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Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Gln-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
?
KKE-5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid-Q9K-4'-dimethylaminoazobenzene-4'-sulfonyl + H2O
?
-
-
-
?
Q20RRGRR + H2O
Q17RRGRR + Q14RRGRR + QQQ
little activity
-
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe 2-naphthylamide + H2O
Ala-Ala-Phe + 2-naphthylamine
-
at 41% the rate of Ala-Ala-Phe 7-amido-4-methylcoumarin
-
?
Ala-Ala-Phe 7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
best chromogenic tripeptyl substrate
-
?
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-p-nitroanilide + H2O
Ala-Ala-Phe + p-nitroaniline
-
-
-
-
?
angiotensin III + H2O
?
-
-
-
-
?
Arg-Ala-(dehydro)Ala-Val-Ala + H2O
?
-
inhibitor, at 0.05% the rate of Arg-Arg-Ala-(phospho)Ser-Val-Ala hydrolysis
-
-
?
Arg-Ala-Ser-Val-Ala + H2O
Arg-Ala-Ser + Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
cholecystokinin octapeptide fragment + H2O
?
-
-
-
-
?
His-Leu-His 2-naphthylamide + H2O
His-Leu-His + 2-naphthylamine
-
at 12% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
L-Ala-L-Ala-L-Phe 4-nitroanilide + H2O
L-Ala-L-Ala-L-Phe + 4-nitroaniline
-
both the KM and kcat are lower for cleavage of L-Ala-L-Ala-L-Ala 4-nitroanilide than for L-Ala-L-Ala-L-Phe 4-nitroanilide, the former possibly can bind non-productively to the active site of the enzyme
-
-
?
neurokinin + H2O
?
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
at 6% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Leu-Glu-Arg + H2O
Val-Gly-Ala + His-Ala-Gly + Glu-Tyr-Gly + Ala-Glu-Ala + Leu-Glu-Arg
-
peptide derived from human hemoglobin alpha-chain, residues 17-31, sequential release of tripeptides from free N-terminus, cleaved into 5 tripeptides by human enzyme, cleavage of Gly25-Ala bond occurs at a lower rate than Ala19-His and Gly22-Glu
-
?
Val-Leu-Arg-Arg-Ala-Ser-Val-Ala + H2O
Val-Leu-Arg + Arg-Ala-Ser-Val-Ala
-
-
the latter product is cleaved at a higher rate than the substrate
?
Val-Tyr-Ser 2-naphthylamide + H2O
Val-Tyr-Ser + 2-naphthylamine
-
at 3% the rate of Ala-Ala-Phe 4-methylcoumarin 7-amide
-
?
additional information
?
-
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
?
Arg-Arg-Ala-(phospho)Ser-Val-Ala + H2O
Arg-Arg-Ala + (phospho)Ser-Val-Ala
-
-
-
-
?
additional information
?
-
the enzyme is important in inactivating extracellular cholecystokinin
-
-
?
additional information
?
-
no activity against Q20RRGRR and KKQ30KK
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Phe 4-methylcoumarin 7-amide, aminoacyl or dipeptidyl methylcoumarylamides
-
-
?
additional information
?
-
-
no substrate: Pro-Lys-Ala 2-naphthylamide
-
-
?
additional information
?
-
-
no substrates are peptides with proline residues around cleavage sites
-
-
?
additional information
?
-
-
association/dissociation may be a way of regulating the enzyme activity in vivo
-
-
?
additional information
?
-
-
the enzyme is important for the degradation of some specific substrates, e.g. the neuropeptide cholecystokinin. It is likely that the main biological function of tripeptidyl-peptidase II is to participate in a general intracellular protein turnover. This peptidase may act on oligopeptides generated by the proteasome, or other endopeptidases, and the tripeptides formed would subsequently be good substrates for other exopeptidases. Tripeptidyl-peptidase II activity is increased in sepsis-induced muscle wasting, a situation of enhanced protein turnover
-
-
?
additional information
?
-
-
TPPII plays an important role in antigen processing, as most proteasomal products require further processing by TPPII for MHC class I presentation. As a consequence, peptide generation for MHCclass I is severely hampered when TPPII activitis inhibited
-
-
?
additional information
?
-
-
tripeptidyl peptidase II plays a role in cross-presentation of CTL epitopes restricted to diverse HLA alleles
-
-
?
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Bone Resorption
Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen.
Bone Resorption
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption.
Burkitt Lymphoma
Down-regulation of proteolytic complexes following EBV activation in BL cells.
Burkitt Lymphoma
Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II.
Burkitt Lymphoma
The MAPK Signaling Cascade is a Central Hub in the Regulation of Cell Cycle, Apoptosis and Cytoskeleton Remodeling by Tripeptidyl-Peptidase II.
Neoplasms
Development, evaluation and application of tripeptidyl-peptidase II sequence signatures.
Neoplasms
Effect of cancer cachexia on the activity of tripeptidyl-peptidase II in skeletal muscle.
Neoplasms
MAP kinase-signaling controls nuclear translocation of tripeptidyl-peptidase II in response to DNA damage and oxidative stress.
Neoplasms
Retraction: Tripeptidyl-peptidase II controls DNA damage responses and in vivo ?-irradiation resistance of tumors. Cancer Research 2007;67:716574.
Neoplasms
Schizophrenia Susceptibility Genes Directly Implicated in the Life Cycles of Pathogens: Cytomegalovirus, Influenza, Herpes simplex, Rubella, and Toxoplasma gondii.
Neoplasms
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors.
Neurodegenerative Diseases
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis.
Neuronal Ceroid-Lipofuscinoses
Tandem mass spectrometry assays of palmitoyl protein thioesterase 1 and tripeptidyl peptidase activity in dried blood spots for the detection of neuronal ceroid lipofuscinoses in newborns.
Neuronal Ceroid-Lipofuscinoses
Therapeutic landscape for Batten disease: current treatments and future prospects.
Sepsis
Tripeptidyl-peptidase II expression and activity are increased in skeletal muscle during sepsis.
tripeptidyl-peptidase ii deficiency
Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with tripeptidyl-peptidase II deficiency.
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Tomkinson, B.; Wernstedt, C.; Hellman, U.; Zetterquist, .
Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type
Proc. Natl. Acad. Sci. USA
84
7508-7512
1987
Homo sapiens
brenda
Balw, R.M.; Tomkinson, B.; Ragnarsson, U.; Zetterquist, .
Purification, substrate specificity, and classification of tripeptidyl peptidase II
J. Biol. Chem.
261
2409-2417
1986
Homo sapiens, Rattus norvegicus
brenda
Macpherson, E.; Tomkinson, B.; Balw, R.M.; Hglund, S.; Zetterquist, .
Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity
Biochem. J.
248
259-263
1987
Homo sapiens
brenda
Balw, R.M.; Eriksson, I.
Tripeptidyl peptidase II in haemolysates and liver homogenates of various species
Biochem. J.
241
75-80
1987
Bos taurus, Equus caballus, Gallus gallus, Homo sapiens, no activity in Escherichia coli, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, Sus scrofa
brenda
Tomkinson, B.; Zetterquist, .
Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin
Biochem. J.
267
149-154
1990
Homo sapiens
brenda
Tomkinson, B.; Grehn, L.; Fransson, B.; Zetterquist, ?.
Use of a dehydroalanine-containing peptide as an efficient inhibitor of tripeptidyl peptidase II
Arch. Biochem. Biophys.
314
276-279
1994
Homo sapiens
brenda
Matrinsson, T.; Vujic, M.; Tomkinson, B.
Localization of the human tripeptidyl peptidase II gene (TPP2) to 13q32-q33 by nonradioactive in situ hybridization and somatic cell hybrids
Genomics
17
493-495
1993
Homo sapiens
brenda
Wilson, C.; Gibosn, A.M.; McDermott, J.R.
Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain
Neurochem. Res.
18
743-749
1993
Homo sapiens
brenda
Tomkinson, B.
Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II
Biomed. Biochim. Acta
50
727-729
1991
Homo sapiens
brenda
Harris, J.; Tomkinson, B.
Electron microscopical and biochemical studies on the oligomeric states of human erythrocyte tripeptidyl peptidase-II
Micron Microsc. Acta
21
77-89
1990
Homo sapiens
-
brenda
Tomkinson, B.
Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity
Arch. Biochem. Biophys.
376
275-280
2000
Homo sapiens
brenda
Tomkinson, B.; Ni Laoi, B.; Wellington, K.
The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex
Eur. J. Biochem.
269
1438-1443
2002
Homo sapiens, Mus musculus
brenda
Hilbi, H.; Jozsa, E.; Tomkinson, B.
Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis
Biochim. Biophys. Acta
1601
149-154
2002
Homo sapiens
brenda
Radu, D.; Tomkinson, B.; Zachrisson, O.; Weber, G.; de Belleroche, J.; Hirsch, S.; Lindefors, N.
Overlapping regional distribution of CCK and TPPII mRNAs in Cynomolgus monkey brain and correlated levels in human cerebral cortex (BA 10)
Brain Res.
1104
175-182
2006
Homo sapiens (P29144), Macaca fascicularis, Rattus norvegicus
brenda
Lindas, A.C.; Tomkinson, B.
Identification and characterization of the promoter for the gene encoding human tripeptidyl-peptidase II
Gene
345
249-257
2005
Homo sapiens
brenda
Reits, E.; Neijssen, J.; Herberts, C.; Benckhuijsen, W.; Janssen, L.; Drijfhout, J.W.; Neefjes, J.
A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
Immunity
20
495-506
2004
Homo sapiens
brenda
Tomkinson, B.; Lindas, A.C.
Tripeptidyl-peptidase II: a multi-purpose peptidase
Int. J. Biochem. Cell Biol.
37
1933-1937
2005
Homo sapiens
brenda
Naujokat, C.; Fuchs, D.; Berges, C.
Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition
Biochim. Biophys. Acta
1773
1389-1397
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Levengood, M.R.; van der Donk, W.A.
Use of lantibiotic synthetases for the preparation of bioactive constrained peptides
Bioorg. Med. Chem. Lett.
18
3025-3028
2008
Homo sapiens
brenda
Hong, X.; Lei, L.; Kuenert, B.; Naredla, R.; Applequist, S.E.; Grandien, A.; Glas, R.
Tripeptidyl-peptidase II controls DNA damage responses and in vivo gamma-irradiation resistance of tumors
Cancer Res.
67
7165-7174
2007
Homo sapiens
brenda
Bhutani, N.; Venkatraman, P.; Goldberg, A.L.
Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
EMBO J.
26
1385-1396
2007
Homo sapiens (P29144)
brenda
Basler, M.; Groettrup, M.
No essential role for tripeptidyl peptidase II for the processing of LCMV-derived T cell epitopes
Eur. J. Immunol.
37
896-904
2007
Homo sapiens
brenda
Endert, P.
Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?
Eur. J. Immunol.
38
609-613
2008
Homo sapiens
brenda
Marcilla, M.; Villasevil, E.M.; de Castro, J.A.
Tripeptidyl peptidase II is dispensable for the generation of both proteasome-dependent and proteasome-independent ligands of HLA-B27 and other class I molecules
Eur. J. Immunol.
38
631-639
2008
Homo sapiens
brenda
Lindas, A.C.; Tomkinson, B.
Characterization of the promoter of the gene encoding human tripeptidyl-peptidase II and identification of upstream silencer elements
Gene
393
62-69
2007
Homo sapiens
brenda
Preuss, K.D.; Held, G.; Kubuschok, B.; Hung, C.Z.; Malatsidze, N.; Wagner, M.; Pfreundschuh, M.
Identification of antigenic targets of paraproteins by expression cloning does not support a causal role of chronic antigenic stimulation in the pathogenesis of multiple myeloma and MGUS
Int. J. Cancer
121
459-461
2007
Homo sapiens
brenda
Guil, S.; Rodriguez-Castro, M.; Aguilar, F.; Villasevil, E.M.; Anton, L.C.; Del Val, M.
Need for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental
J. Biol. Chem.
281
39925-39934
2006
Homo sapiens
brenda
Anton, L.C.; Villasevil, E.M.
Is there an alternative to the proteasome in cytosolic protein degradation?
Biochem. Soc. Trans.
36
839-842
2008
Homo sapiens
brenda
Schnurr, M.; Orban, M.; Robson, N.C.; Shin, A.; Braley, H.; Airey, D.; Cebon, J.; Maraskovsky, E.; Endres, S.
ISCOMATRIX adjuvant induces efficient cross-presentation of tumor antigen by dendritic cells via rapid cytosolic antigen delivery and processing via tripeptidyl peptidase II
J. Immunol.
182
1253-1259
2009
Homo sapiens
brenda
Nahalkova, J.; Tomkinson, B.
TPPII, MYBBP1A and CDK2 form a protein-protein interaction network
Arch. Biochem. Biophys.
564
128-135
2014
Homo sapiens
brenda
Eklund, S.; Lindas, A.C.; Hamnevik, E.; Widersten, M.; Tomkinson, B.
Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics
Biochim. Biophys. Acta
1824
561-570
2012
Drosophila melanogaster, Drosophila melanogaster (Q9V6K1), Homo sapiens, Mus musculus, Mus musculus (Q64514)
brenda
Usukura, K.; Kasamatsu, A.; Okamoto, A.; Kouzu, Y.; Higo, M.; Koike, H.; Sakamoto, Y.; Ogawara, K.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Tripeptidyl peptidase II in human oral squamous cell carcinoma
J. Cancer Res. Clin. Oncol.
139
123-130
2013
Homo sapiens, Homo sapiens (P29144)
brenda
Schoenegge, A.M.; Villa, E.; Foerster, F.; Hegerl, R.; Peters, J.; Baumeister, W.; Rockel, B.
The structure of human tripeptidyl peptidase II as determined by a hybrid approach
Structure
20
593-603
2012
Homo sapiens (P29144), Homo sapiens
brenda
Wiemhoefer, A.; Stargardt, A.; van der Linden, W.A.; Renner, M.C.; van Kesteren, R.E.; Stap, J.; Raspe, M.A.; Tomkinson, B.; Kessels, H.W.; Ovaa, H.; Overkleeft, H.S.; Florea, B.; Reits, E.A.
Tripeptidyl peptidase II mediates levels of nuclear phosphorylated ERK1 and ERK2
Mol. Cell. Proteomics
14
2177-2193
2015
Homo sapiens (P29144)
brenda