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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
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-
?
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-p-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + p-nitroaniline
-
-
-
?
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-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
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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-
-
-
?
additional information
?
-
additional information
?
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-
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
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-
?
additional information
?
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-
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
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?
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0.008 - 20
L-Ala-L-Ala-L-Ala 4-nitroanilide
0.017 - 30
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.013 - 1
L-Ala-L-Ala-L-Phe-p-nitroanilide
0.008 - 0.062
Ala-Ala-Ala-4-nitroanilide
0.017 - 0.1
Ala-Ala-Phe-4-nitroanilide
0.008
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.009
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.01
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.01
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.014
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
0.05
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
0.054
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
0.057
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
0.062
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
0.6
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
1.19
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
3.3
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
20
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
0.017
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.024
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.028
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.037
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.054
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.056
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
0.062
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
0.07
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
0.09
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
0.1
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
0.5
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
0.6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
30
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 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
0.008
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.009
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.01
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.014
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.05
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.05
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.054
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.057
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.062
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.017
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.024
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.028
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
0.037
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.054
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.056
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.062
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.07
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.09
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.1
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.25 - 100
L-Ala-L-Ala-L-Ala 4-nitroanilide
0.38 - 500
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.25 - 33
Ala-Ala-Ala-4-nitroanilide
0.38 - 114
Ala-Ala-Phe-4-nitroanilide
0.25
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.509
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.58
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
0.857
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
1.12
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
4.2
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
11
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
21
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
27
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
30
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
33
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
33
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
100
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
0.38
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
0.441
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
0.86
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
0.9
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
4
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
4
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
18
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
42
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
58.8
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
80
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
96
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
114
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
125
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
500
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
0.25
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.509
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.58
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.857
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
1.12
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
21
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
27
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
30
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
33
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
33
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.38
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.441
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.86
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.9
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.9
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
21
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
42
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
56.8
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
96
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
114
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.4 - 3900
L-Ala-L-Ala-L-Ala 4-nitroanilide
3.82 - 3500
L-Ala-L-Ala-L-Phe 4-nitroanilide
0.000005 - 0.0039
Ala-Ala-Ala-4-nitroanilide
0.0000038 - 0.0035
Ala-Ala-Phe-4-nitroanilide
3.4
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
5
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.4, 37°C
6.7
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
8
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
9
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
9.6
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
10
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 6.8, 37°C
11
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.6, 37°C
14
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 8.3, 37°C
20
L-Ala-L-Ala-L-Ala 4-nitroanilide
mutant H267A, pH 7.9, 37°C
2100
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.4, 37°C
2600
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 8.3, 37°C
2900
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 6.8, 37°C
3800
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.9, 37°C
3900
L-Ala-L-Ala-L-Ala 4-nitroanilide
wild-type, pH 7.6, 37°C
3.82
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.4, 37°C
6
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 8.3, 37°C
7.1
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 8.3, 37°C
10
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.9, 37°C
13
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 6.8, 37°C
15
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.4, 37°C
15
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.9, 37°C
16.5
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant H267A, pH 7.6, 37°C
17
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 6.8, 37°C
20
L-Ala-L-Ala-L-Phe 4-nitroanilide
mutant E331Q, pH 7.6, 37°C
1800
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.4, 37°C
2500
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 8.3, 37°C
2800
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 6.8, 37°C
3100
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.9, 37°C
3500
L-Ala-L-Ala-L-Phe 4-nitroanilide
wild-type, pH 7.6, 37°C
0.000005
Ala-Ala-Ala-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.00001
Ala-Ala-Ala-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.000011
Ala-Ala-Ala-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.000014
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.00002
Ala-Ala-Ala-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.00023
Ala-Ala-Ala-4-nitroanilide
pH 8.3, 37°C
0.0026
Ala-Ala-Ala-4-nitroanilide
pH 7.9, 37°C
0.0029
Ala-Ala-Ala-4-nitroanilide
pH 6.4, 37°C
0.0038
Ala-Ala-Ala-4-nitroanilide
pH 7.6, 37°C
0.0039
Ala-Ala-Ala-4-nitroanilide
pH 6.8, 37°C
0.0000038
Ala-Ala-Phe-4-nitroanilide
pH 6.2, 37°C, mutant H267A
0.000007
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C, mutant H267A
0.00001
Ala-Ala-Phe-4-nitroanilide
pH 7.3, 37°C, mutant H267A
0.000013
Ala-Ala-Phe-4-nitroanilide
pH 6.7, 37°C, mutant H267A
0.0000165
Ala-Ala-Phe-4-nitroanilide
pH 7.0, 37°C, mutant H267A
0.0018
Ala-Ala-Phe-4-nitroanilide
pH 6.4, 37°C
0.0025
Ala-Ala-Phe-4-nitroanilide
pH 8.3, 37°C
0.0028
Ala-Ala-Phe-4-nitroanilide
pH 6.8, 37°C
0.0031
Ala-Ala-Phe-4-nitroanilide
pH 7.9, 37°C
0.0035
Ala-Ala-Phe-4-nitroanilide
pH 7.6, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000011 - 0.14
butabindide
0.001 - 2
L-Val-L-Leu-L-Arg-L-Arg-L-Ala-L-Ser-L-Val-L-Ala
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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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
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
-
it is demonstrated that both, the proteasome and TPPII play a role in the processing of Listeria monocytogenes-derived antigenic peptides
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
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D387G
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
E305K
the mutant shows extremely low activity
E305Q
the mutant shows extremely low activity
E331K
the catalytic efficiency is reduced 20000fold for the E331K variant compared to the wild type enzyme
G375D
less than 0.1% of wild-type activity
H267A
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
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 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
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
additional information
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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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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.; 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
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
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
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
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
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
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
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
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