
Histochemical demonstration of tripeptidyl aminopeptidase I in the rat carotid body
Acta Histochem.
117
219-222
2015
Rattus norvegicus
brenda
Zhu, L.; Nemoto, T.; Yoon, J.; Maruyama, J.; Kitamoto, K.
Improved heterologous protein production by a tripeptidyl peptidase gene (AosedD) disruptant of the filamentous fungus Aspergillus oryzae
J. Gen. Appl. Microbiol.
58
199-209
2012
Aspergillus oryzae (Q2U9N2), Aspergillus oryzae ATCC 42149 (Q2U9N2)
brenda
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