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(Gln)17-Arg-Arg-Gly-Arg-Arg + H2O
(Gln)14-Arg-Arg-Gly-Arg-Arg + Gln-Gln-Gln
-
little activity
-
-
?
(Gln)20-Arg-Arg-Gly-Arg-Arg + H2O
(Gln)17-Arg-Arg-Gly-Arg-Arg + Gln-Gln-Gln
-
little activity
-
-
?
Ala-Ala-Ala + H2O
Ala + Ala-Ala
26% of the activity with Met-Gly-Gly
-
?
Ala-Ala-Phe-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Ala-Ala-Phe-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
-
-
-
?
Ala-Phe-Pro-beta-naphthylamide + H2O
Ala-Phe-Pro + beta-naphthylamine
angiotensin II + H2O
?
-
-
-
-
?
angiotensin III + H2O
?
-
-
-
-
?
Arg-Ala-Arg + H2O
Arg + Ala-Arg
-
-
-
-
?
Arg-Ser-Arg + H2O
Arg + Ser-Arg
-
-
-
-
?
casein + H2O
?
-
assay at pH 8.0, 37°C
-
-
?
cholecystokinin octapeptide + H2O
?
-
-
-
-
?
des-Tyr-dynorphin A1-8 + H2O
?
-
-
-
-
?
enkephalin + H2O
?
-
-
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + Gly
-
assay at pH 8.0, 37°C
-
-
?
Gly-Ala-Pro-beta-naphthylamide + H2O
Gly-Ala-Pro + beta-naphthylamine
Gly-Gly-Gly + H2O
Gly + Gly-Gly
Gly-Gly-Phe + H2O
Gly + Gly-Phe
Gly-Leu-Tyr + H2O
Gly + Leu-Tyr
L-Ala-Gly-Gly + H2O
L-Ala + Gly-Gly
-
-
-
-
?
L-Ala-L-Ala-D-Ala + H2O
L-Ala + L-Ala-D-Ala
-
-
-
-
?
L-Ala-L-Ala-L-Ala + H2O
L-Ala + L-Ala-L-Ala
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Ala-L-Ala-L-Phe
-
assay at pH 8.0, 37°C
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Asp
-
assay at pH 8.0, 37°C
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gln
-
assay at pH 8.0, 37°C
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
assay at pH 8.0, 37°C
-
-
?
L-Lys-4-nitroanilide + H2O
4-nitroaniline + L-Lys
-
assay at pH 8.0, 37°C
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Met
-
assay at pH 8.0, 37°C
-
-
?
L-Met-L-Met-L-Met + H2O
L-Met + L-Met-L-Met
L-Phe-Gly-Gly + H2O
L-Phe + Gly-Gly
L-Pro-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Pro
-
assay at pH 8.0, 37°C
-
-
?
L-Pro-Gly-Gly + H2O
L-Pro + Gly-Gly
-
-
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Thr
-
assay at pH 8.0, 37°C
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Trp
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Tyr
-
assay at pH 8.0, 37°C
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
Leu-Leu-Ala + H2O
Leu + Leu-Ala
33% of the activity with Met-Gly-Gly
-
?
Leu-Leu-Leu + H2O
Leu + Leu-Leu
15% of the activity with Met-Gly-Gly
-
?
Lys-Gly-Gly + H2O
Lys + Gly-Gly
13% of the activity with Met-Gly-Gly
-
?
Met-Ala-Ser + H2O
?
-
-
-
-
?
Met-Ala-Ser + H2O
Met + Ala-Ser
-
-
-
?
Met-Gly-Gly + H2O
Met + Gly-Gly
microcin C + H2O
?
-
microcin C is processed to a nonhydrolyzable analog of aspartyl-adenylate
-
-
?
neurokinin alpha + H2O
?
-
-
-
-
?
oxidized insulin B chain + H2O
?
-
assay at pH 8.0, 37°C
-
-
?
Ser-Ser-Ser + H2O
?
-
-
-
-
?
tripeptides + H2O
?
-
e.g. Met-Leu-Tyr: chemotactic factor, Gly-His-Lys: liver growth factor, slow hydrolysis
-
-
?
Tyr-Gly-Gly + H2O
Tyr + Gly-Gly
11% of the activity with Met-Gly-Gly
-
?
additional information
?
-
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Phe-Pro-beta-naphthylamide + H2O
Ala-Phe-Pro + beta-naphthylamine
-
-
-
-
?
Ala-Phe-Pro-beta-naphthylamide + H2O
Ala-Phe-Pro + beta-naphthylamine
-
-
-
-
?
Gly-Ala-Pro-beta-naphthylamide + H2O
Gly-Ala-Pro + beta-naphthylamine
-
-
-
-
?
Gly-Ala-Pro-beta-naphthylamide + H2O
Gly-Ala-Pro + beta-naphthylamine
-
-
-
-
?
Gly-Gly-Gly + H2O
Gly + Gly-Gly
-
-
-
-
?
Gly-Gly-Gly + H2O
Gly + Gly-Gly
-
-
-
-
?
Gly-Gly-Phe + H2O
Gly + Gly-Phe
-
-
-
?
Gly-Gly-Phe + H2O
Gly + Gly-Phe
-
-
-
-
?
Gly-Leu-Tyr + H2O
Gly + Leu-Tyr
-
-
-
-
?
Gly-Leu-Tyr + H2O
Gly + Leu-Tyr
15% of the activity with Met-Gly-Gly
-
?
L-Ala-L-Ala-L-Ala + H2O
L-Ala + L-Ala-L-Ala
-
-
-
-
?
L-Ala-L-Ala-L-Ala + H2O
L-Ala + L-Ala-L-Ala
-
-
-
-
?
L-Ala-L-Ala-L-Ala + H2O
L-Ala + L-Ala-L-Ala
-
-
-
-
?
L-Met-L-Met-L-Met + H2O
L-Met + L-Met-L-Met
-
-
-
?
L-Met-L-Met-L-Met + H2O
L-Met + L-Met-L-Met
-
-
-
-
?
L-Phe-Gly-Gly + H2O
L-Phe + Gly-Gly
-
-
-
?
L-Phe-Gly-Gly + H2O
L-Phe + Gly-Gly
-
-
-
-
?
L-Phe-Gly-Gly + H2O
L-Phe + Gly-Gly
-
-
-
-
?
L-Phe-Gly-Gly + H2O
L-Phe + Gly-Gly
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Pro and Ala
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
D-Leu
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
34% of the activity with Met-Gly-Gly
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Phe
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Tyr
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Ala, Phe, Gly-Pro
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Phe and Trp
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Ala, Phe, Gly-Pro
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Tyr
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Leu can be replaced by Ala, Phe, Gly-Pro
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
Hyp, Thr, His
-
?
Met-Gly-Gly + H2O
Met + Gly-Gly
-
-
-
-
?
Met-Gly-Gly + H2O
Met + Gly-Gly
-
-
-
-
?
Met-Gly-Gly + H2O
Met + Gly-Gly
-
-
?
additional information
?
-
-
the enzyme digests peptide products of the 26S proteasome and other endopeptidases into tripeptides
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no digestion is observed against Lys-Lys-(Gln)30-Lys-Lys
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity with Gly-Pro-beta-naphthylamide, Z-Gly-Pro-beta-naphthylamide, Z-Gly-Ala-Pro-beta-naphthylamide, Z-Ala-Gly-Pro-beta-naphthylamide, Gly-Ala-Gly-Pro-beta-naphthylamide, Z-Gly-Ala-Gly-Pro-beta-naphthylamide, and Ala-Gly-Ala-Gly-Pro-beta-naphthylamide
-
-
?
additional information
?
-
-
-
-
-
?
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Alzheimer Disease
Comparison of aminopeptidase, dipeptidyl aminopeptidase and tripeptidyl aminopeptidase activities in brain tissue from normal and Alzheimer's disease cases.
Anaphylaxis
[Determination of the dipeptidase and tripeptidase activity in anaphylactoid shock.]
Arthritis, Rheumatoid
Effects of intra-articular hydrocortisone acetate on the clinical course, aminotripeptidase activity and other changes in the synovial fluid in rheumatoid arthritis.
Atherosclerosis
[The changes in the activity of tripeptidyl peptidase II in experimental atherosclerosis and hypertension].
Autoimmune Diseases
Examination of the subcellular distribution of tripeptide aminopeptidase and evaluation of its clinical usefulness in human serum.
Breast Neoplasms
A role for nuclear translocation of tripeptidyl-peptidase II in reactive oxygen species-dependent DNA damage responses.
Burkitt Lymphoma
Tripeptidyl Peptidase II Is Required for c-MYC-Induced Centriole Overduplication and a Novel Therapeutic Target in c-MYC-Associated Neoplasms.
Carcinogenesis
Linking TPPII to the protein interaction and signalling networks.
Carcinogenesis
The protein-interaction network with functional roles in tumorigenesis, neurodegeneration, and aging.
Carcinoma
Tripeptidyl peptidase II in human oral squamous cell carcinoma.
Carcinoma, Hepatocellular
Clinical usefulness of serum tripeptide aminopeptidase activity in diagnosing liver diseases.
Colonic Neoplasms
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.
Coxsackievirus Infections
Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells.
Hepatitis B
Adenovirus Vector Harboring the HBcAg and Tripeptidyl Peptidase II Genes Induces Potent Cellular Immune Responses In Vivo.
Hypercholesterolemia
[The changes in the activity of tripeptidyl peptidase II in experimental atherosclerosis and hypertension].
Hypertension
[The changes in the activity of tripeptidyl peptidase II in experimental atherosclerosis and hypertension].
Leukemia
Examination of the subcellular distribution of tripeptide aminopeptidase and evaluation of its clinical usefulness in human serum.
Liver Diseases
Clinical usefulness of serum tripeptide aminopeptidase activity in diagnosing liver diseases.
Lung Neoplasms
Linking TPPII to the protein interaction and signalling networks.
Lymphocytic Choriomeningitis
Analysis of the Role of Tripeptidyl Peptidase II in MHC Class I Antigen Presentation In Vivo.
Lymphocytic Choriomeningitis
No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes.
Lymphoma
A role for nuclear translocation of tripeptidyl-peptidase II in reactive oxygen species-dependent DNA damage responses.
Lymphoma
Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice.
Lymphoma
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors.
Lysosomal Storage Diseases
Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.
Melanoma
A role for nuclear translocation of tripeptidyl-peptidase II in reactive oxygen species-dependent DNA damage responses.
Melanoma
MAP kinase-signaling controls nuclear translocation of tripeptidyl-peptidase II in response to DNA damage and oxidative stress.
Myocardial Infarction
[Tripeptidase activity in the blood serum in the course of myocardial infarct.]
Neoplasms
Distribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions.
Neoplasms
Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle.
Neoplasms
ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II.
Neoplasms
MAP kinase-signaling controls nuclear translocation of tripeptidyl-peptidase II in response to DNA damage and oxidative stress.
Neoplasms
TPPII, MYBBP1A and CDK2 form a protein-protein interaction network.
Neoplasms
Tripeptidyl Peptidase II Is Required for c-MYC-Induced Centriole Overduplication and a Novel Therapeutic Target in c-MYC-Associated Neoplasms.
Neoplasms
Tripeptidyl peptidase II plays a role in the radiation response of selected primary cell types but not based on nuclear translocation and p53 stabilization.
Neoplasms
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors.
Neoplasms
Tumors acquire inhibitor of apoptosis protein (IAP)-mediated apoptosis resistance through altered specificity of cytosolic proteolysis.
Neoplasms
Viability and DNA damage responses of TPPII-deficient Myc- and Ras-transformed fibroblasts.
Neoplasms
[Aldolase, dipeptidase, tripeptidase, tributyrinase, phosphatase, amylase, proteins and protein polysaccharides in the blood serum and ascites fluid in the mouse ascites tumor.]
Neurodegenerative Diseases
Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.
Neurodegenerative Diseases
[Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation]
Neuronal Ceroid-Lipofuscinoses
Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.
Neuronal Ceroid-Lipofuscinoses
Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.
Neuronal Ceroid-Lipofuscinoses
N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.
Neuronal Ceroid-Lipofuscinoses
Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.
Neuronal Ceroid-Lipofuscinoses
Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.
Neuronal Ceroid-Lipofuscinoses
[Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation]
Renal Insufficiency
[Tripeptidase activity of plasma during renal insufficiency; contribution to the study of protein catabolism.]
Renal Insufficiency, Chronic
[Serum tripeptidase activity in acute and chronic renal insufficiency (author's transl)]
Rheumatic Fever
[Observation of serum aminotripeptidase activity in rheumatic fever]
Sarcoma
A role for nuclear translocation of tripeptidyl-peptidase II in reactive oxygen species-dependent DNA damage responses.
Sepsis
Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis.
Squamous Cell Carcinoma of Head and Neck
Tripeptidyl peptidase II in human oral squamous cell carcinoma.
tripeptide aminopeptidase deficiency
Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice.
Uveitis
[On the peptidase activity of the aqueous humor in the course of experimental anaphylactic uveitis (aminodipeptidase and aminotripeptidase activities).]
Vaccinia
Analysis of the Role of Tripeptidyl Peptidase II in MHC Class I Antigen Presentation In Vivo.
Virus Diseases
Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells.
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0.04 - 41.66
Ala-Ala-Phe-7-amido-4-methylcoumarin
6.8 - 511
Ala-Phe-Pro-beta-naphthylamide
5.3
Arg-Ala-Arg
-
calculated value, wild type enzyme
0.56
Arg-Ser-Arg
-
calculated value, wild type enzyme
12
Gly-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
265 - 354
Gly-Ala-Pro-beta-naphthylamide
14.4
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
11.7
L-Asp-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
19
L-Leu-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
14.3
L-Lys-4-nitroanilide
-
pH 8.0, 37°C
14
L-Met-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
additional information
additional information
-
-
-
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 S475A
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
9.36
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, mutant enzyme D276A
41.66
Ala-Ala-Phe-7-amido-4-methylcoumarin
-
pH 5.0, 37°C, wild-type enzyme
6.8
Ala-Phe-Pro-beta-naphthylamide
-
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0) at 37°C
511
Ala-Phe-Pro-beta-naphthylamide
-
wild type enzyme, in 20 mM Tris-HCl (pH 7.0) at 37°C
265
Gly-Ala-Pro-beta-naphthylamide
-
mutant enzyme E636A, in 20 mM Tris-HCl (pH 7.0) at 37°C
354
Gly-Ala-Pro-beta-naphthylamide
-
in 20 mM Tris-HCl buffer (pH 7.0), at 37°C
354
Gly-Ala-Pro-beta-naphthylamide
-
wild type enzyme, in 20 mM Tris-HCl (pH 7.0) at 37°C
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Morgan, J.G.; Donlon, J.
Kinetics of inhibition of guinea-pig intestinal aminotripeptidases
Biochem. Soc. Trans.
14
458-459
1986
Cavia porcellus
-
brenda
Morgan, J.G.; Donlan, J.
Purification and characterization of two aminopeptidases from guinea-pig small-intestinal mucosa. Cavian intestinal tripeptide hydrolases
Eur. J. Biochem.
146
429-435
1985
Cavia porcellus
brenda
Frick, L.; Wolfenden, R.
Mechanistic implications of the inhibition of peptidases by amino aldehydes and bestatin
Biochim. Biophys. Acta
829
311-318
1985
Rattus norvegicus
brenda
Sachs, L.; Marks, N.
A highly specific aminotripeptidase of rat brain cytosol. Substrate specificity and effects of inhibitors
Biochim. Biophys. Acta
706
229-238
1982
Rattus norvegicus
brenda
Parker, D.D.; Naider, F.; Becker, J.M.
Separation of peptide transport and hydrolysis in trimethionine uptake by Saccharomyces cerevisiae
J. Bacteriol.
143
1066-1069
1980
Saccharomyces cerevisiae
brenda
Hayashi, M.; Oshima, K.
Isolation and characterization of aminotripeptidase from monkey brain
J. Biochem.
87
1403-1411
1980
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