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(pGlu)LYENKPRRRPYIL + H2O
(pGlu)L + YENKPRRRPYIL
-
i.e. neurotensin, 15.0% degradation after 16 h
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
Ala-Ala-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
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
-
-
-
-
?
angiotensin II + H2O
? + Asp-Arg-Val
-
-
-
-
?
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
-
-
-
-
?
Arg-Pro-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Arg-Pro-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Asp-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Asp-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Cholecystokinin + H2O
?
-
-
-
-
?
DRVYIHPF + H2O
DRV + YIHPF
DRVYIHPFHL + H2O
DRV + YIHPFHL
-
i.e. angiotensin I, 11.3% degradation after 16 h
-
?
GKPIPFFRLK + H2O
GKPIP + FFRLK
-
endo-type substrate, 24.5% degradation after 16 h
-
?
Gly-L-Pro-L-Met-2-anthraquinonyl hydrazide + H2O
Gly-L-Pro-L-Met + 2-anthraquinonyl hydrazine
-
-
-
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
Gly-Lys-Pro-Ile-Pro-Phe-Phe-Arg-Leu-Lys + H2O
Gly-Lys-Pro-Ile-Pro-Phe + Phe-Arg-Leu-Lys
-
-
-
-
?
Gly-Pro-Ala 4-nitroanilide + H2O
Gly-Pro-Ala + 4-nitroaniline
-
at 20% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
-
-
?
Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
at 10% the rate of Gly-Pro-Met 4-methylcoumarin 7-amide hydrolysis
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O
Gly-Pro-Leu + 2-naphthylamine
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
Gly-Pro-Met 4-nitroanilide + H2O
Gly-Pro-Met + 4-nitroaniline
-
-
-
-
?
Gly-Pro-Met-7-amido-4-methylcoumarin + H2O
Gly-Pro-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
GNLWATGHFM-NH2 + H2O
GNL + WATGHFM-NH2
-
i.e. neuromedin B, complete degradation after 16 h
-
?
His-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
His-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
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
-
-
-
-
?
Neuromedin B + H2O
?
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
synthetic peptide modeled after NH2-terminal tripeptide sequence of the phenylalanyl monomer of bovine or rat growth hormone, fluorogenic substrate
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
phenylalanyl monomer of bovine growth hormone + H2O
?
-
cleaves 11 tripeptides sequentially from the NH2-terminus
-
-
?
poly(Gly-Pro-Ala) + H2O
Gly-Pro-Ala
-
-
-
?
RVYIHPF + H2O
RVY + IHPF
-
i.e. angiotensin III, 95.0% degradation after 15 min
-
?
Ser-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ser-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
subunit C of mitochondrial ATP synthase + H2O
?
-
-
-
-
?
synthetic collagen-like polypetides + H2O
Gly-Pro-Xaa tripeptides
-
-
-
?
Val-Pro-Arg 4-nitroanilide + H2O
Val-Pro-Arg + 4-nitroaniline
-
at 11% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
-
-
?
YGGFLRKYP + H2O
YGG + FLRKYP
-
i.e. beta-neo-endorphin, 28% degradation after 16 h
-
?
[Ala-Ala-Phe]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
-
specific substrate for determining TPP-I activity and intracellular localization in living cells
-
-
?
[Arg-Nle-Nle]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
-
specific substrate for determining TPP-I activity and intracellular localization in living cells
-
-
?
glucagon + H2O
additional information
-
Ala-Ala-Ala-4-nitroanilide + H2O

Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O

Ala-Ala-Phe + 4-nitroaniline
SedB
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedC
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedD
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O

Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
33.8% degradation within 60 min
-
-
?
DRVYIHPF + H2O

DRV + YIHPF
-
-
-
?
DRVYIHPF + H2O
DRV + YIHPF
-
i.e. angiotensin II, 18.2% degradation after 16 h
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O

?
-
-
-
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
-
-
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O

Gly-Pro-Leu + 2-naphthylamine
-
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
-
at 30% the rate of Gly-Pro-Met 2-naphthylamide hydrolysis
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O

Gly-Pro-Met + 2-naphthylamine
-
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
-
-
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
-
-
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O

?
-
-
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
glucagon + H2O

additional information
-
-
-
all nine tripeptides and the C-terminal pentapeptide are identified
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no significant aminopeptidase activity
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme removes tripeptides from the free N-termini of small polypeptides and also shows a minor endoprotease activity
-
-
-
additional information
?
-
-
absolute requirement for unsubstituted amino-terminus
-
-
-
additional information
?
-
-
involved in degradation of bone collagen
-
-
-
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
?
-
-
determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
TPP I acts preferentially on small, unstructured oligopeptides of less than 5 kDa
-
-
-
additional information
?
-
-
dipeptidyl-peptidase I cannot functionally compensate for the loss of tripeptidyl-peptidase I
-
-
-
additional information
?
-
-
substrates not cleaved after 24 h of digestion: dynorphin, beta-casomorphin-7, Leu-enkephalin, Met-enkephalin, neurokinin-A, LVV-hemorphin, bradykinin
-
-
-
additional information
?
-
-
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
-
-
-
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
?
-
-
N-terminal exopeptidase that removes tripeptide units provided the P3 residue is unsubstituted
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils
-
-
-
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0.233
Ala-Ala-Phe-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.076 - 0.73
Ala-Ala-Phe-7-amido-4-methylcoumarin
0.0268
Ala-Ala-Phe-p-nitroanilide
-
pH 4.5
0.0148
Ala-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.888
Ala-Ala-Pro-p-nitroanilide
-
pH 4.5
0.00402 - 0.123
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
0.00509
Ala-Asp-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.0422
Ala-His-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.028
Ala-Nle-Leu-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.037
Ala-Nle-Nle-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.03
Ala-Nva-Nle-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.437
Ala-Phe-Pro-p-nitroanilide
-
pH 4.5
0.0483
Ala-Ser-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.0193
Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.054
Arg-Pro-Phe-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.11
Asp-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.45
Gly-Pro-Met 2-naphthylamide
-
-
0.167
His-Ala-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
0.108
Ser-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.076
Ala-Ala-Phe-7-amido-4-methylcoumarin

-
pH 5.0, 37°C, mutant enzyme S475L
0.098
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, wild-type enzyme
0.105
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D276A
0.111
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D360A
0.118
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme E272A
0.164
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D327A
0.188
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 4.5, 30°C
0.68
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 4.0
0.73
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 4.0
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.3
Ala-Ala-Phe-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
0.04 - 41.66
Ala-Ala-Phe-7-amido-4-methylcoumarin
550000
Ala-Ala-Phe-p-nitroanilide
-
pH 4.5
34.5
Ala-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
210000
Ala-Ala-Pro-p-nitroanilide
-
pH 4.5
0.0124 - 11.8
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
11
Ala-Asp-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
26.4
Ala-His-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
3.6
Ala-Nle-Leu-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
4.2
Ala-Nle-Nle-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
4.7
Ala-Nva-Nle-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
140000
Ala-Phe-Pro-p-nitroanilide
-
pH 4.5
30.7
Ala-Ser-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.91
Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
8.2
Arg-Pro-Phe-7-amido-4-carbamoylmethylcoumarin
-
pH 4.5, 30°C
18.5
Asp-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
13.7
His-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
35
Phe-Pro-Ala-4-nitroanilide
pH 6.0, 20°C, SedB
4.7
Ser-Ala-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
0.04 - 1.97
Ala-Ala-Phe-7-amido-4-methylcoumarin

-
pH 5.0, 37°C, mutant enzyme D276A
0.12
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme S475L
1.52
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D360A
1.54
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme E272A
3.22
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, wild-type enzyme
4.22
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D327A
5.2
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 4.5, 30°C
9.36
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D276A
33.1
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 4.0
41.66
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, wild-type enzyme
0.0124
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu

-
pH 4.0, 378°C, mutant enzyme E77A
11.8
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
-
pH 4.0, 37°C, wild-type enzyme
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D276A
-
kcat/Km is 21% of the wild-type value
D327A
-
kcat/Km is 6% of the wild-type value
D517A
-
lack of enzyme activity and processing
D81A
-
not expressed in Sf9 cells
E272A
-
kcat/Km is 3% of the wild-type value
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
E343L
-
decreased activity
E77A
-
very low activity with Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu
G473R
-
the mutation probably compromises the active center and results in loss of proteolytic activity
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
Q248P
-
the mutation probably compromises the active center and results in loss of proteolytic activity
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
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
S475
-
inactive mutant enzyme
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
C365R

-
decreased activity
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
D360A

-
lack of enzyme activity and processing
D360A
-
kcat/Km is 3% of the wild-type value
G284V

-
decreased 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

-
decreased 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
-
decreased activity
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
-
decreased activity
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

-
decreased 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
Q422H
-
decreased activity
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

-
decreased 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

-
decreased 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

-
kcat/Km is 0.4% of the wild-type value
S475L
-
decreased activity; inactive
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

-
decreased activity
V277M
-
the mutation probably compromises the active center and results in loss of proteolytic activity
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